Journal articles: 'DCCD'

1

Matsumura, K., F. J. Lovas, and R. D. Suenram. "Fourier-transform microwave spectroscopy of the deuterated acetylene dimers: The interconversion tunneling motions of (DCCD)2, (DCCH)2, DCCDDCCH, DCCHDCCD, HCCHDCCD, and HCCHDCCH." Journal of Molecular Spectroscopy 150, no. 2 (December 1991): 576–96. http://dx.doi.org/10.1016/0022-2852(91)90250-e.

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2

MATSUMURA, K., F. J. LOVAS, and R. D. SUENRAM. "ChemInform Abstract: Fourier-Transform Microwave Spectroscopy of the Deuterated Acetylene Dimers: The Interconversion Tunneling Motions of (DCCD)2, (DCCH)2, DCCD-DCCH, DCCH-DCCD, HCCH-DCCD, and HCCH-DCCH." ChemInform 23, no. 9 (August 22, 2010): no. http://dx.doi.org/10.1002/chin.199209034.

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Dhyanti, Yustina, Khairul Munadi, and Fitri Arnia. "Penerapan Deskriptor Warna Dominan untuk Temu Kembali Citra Busana pada Peranti Bergerak." Jurnal Rekayasa Elektrika 12, no. 3 (December 15, 2016): 104. http://dx.doi.org/10.17529/jre.v12i3.5701.

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Nowadays, clothes with various designs and color combinations are available for purchasing through an online shop, which is mostly equipped with keyword-based item retrieval. Here, the object in the online database is retrieved based on the keyword inputted by the potential buyers. The keyword-based search may bring potential customers on difficulties to describe the clothes they want to buy. This paper presents a new searching approach, using an image instead of text, as the query into an online shop. This method is known as content-based image retrieval (CBIR). Particularly, we focused on using color as the feature in our Muslimah clothes image retrieval. The dominant color descriptor (DCD) extracts the wardrobe's color. Then, image matching is accomplished by calculating the Euclidean distance between the query and image in the database, and the last step is to evaluate the performance of the DWD by calculating precision and recall. To determine the performance of the DCD in extracting color features, the DCD is compared with another color descriptor, that is dominant color correlogram descriptor (DCCD). The values of precision and recall of DCD ranged from 0.7 to 0.9 while the precision and recall of DCCD ranged from 0.7 to 0.8. These results showed that the DCD produce a superior performance compared to DCCD in retrieving a set of clothing image, either plain or patterned colored clothes.

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Vuokila, P. T., and I. E. Hassinen. "NN′-dicyclohexylcarbodi-imide-sensitivity of bovine heart mitochondrial NADH: ubiquinone oxidoreductase. Inhibition of activity and binding to subunits." Biochemical Journal 249, no. 2 (January 15, 1988): 339–44. http://dx.doi.org/10.1042/bj2490339.

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Dicyclohexylcarbodi-imide (DCCD) inhibition of NADH: ubiquinone oxidoreductase was studied in submitochondrial particles and in the isolated form, together with the binding of the reagent to the enzyme. DCCD inhibited the isolated enzyme in a time- and concentration-dependent manner. Over the concentration range studied, a maximum inhibition of 85% was attained within 60 min. The time course for the binding of DCCD to the enzyme was similar to that of activity inhibition. The NADH:ubiquinone oxidoreductase activity of the submitochondrial particles was also sensitive to DCCD, and the locus of binding of the inhibitor was studied by subsequent resolution of the enzyme into subunit polypeptides. Only two subunits (molecular masses 13.7 and 21.5 kDa) were labelled by [14C]DCCD, whereas, when the enzyme in its isolated form was treated with [14C]DCCD, six subunits (13.7, 16.1, 21.5, 39, 43 and 53 kDa) were labelled. Comparison with the subunit labelling of F1F0-ATPase and ubiquinol:cytochrome c oxidoreductase indicated that the labelling pattern of NADH:ubiquinone oxidoreductase, and enzyme complex with a multitude of subunits, is unique and not due to contamination by other inner-membrane proteins. The correlation between the electron- and proton-transport functions and the DCCD-binding components remains to be established.

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5

Peerce, B. E. "Molecular mechanism of two noncompetitive inhibitors of Na(+)-glucose cotransporter: comparison of DCCD and PCMB." American Journal of Physiology-Gastrointestinal and Liver Physiology 264, no. 2 (February 1, 1993): G300—G305. http://dx.doi.org/10.1152/ajpgi.1993.264.2.g300.

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The effects of noncompetitive inhibitors of Na(+)-dependent glucose uptake, p-chloromercuribenzoate N,N'-dicyclohexylcarbodiimide (DCCD), on substrate-induced cotransporter conformational changes were examined using fluorescein isothiocyanate (FITC) and tryptophan fluorescence. p-chloromercuribenzoate (PCMB) inhibited both substrate-induced conformational changes with similar concentration required for 50% quenching/enhancement of tryptophan or FITC fluorescence. In contrast, DCCD inhibited the Na(+)-induced conformational change with an apparent concentration resulting in 50% inhibition (K0.5) of 18 microM and the glucose-induced conformational change with an apparent K0.5 of 5 microM. DCCD slightly increased the apparent K0.5 for the Na+ concentration required for Na(+)-induced conformational change. DCCD and PCMB altered tryptophan accessibility to quench reagents in all three conformations. Tryptophan residues on the PCMB-treated cotransporter were more Cs+ than I- sensitive in contrast to the unlabeled cotransporter. The PCMB-treated cotransporter had a reduced response to Na+, suggesting that the mode of PCMB inactivation of cotransporter activity resulted from conformational changes in the substrate-free cotransporter. DCCD had a smaller effect on cotransporter tryptophan quench reagent susceptibility. However, DCCD-labeled cotransporter was equally accessible to I- and Cs+, and the DCCD-labeled cotransporter did not respond to substrates. Loss of charge distribution around cotransporter tryptophans correlated with loss of substrate-induced conformational changes.

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Müller, Tina A., Steven M. Byrde, Christoph Werlen, Jan Roelof van der Meer, and Hans-Peter E. Kohler. "Genetic Analysis of Phenoxyalkanoic Acid Degradation in Sphingomonas herbicidovorans MH." Applied and Environmental Microbiology 70, no. 10 (October 2004): 6066–75. http://dx.doi.org/10.1128/aem.70.10.6066-6075.2004.

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ABSTRACT Phenoxyalkanoic acid degradation is well studied in Beta- and Gammaproteobacteria, but the genetic background has not been elucidated so far in Alphaproteobacteria. We report the isolation of several genes involved in dichlor- and mecoprop degradation from the alphaproteobacterium Sphingomonas herbicidovorans MH and propose that the degradation proceeds analogously to that previously reported for 2,4-dichlorophenoxyacetic acid (2,4-D). Two genes for α-ketoglutarate-dependent dioxygenases, sdpA MH and rdpA MH, were found, both of which were adjacent to sequences with potential insertion elements. Furthermore, a gene for a dichlorophenol hydroxylase (tfdB), a putative regulatory gene (cadR), two genes for dichlorocatechol 1,2-dioxygenases (dccA I/II), two for dienelactone hydrolases (dccD I/II), part of a gene for maleylacetate reductase (dccE), and one gene for a potential phenoxyalkanoic acid permease were isolated. In contrast to other 2,4-D degraders, the sdp, rdp, and dcc genes were scattered over the genome and their expression was not tightly regulated. No coherent pattern was derived on the possible origin of the sdp, rdp, and dcc pathway genes. rdpA MH was 99% identical to rdpA MC1, an (R)-dichlorprop/α-ketoglutarate dioxygenase from Delftia acidovorans MC1, which is evidence for a recent gene exchange between Alpha- and Betaproteobacteria. Conversely, DccAI and DccAII did not group within the known chlorocatechol 1,2-dioxygenases, but formed a separate branch in clustering analysis. This suggests a different reservoir and reduced transfer for the genes of the modified ortho-cleavage pathway in Alphaproteobacteria compared with the ones in Beta- and Gammaproteobacteria.

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YANG, Su J., Shih S. JIANG, Soong Y. KUO, Shu H. HUNG, Ming F. TAM, and Rong L. PAN. "Localization of a carboxylic residue possibly involved in the inhibition of vacuolar H+-pyrophosphatase by N,N′-dicyclohexylcarbodi-imide." Biochemical Journal 342, no. 3 (September 5, 1999): 641–46. http://dx.doi.org/10.1042/bj3420641.

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A vacuolar H+-pyrophosphatase (EC 3.6.1.1) that catalyses PPi hydrolysis and the electrogenic translocation of protons from the cytosol to the vacuole lumen, was purified from etiolated hypocotyls of mung bean seedlings (Vigna radiata L.). Group-specific modification was used to identify a carboxylic residue involved in the inhibition of vacuolar H+-pyrophosphatase. Carbodi-imides, such as N,N′-dicyclohexylcarbodi-imide (DCCD) and 1-ethyl-3-(3-dimethylamino-propyl)carbodi-imide, and Woodward's reagent K caused a progressive decline in the enzymic activity of vacuolar H+-pyrophosphatase in a time- and concentration-dependent manner. The stoichiometry of labelling of the vacuolar H+-pyrophosphatase by [14C]DCCD determined that DCCD modifies one carboxylic residue per subunit of the enzyme. Protection studies suggest that the DCCD-reactive carboxylic residue resides at or near the substrate-binding site. Furthermore, peptide mapping analysis reveals that Asp283, located in the putative loop V of a tentative topological model of vacuolar H+-pyrophosphatase on the cytosolic side, was labelled by radioactive [14C]DCCD. Cytosolic loop V contains both DCCD-sensitive Asp283 and a conserved motif sequence, rendering it a candidate for the catalytic site of vacuolar H+-pyrophosphatase. A topological picture of the active domain of vacuolar H+-pyrophosphatase is tentatively proposed.

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8

Lauzin, Clément, N. Moazzen-Ahmadi, and A. R. W. McKellar. "Infrared spectra of acetylene dimers and acetylene–nitrogen: (DCCD)2, H-bonded DCCD–HCCH, and DCCD–NN in the 4.1μm region." Journal of Molecular Spectroscopy 269, no. 1 (September 2011): 124–28. http://dx.doi.org/10.1016/j.jms.2011.05.010.

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9

Vgenopoulou, Irini, Anja C. Gemperli, and Julia Steuber. "Specific Modification of a Na+ Binding Site in NADH:Quinone Oxidoreductase from Klebsiella pneumoniae with Dicyclohexylcarbodiimide." Journal of Bacteriology 188, no. 9 (May 1, 2006): 3264–72. http://dx.doi.org/10.1128/jb.188.9.3264-3272.2006.

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ABSTRACT The respiratory NADH:quinone oxidoreductase (complex I) (NDH-1) is a multisubunit enzyme that translocates protons (or in some cases Na+) across energy-conserving membranes from bacteria or mitochondria. We studied the reaction of the Na+-translocating complex I from the enterobacterium Klebsiella pneumoniae with N,N′-dicyclohexylcarbodiimide (DCCD), with the aim of identifying a subunit critical for Na+ binding. At low Na+ concentrations (0.6 mM), DCCD inhibited both quinone reduction and Na+ transport by NDH-1 concurrent with the covalent modification of a 30-kDa polypeptide. In the presence of 50 mM Na+, NDH-1 was protected from inhibition by DCCD, and the modification of the 30-kDa polypeptide with [14C]DCCD was prevented, indicating that Na+ and DCCD competed for the binding to a critical carboxyl group in NDH-1. The 30-kDa polypeptide was assigned to NuoH, the homologue of the ND1 subunit from mitochondrial complex I. It is proposed that Na+ binds to the NuoH subunit during NADH-driven Na+ transport by NDH-1.

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10

Kisnierienë, Vilma, and Vidmantas Sakalauskas. "The effect of aluminium on bioelectrical activity of the Nitellopsis obtusa cell membrane after H+-ATPase inhibition." Open Life Sciences 2, no. 2 (June 1, 2007): 222–32. http://dx.doi.org/10.2478/s11535-007-0009-y.

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AbstractAluminium induced membrane potential (Em) changes and potential changes during repolarization phase of the action potential (AP) in the internodal cells of Nitellopsis obtusa after blocking H+-ATPase activity by DCCD were investigated. Micromolar concentrations of DCCD are sufficient to give complete and irreversible inhibition of proton pumping. The membrane potential was measured by conventional glass-microelectrode technique. We found that the half-amplitude pulse duration differs significantly between standard conditions, after DCCD application, and after H+-ATPase blocking and subsequent Al3+ treatment: 4.9, 7.7 and 17.2 seconds, respectively. We propose that in the short term (2 hours) treatment of Al3+, the decrease in membrane potential was compensated for by H+-ATPase activity. Blocking H+-ATPase activity by DCCD can enhance the influence of Al3+ on the bioelectrical activity of cell membranes.

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11

Swain, L. D., and B. D. Boyan. "Ion-translocating Properties of Calcifiable Proteolipids." Journal of Dental Research 67, no. 3 (March 1988): 526–30. http://dx.doi.org/10.1177/00220345880670030101.

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De novo formation of calcium hydroxyapatite in biological systems occurs on membrane surfaces through specific interactions of Ca, Pi, phospholipids, calcifiable proteolipids, and ion flux to and from the nucleating site. This paper reports an in vitro model demonstrating an ion transport function for calcifiable proteolipid. Bacterionema matruchotii proteolipid was incubated with a radiolabeled H+ -channel inhibitor, 14C-dicyclohexyl-carbodiimide, and binding characterized by displacement studies with DCCD or ethyldimethylaminopropylcarbodiimide. A carboxyl binding site was suggested by displacement of DCCD by the nucleophile, glycine ethyl ester. The displacement studies indicated that proteolipid bound DCCD via carboxyl group interaction in a hydrophobic region of the protein. SDS-polyacrylamide gel electrophoresis showed that all label was associated with a single band of 8500 Mr. No non-specific binding of 14C-DCCD to phospholipids occurred, since all bound label was associated with protein following Sephadex LH-20 chromatography of crude proteolipid. Phospholipid liposomes were prepared containing bacteriorhodopsin and proteolipid or proteolipid-14C-DCCD, via cholate dialysis. Transmembrane pH changes established by the bacteriorhodopsin H+ pump were measured in the presence and absence of added proteolipid. Proteolipid had an effect similar to those of uncouplers such as tetraphenylboron. Both the rate and extent of proton translocation increased following addition of proteolipid to BR-liposomes. 14C-DCCD abolished the proteolipid-augmented ion transport. When tetraphenylboron was used to abolish the transmembrane electrical potential, calcifiable proteolipid did not augment proton transport. These data suggest that calcifiable proteolipids may function as an ionophore during membrane-initiated calcification.

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12

Peerce, B. E., M. Cedilote, and R. D. Clarke. "Role of carboxyl and sulfhydryl residues on rabbit small intestinal brush-border membrane Na(+)-glucose cotransporter." American Journal of Physiology-Gastrointestinal and Liver Physiology 264, no. 2 (February 1, 1993): G294—G299. http://dx.doi.org/10.1152/ajpgi.1993.264.2.g294.

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The role of sulfhydryl (SH) and carboxylic acid residues in Na(+)-dependent glucose uptake, Na(+)-dependent phlorizin binding, and substrate exchange by the rabbit small intestinal brush-border membrane (BBM) Na(+)-glucose cotransporter was examined in sodium dodecyl sulfate-BBM vesicles. The sulfhydryl reagent p-chloromercuribenzoate (PCMB) inhibited all three measures of cotransporter function in a dithiothreitol-sensitive manner with similar K0.5 values (concn of PCMB resulting in 50% inhibition). PCMB sulfonate had no effect on Na(+)-glucose cotransporter function < 250 microM. The carboxylic acid reagent 1-ethyl-3-(4-azonia-4,4-dimethylpentyl)carbodiimide no effect on Na(+)-glucose cotransporter function. N,N'-dicyclohexylcarbodiimide (DCCD) inhibited all three measures of cotransporter function with similar K0.5 values for inhibition. Inhibition by DCCD did not require addition of a nucleophile. In contrast, PCMB-pretreated cotransporter was insensitive to DCCD in the absence of added nucleophile with respect to substrate transport (Na(+)-dependent glucose uptake) but not Na(+)-dependent phlorizin binding. These results indicate an intravesicular or lipophilic environment for both the PCMB-reactive SH residue and the DCCD-reactive carboxylic acid residues, suggesting that a SH residue may act as an endogenous nucleophile for interaction of DCCD with the Na(+)-glucose cotransporter and suggesting that different carboxylic acid residues may be involved in Na(+)-dependent glucose uptake and Na(+)-dependent phlorizin binding.

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13

Bhattacharjee, R. L., J. S. Muenter, and L. H. Coudert. "The hyperfine structure of (DCCD)2." Journal of Chemical Physics 97, no. 12 (December 15, 1992): 8850–63. http://dx.doi.org/10.1063/1.463360.

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VYu, Artzatbanov, and D. N. Ostrovsky. "The distribution of electron flow in the branched respiratory chain of Micrococcus luteus." Biochemical Journal 266, no. 2 (March 1, 1990): 481–86. http://dx.doi.org/10.1042/bj2660481.

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Endogenous coupled respiration of Micrococcus luteus protoplasts showed a relatively high resistance to low concentrations of KCN, 2-nonyl-4-hydroxyquinoline N-oxide (NQNO) and dicyclohexylcarbodi-imide (DCCD) when the inhibitors were applied individually. In the presence of both KCN and NQNO (or DCCD), O2 uptake was strongly inhibited. The proteolysis of external membrane proteins of protoplasts also induced the high sensitivity of endogenous coupled respiration to low KCN. The effects of NQNO, DCCD and proteolysis were explained by the inhibition of an alternative respiratory system when reducing equivalents passed preferentially down the KCN-sensitive cytochrome oxidase. Uncoupling of the cell membrane increased the electron flow via the cytochrome oxidase-containing respiratory branch. It is suggested that the energy state of cells could control the electron-flow distribution between two branches, and quinones of different levels of reduction could be involved in the mechanism of respiratory branching.

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15

Honkakoski, P. J., and I. E. Hassinen. "Sensitivity to NN'-dicyclohexylcarbodi-imide of proton translocation by mitochondrial NADH:ubiquinone oxidoreductase." Biochemical Journal 237, no. 3 (August 1, 1986): 927–30. http://dx.doi.org/10.1042/bj2370927.

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Proton extrusion during ferricyanide reduction by NADH-generating substrates or succinate was studied in isolated rat liver mitochondria with the use of optical indicators. NN'-Dicyclohexylcarbodi-imide (DCCD) caused a decrease of 84% in the H+/e- ratio of NADH:cytochrome c reduction, but a decrease of only 49% in that of succinate:cytochrome c reduction, even though electron transfer was decreased equally in both spans. The data indicate that a DCCD-sensitive channel operates in the NADH:ubiquinone oxidoreductase region of the respiratory chain.

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16

DiResta, D. J., K. P. Kutschke, M. D. Hottois, and K. D. Garlid. "K+-H+ exchange and volume homeostasis in brown adipose tissue mitochondria." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 251, no. 4 (October 1, 1986): R787—R793. http://dx.doi.org/10.1152/ajpregu.1986.251.4.r787.

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K+-H+ exchange activity in hamster brown adipose tissue mitochondria is activated following depletion of matrix Mg2+ with the divalent cation ionophore A23187. Quinine inhibits K+-H+ exchange reversibly with an I50 of 22 microM, whereas mild treatment with N,N'-dicyclohexylcarbodiimide (DCCD) inhibits this activity irreversibly. In an attempt to label and identify the K+-H+ antiporter protein, brown adipose tissue mitochondria were incubated with [14C]DCCD and subjected to denaturing polyacrylamide gel electrophoresis and fluorography. We observed a labeled band of relative mol wt, 78,000, which satisfies criteria established in rat liver mitochondria for the identification of this carrier (W. H. Martin et al., J. Biol. Chem. 259: 2062-2065, 1984). Thus Mg2+ and quinine each protect the K+-H+ exchanger against both inhibition and binding by DCCD. Volume homeostasis in brown adipose tissue mitochondria, as in other mitochondria, requires a balance between K+ influx and efflux. We propose that regulation of the K+-H+ antiporter, the primary K+ efflux mechanism, plays a major role in this process.

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17

Nakashima, Richard A. "Hexokinase-binding properties of the mitochondrial VDAC protein: Inhibition by DCCD and location of putative DCCD-binding sites." Journal of Bioenergetics and Biomembranes 21, no. 4 (August 1989): 461–70. http://dx.doi.org/10.1007/bf00762518.

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18

Bank, N., H. S. Aynedjian, and B. F. Mutz. "Evidence for a DCCD-sensitive component of proximal bicarbonate reabsorption." American Journal of Physiology-Renal Physiology 249, no. 5 (November 1, 1985): F636—F644. http://dx.doi.org/10.1152/ajprenal.1985.249.5.f636.

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To examine the possible contribution of active H+ secretion mediated by brush border enzymes to proximal tubule HCO-3 absorption, paired reperfusions of surface proximal convoluted tubules were performed with the inhibitor dicyclohexylcarbodiimide (DCCD). In control studies using a solution devoid of HCO-3 but containing 5.5 mM glucose, 1 mM DCCD had no effect on glucose or fluid (Na+) absorption, suggesting that this inhibitor did not interfere with sodium entry at the brush border or mitochondrial energy production (ATP synthesis). In experiments using a perfusion solution containing 18-25 mM HCO-3, DCCD caused a fall in absolute CO2 absorption of approximately 15% under eucapneic conditions and 30% during acute hypercapnia. One millimole per liter amiloride (an inhibitor of the passive Na+-H+ exchanger) caused a 15% inhibition of CO2 absorption during acute hypercapnia and a disproportionately large reduction in fluid (Na+) absorption. The latter was not due to cell poisoning, since 1 mM amiloride had no inhibitory effect on fluid or glucose absorption when a HCO-3-free perfusion solution was used. Addition of 1 mM DCCD to a perfusion solution containing either 10(-3) M amiloride or 10(-4) M acetazolamide caused a significant inhibition of CO2 absorption compared with amiloride or acetazolamide alone. The observations are consistent with the view that in addition to passive Na+-H+ exchange, active transport mediated by either a H+-ATPase or a redox-driven H+ pump in the brush border contributes significantly to HCO-3 absorption in the proximal tubule.

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Buczek, Józef, Marek Burzyński, and Anna Suder-Moraw. "Inhibition of nitrate reductase and ATPase activities in Zea mays roots by tungsten and N, N'-dicyclohexylcarbodiimide." Acta Societatis Botanicorum Poloniae 50, no. 3 (2014): 455–64. http://dx.doi.org/10.5586/asbp.1981.069.

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The activity of soluble and membrane-bound ATPase obtained from corn roots was in vivo markedly inhibited by N,N' -dicyclohexylcanbodiimide (DCCD) and W042- ions. DCCD (2.5 X 10-5 M) added to the nutrient solution strongly decreased in vivo nitrate reductase (NR) activity after 12-h growth of plants while it had no effect in experiments in vitro on NR activity. Tungsten in a concentration of 10-4 M completely blocked NR activity after 24 h. In the above used concentrations neither DCCD nor W042- inhibited completely N03- absorption by corn roots. The results suggest that there must exist in corn roots another or an additional mechanism of N03- assimilation apart from of that proposed by Butz and Jackson (1977).

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Gevorgyan, Heghine Kh, Anait V. Vassilian, and Karen A. Trchounian. "THE ROLE OF PROTON ATPase SPECIFIC INHIBITOR $N,N'$-DICYCLOHEXYLCARBODIIMIDE AND EXTERNAL FORMATE CONCENTRATION ON $E.~COLI$ GROWTH DURING MIXED CARBON SOURCES FERMENTATION AT DIFFERENT pHs." Proceedings of the YSU B: Chemical and Biological Sciences 55, no. 1 (254) (April 28, 2021): 67–74. http://dx.doi.org/10.46991/pysu:b/2021.55.1.067.

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This research is focused on the investigation of specific growth rate changes of $E.~coli$ wild type and mutant strains with defect of Hyd, FDH enzymes and FhlA regulatory protein in the presence of $N,N'$-dicyclohexylcarbodiimide (DCCD) and external formate various concentration during co-fermentation of glucose, glycerol and formate at pHs $5.5-7.5.$ The highest value of SGR was observed at pH 7.5. It was revealed that SGR depends on external formate concentration at all pHs. DCCD inhibitory effect was shown mainly at pH 7.5 and partially at pH 6.5 and 5.5. In the case of the F0F1-ATPase inhibition FhlA compensatory effect on SGR was revealed.

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Lahankar, Sridhar A., Jianming Zhang, Sophya Garashchuk, George C. Schatz, and Timothy K. Minton. "Electronic Population Inversion in HCCO/DCCO Products from Hyperthermal Collisions of O(3P) with HCCH/DCCD." Journal of Physical Chemistry Letters 4, no. 8 (April 8, 2013): 1315–21. http://dx.doi.org/10.1021/jz400568t.

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22

Jezek, P., A. D. Beavis, D. J. Diresta, R. N. Cousino, and K. D. Garlid. "Evidence for two distinct chloride uniport pathways in brown adipose tissue mitochondria." American Journal of Physiology-Cell Physiology 257, no. 6 (December 1, 1989): C1142—C1148. http://dx.doi.org/10.1152/ajpcell.1989.257.6.c1142.

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Chloride permeability of the inner membrane of brown adipose tissue mitochondria was analyzed by monitoring mitochondrial swelling in KCl salts in the presence of K+ ionophores. The results indicate that the high anion conductance observed in these mitochondria is due to the presence of two separate pathways: 1) a Cl-conducting pathway that is inhibited by guanosine 5'-diphosphate (GDP) but neither by N,N'-dicyclohexylcarbodiimide (DCCD) nor by amphiphilic amines and that is found uniquely in brown adipose tissue mitochondria and 2) an inner membrane anion uniport channel that is inhibited both by DCCD and by amphiphilic amines but not by GDP and that is opened either by depletion of matrix Mg2+ or by alkalinization of the matrix.

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Kuwahara, M., S. Sasaki, and F. Marumo. "Cell pH regulation in rabbit outer medullary collecting duct cells: mechanisms of HCO3(-)-independent processes." American Journal of Physiology-Renal Physiology 259, no. 6 (December 1, 1990): F902—F909. http://dx.doi.org/10.1152/ajprenal.1990.259.6.f902.

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To clarify mechanisms of intracellular pH (pHi) regulation in outer stripe of outer medullary collecting duct (OMCDOS), isolated perfused OMCDOS of the rabbit were loaded with 2',7'-bis(carboxyethyl)-5(6)-carboxyfluorescein (BCECF), and single cell pHi was monitored by an image processing system. Initial pHi recovery rates (dpHi/dt, pH unit/s x 10(3)) after intracellular acid load made by NH4Cl prepulse were determined. In the absence of exogenous CO2-HCO3-, dpHi/dt was 12.3 +/- 0.9 (means +/- SE) in principal cells (PC), and 11.5 +/- 1.0 in intercalated cells (IC). In PC, total ambient Na+ removal halted pHi recovery (dpHi/dt = 0.6 +/- 0.5), and pHi recovered when Na+ was added to the basolateral (dpHi/dt = 14.7 +/- 0.8) but not to the luminal (dpHi/dt = 0.9 +/- 0.5) solutions. This bath Na+ effect was amiloride inhibitable. In IC, pHi recovered (dpHi/dt = 6.4 +/- 0.3) in the absence of ambient Na+. This pHi recovery was significantly reduced by luminal 0.5 mM N-ethylmaleimide (NEM) or 0.5 mM N,N'-dicyclohexylcarbodiimide (DCCD). Basolateral NEM or DCCD had no significant effect. Basolateral addition of Na+ significantly accelerated the pHi recovery. These data suggest the presence of basolateral Na(+)-H+ exchange in both PC and IC, and luminal NEM- and DCCD-sensitive H+ pump in IC of rabbit OMCDOS.

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MORENO, N. J. Silvia, Li ZHONG, Hong-Gang LU, Wanderley DE SOUZA, and Marlene BENCHIMOL. "Vacuolar-type H+-ATPase regulates cytoplasmic pH in Toxoplasma gondii tachyzoites." Biochemical Journal 330, no. 2 (March 1, 1998): 853–60. http://dx.doi.org/10.1042/bj3300853.

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Cytoplasmic pH (pHi) regulation was studied in Toxoplasma gondii tachyzoites by using the fluorescent dye 2ʹ,7ʹ-bis-(2-carboxyethyl)-5(6)-carboxyfluorescein. Their mean baseline pHi (7.07±0.06; n = 5) was not significantly affected in the absence of extracellular Na+, K+ or HCO3- but was significantly decreased in a dose-dependent manner by low concentrations of N,Nʹ-dicyclohexylcarbodi-imide (DCCD), N-ethylmaleimide (NEM) or bafilomycin A1. Bafilomycin A1 also inhibited the recovery of tachyzoite pHi after an acid load with sodium propionate. Similar concentrations of DCCD, NEM and bafilomycin A1 produced depolarization of the plasma membrane potential as measured with bis-(1,3-diethylthiobarbituric)trimethineoxonol (bisoxonol), and DCCD prevented the hyperpolarization that accompanies acid extrusion after the addition of propionate, in agreement with the electrogenic nature of this pump. Confocal laser scanning microscopy indicated that, in addition to being located in cytoplasmic vacuoles, the vacuolar (V)-H+-ATPase of T. gondii tachyzoites is also located in the plasma membrane. Surface localization of the V-H+-ATPase was confirmed by experiments using biotinylation of cell surface proteins and immunoprecipitation with antibodies against V-H+-ATPases. Taken together, the results are consistent with the presence of a functional V-H+-ATPase in the plasma membrane of these intracellular parasites and with an important role of this enzyme in the regulation of pHi homoeostasis in these cells.

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25

Grotmol, T., T. Buanes, and M. G. Ræder. "DCCD (N, N′-Dicyclohexylcarbodiimide) Inhibits Biliary Secretion of HCO3." Scandinavian Journal of Gastroenterology 22, no. 2 (January 1987): 207–13. http://dx.doi.org/10.3109/00365528708991881.

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26

DeLeon, Robert L., and John S. Muenter. "Radiofrequency spectroscopy of DCCD: Deuterium quadrupole coupling in acetylene." Journal of Molecular Spectroscopy 126, no. 1 (November 1987): 13–18. http://dx.doi.org/10.1016/0022-2852(87)90071-3.

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27

HUGHES, Glen, Michael A. HARRISON, Yong-In KIM, David E. GRIFFITHS, Malcolm E. FINBOW, and John B. C. FINDLAY. "Interaction of dibutyltin-3-hydroxyflavone bromide with the 16 kDa proteolipid indicates the disposition of proton translocation sites of the vacuolar ATPase." Biochemical Journal 317, no. 2 (July 15, 1996): 425–31. http://dx.doi.org/10.1042/bj3170425.

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The organotin complex dibutyltin-3-hydroxyflavone bromide [Bu2Sn(of)Br] has been shown to bind to the 16 kDa proteolipid of Nephrops norvegicus, either in the form of the native protein or after heterologous expression in Saccharomyces and assembly into a hybrid vacuolar H+-ATPase. Titration of Bu2Sn(of)Br against the 16 kDa proteolipid results in a marked fluorescence enhancement, consistent with binding to a single affinity site on the protein. Vacuolar ATPase-dependent ATP hydrolysis was also inhibited by Bu2Sn(of)Br, with the inhibition constant correlating well with dissociation constants determined for binding of Bu2Sn(of)Br complex to the proteolipid. The fluorescence enhancement produced by interaction of probe with proteolipid can be back-titrated by dicyclohexylcarbodiimide (DCCD), which covalently modifies Glu140 on helix-4 of the polypeptide. Expression of a mutant proteolipid in which Glu140 was changed to a glycine resulted in assembly of a vacuolar ATPase which was inactive in proton pumping and which had reduced ATPase activity. Co-expression studies with this mutant and wild-type proteolipids suggest that proton pumping can only occur in a vacuolar ATPase containing exclusively wild-type proteolipid. The fluorescent enhancement or affinity of Bu2Sn(of)Br for the mutant proteolipid was not significantly altered, with the organotin complex having no effect on residual ATPase activity. Interaction of the probe with mutant proteolipid was unaffected by DCCD. These data suggest an overlap in the binding sites for organotin and DCCD, and have implications for the organization and structure of proton-translocating pathways in the vacuolar H+-ATPase.

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28

Trchounian, Armen, and Hiroshi Kobayashi. "K+ Uptake by Fermenting Escherichia coli Cells: pH Dependent Mode of the TrkA System Operating." Bioscience Reports 20, no. 4 (August 1, 2000): 277–88. http://dx.doi.org/10.1023/a:1026493024066.

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Escherichia coli accumulates K+ by means of multiple transportsystems, of which TrkA is the most prominent at neutral and alkalinepH while Kup is major at acidic pH. In the present study, K+ uptakewas observed with cells grown under fermentative conditions at an initialpH of 9.0 and 7.3 (the medium pH decreased to 8.4 and 6.8, respectively, during the mid-logarithmic growth phase), washed with distilled water andresuspended in a K+ containing medium at pH 7.5 in the presence ofglucose. The kinetics for this K+ uptake and the amount of K+accumulated by the wild type and mutants having a functional TrkA or Kup could confirm that K+ uptake by E. coli grown either at pH 9.0or pH 7.3 occurs mainly through TrkA. The following results distinguishpH dependent mode of TrkA operating: (1) K+ uptake was inhibited byDCCD in cells grown either at pH 9.0 or pH 7.3, although the stoichiometryof K+ influx to DCCD-inhibited H+ efflux for bacteria grownat pH 9.0 varied with external K+ concentration, but remained constantfor cells grown at pH 7.3; (2) K+ uptake was observed with an atpDmutant grown at pH 9.0 but not at pH 7.3; (3) The DCCD-inhibited H+efflux was increased 8-fold less by 5 mM K+ added into a K+ freemedium for bacteria grown at pH 9.0 than that for cells grown at pH 7.3;(4) the DCCD-inhibited ATPase activity of membrane vesicles from bacteriagrown at pH 9.0 was reduced a little in the presence of 100 mM K+, but stimulated more than 2.4-fold at pH 7.3.

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29

VANDERHEYDEN, Nicole, Julian WONG, and Roberto DOCAMPO. "A pyruvate–proton symport and an H+-ATPase regulate the intracellular pH of Trypanosoma brucei at different stages of its life cycle." Biochemical Journal 346, no. 1 (February 8, 2000): 53–62. http://dx.doi.org/10.1042/bj3460053.

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Regulation of intracellular pH (pHi) and H+ efflux were investigated in Trypanosoma brucei bloodstream and procyclic trypomastigotes using the fluorescent dyes 2ʹ,7ʹ-bis-(2-carboxyethyl)-5(6)-carboxyfluorescein (BCECF) acetoxymethyl ester and free BCECF respectively. pHi in bloodstream and procyclic trypomastigotes was 7.47±0.06 and 7.53±0.07 respectively. Differences in the mechanisms for the regulation of pHi were noted between bloodstream and procyclic forms. Procyclic trypomastigotes maintained their pHi at neutral over a wide range of external pH values from 6 to 8, and in the absence of K+ or Na+. The H+-ATPase inhibitors N,Nʹ-dicyclohexylcarbodi-imide (DCCD), diethylstilboestrol and N-ethylmaleimide substantially decreased the steady-state pHi and inhibited its recovery from acidification. The rate of H+ efflux in these forms was determined to be 62±6.5 nmol/min per mg of protein, and was substantially decreased by H+-ATPase inhibitors. The data support the presence of an H+-ATPase as the major regulator of pHi in procyclic trypomastigotes. In contrast, bloodstream trypomastigotes were unable to maintain a neutral pH under acidic conditions, and their steady-state pHi and recovery from acidification were unaffected by H+-ATPase inhibitors, except for DCCD (100 μM). Their steady-state pHi was markedly decreased in glucose-free buffer or by ≥ 10 mM pyruvate, whereas procyclic trypomastigotes were unaffected by similar treatments. The rate of H+ efflux in bloodstream trypomastigotes was 534±38 nmol/min per mg of protein, and was decreased in the absence of glucose and by the addition of pyruvate or DCCD. Pyruvate efflux in these forms was calculated to be 499±34 nmol/min per mg of protein, and was significantly inhibited by DCCD, 4,4ʹ-di-isothiocyanatodihydrostilbene-2,2ʹ-disulphonic acid and α-cyanohydroxycinnamic acid. The pyruvate analogues β-hydroxypyruvate, 3-bromopyruvate, 3-oxoglutarate, oxaloacetate, 3-oxoisovalerate and 3-oxoisohexanoate significantly decreased pHi, as well as proton and pyruvate efflux, whereas lactate had only a small effect, and no effect was observed with citrate or fumarate. The inhibition by pyruvate analogues of pyruvate efflux, proton efflux and acidification of pHi supports the hypothesis that pyruvate efflux is accompanied by proton efflux and that this is the major pHi control mechanism in bloodstream forms. Inhibition by H+-ATPase inhibitors of residual H+ efflux in the absence of glucose or in the presence of high extracellular pyruvate indicates a minor role for H+-ATPase(s) in control of pHi in bloodstream forms.

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30

Jansma, Esther, Rowin J. van Lanen, Peter W. Brewer, and Rutger Kramer. "The DCCD: A digital data infrastructure for tree-ring research." Dendrochronologia 30, no. 4 (January 2012): 249–51. http://dx.doi.org/10.1016/j.dendro.2011.12.002.

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31

Trchounian, Armen, Yelena Ohanjanyan, Karine Bagramyan, Vitya Vardanian, Eleonora Zakharyan, Anait Vassilian, and Misak Davtian. "Relationship of the Escherichia coli TrkA System of Potassium Ion Uptake with the F0F1-ATPase Under Growth Conditions Without Anaerobic or Aerobic Respiration." Bioscience Reports 18, no. 3 (June 1, 1998): 143–54. http://dx.doi.org/10.1023/a:1020144628839.

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K+ uptake by the Escherichia coli TrkA system is unusual in that it requires both ATP and ΔμH; a relation withH+ circulation through the membrane is thereforesuggested. The relationship of this system with the F0F1-ATPase was studied in intact cells grownunder different conditions. A significant increase of the N,N'-dicyclohexylcarbodiimide(DCCD)-inhibitedH+ efflux through the F0F1 by 5 mMK+, but not by Na+ added into thepotassium-free medium was revealed only in fermenting wild-type orparent cells, that were grown under anaerobic conditions withoutanaerobic or aerobic respiration and with the production of H2. Such an increase disappeared in the Δunc or the trkA mutants that have alteredF0F1 or defective TrkA, respectively. This finding indicates a closed relationship between TrkA andF0F1, with these transport systems beingassociated in a single mechanism that functions as an ATP-driven H+–K+-exchanging pump. ADCCD-inhibited H+–K+-exchangethrough these systems with the fixed stoichiometry of H+and K+ fluxes(2H+/K+) and a higherK+ gradient between the cytoplasm and the externalmedium were also found in these bacteria. They were not observed incells cultured under anaerobic conditions in the presence of nitrate orunder aerobic conditions with respiration and without production of H2. The role of anaerobic or aerobic respiration as adeterminant of the relationship of the TrkA with the F0F1 is postulated. Moreover, an increase of DCCD-inhibited H+ efflux by added K+, aswell as the characteristics of DCCD-sensitiveH+–K+-exchange found in a parentstrain, were lost in the arcA mutant with a defective Arc system, suggesting a repression of enzymes in respiratorypathways. In addition, K+ influx in the latest mutantwas not markedly changed by valinomycin or with temperature. The arcA gene product or the Arc system is proposed to beimplicated in the regulation of the relationship between TrkA and F0F1.

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32

Sabolic, I., and G. Burckhardt. "Characteristics of the proton pump in rat renal cortical endocytotic vesicles." American Journal of Physiology-Renal Physiology 250, no. 5 (May 1, 1986): F817—F826. http://dx.doi.org/10.1152/ajprenal.1986.250.5.f817.

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The characteristics of the H+ pump in isolated rat renal endocytotic vesicles were studied by the delta pH-sensitive dye acridine orange, the voltage-sensitive dye 3,3'-dipropylthiadicarbocyanine iodide, and by a coupled optical ATPase assay. Intravesicular acidification depended on ATP and Mg2+ concentrations with half-maximal activations at 73 and 77 microM, respectively. CTP, GTP, UTP, and ITP partially supported acidification, but ADP and AMP did not. Ouabain, ethoxzolamide, levamisole, and vanadate did not inhibit H+ uptake into endocytotic vesicles. Oligomycin inhibited partially. Depending on concentration and preincubation time, Dio-9, filipin, N-ethylmaleimide (NEM), and dicyclohexylcarbodiimide (DCCD) inhibited H+ uptake completely. Filipin and, partially, DCCD acted nonspecifically by dissipating pH gradients. A specific cation was not required for the H+ pump; Zn2+ inhibited. Compared with mannitol, ATP-driven H+ uptake was stimulated by SCN- greater than Cl- greater than Br- greater than I- much greater than HPO4(2-) = gluconate = HCO3- = F-, but not by SO4(2-), NO3-, CH3COO-, S2O3(2-), and S4O6(2-). Chloride stimulated H+ uptake from the outside of the vesicles with an apparent Km of 27 mM. In the absence of Cl-, ATP-driven proton uptake was increased by intravesicular K+ and valinomycin, suggesting that the pump is electrogenic. The electrogenicity, however, could not be demonstrated with voltage-sensitive dyes. The vesicle membrane contains no significant K+ and Cl- conductances; only a conductance for H+ was found. The vesicles exhibited an ouabain-, oligomycin-, and vanadate-insensitive ATPase activity that was inhibited by DCCD and NEM. Our data indicate the presence of an electrogenic H+ pump in endocytotic vesicles from rat renal proximal tubules with similar characteristics as H+ pumps present in various intracellular (nonmitochondrial) membranes.

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33

Harvey, B., I. Lacoste, and J. Ehrenfeld. "Common channels for water and protons at apical and basolateral cell membranes of frog skin and urinary bladder epithelia. Effects of oxytocin, heavy metals, and inhibitors of H(+)-adenosine triphosphatase." Journal of General Physiology 97, no. 4 (April 1, 1991): 749–76. http://dx.doi.org/10.1085/jgp.97.4.749.

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We have compared the response of proton and water transport to oxytocin treatment in isolated frog skin and urinary bladder epithelia to provide further insights into the nature of water flow and H+ flux across individual apical and basolateral cell membranes. In isolated spontaneous sodium-transporting frog skin epithelia, lowering the pH of the apical solution from 7.4 to 6.4, 5.5, or 4.5 produced a fall in pHi in principal cells which was completely blocked by amiloride (50 microM), indicating that apical Na+ channels are permeable to protons. When sodium transport was blocked by amiloride, the H+ permeability of the apical membranes of principal cells was negligible but increased dramatically after treatment with antidiuretic hormone (ADH). In the latter condition, lowering the pH of the apical solution caused a voltage-dependent intracellular acidification, accompanied by membrane depolarization, and an increase in membrane conductance and transepithelial current. These effects were inhibited by adding Hg2+ (100 microM) or dicyclohexylcarbodiimide (DCCD, 10(-5) M) to the apical bath. Net titratable H+ flux across frog skin was increased from 30 +/- 8 to 115 +/- 18 neq.h-1.cm-2 (n = 8) after oxytocin treatment (at apical pH 5.5 and serosal pH 7.4) and was completely inhibited by DCCD (10(-5) M). The basolateral membranes of the principal cells in frog skin epithelium were found to be spontaneously permeable to H+ and passive electrogenic H+ transport across this membrane was not affected by oxytocin. Lowering the pH of the basolateral bathing solution (pHb) produced an intracellular acidification and membrane depolarization (and an increase in conductance when the normal dominant K+ conductance of this membrane was abolished by Ba2+ 1 mM). These effects of low pHb were blocked by micromolar concentrations of heavy metals (Zn2+, Ni2+, Co2+, Cd2+, and Hg2+). Lowering pHb in the presence of oxytocin (50 mU/ml) produced a transepithelial current (3 microA.cm-2 at pHb 5.5) which was blocked by 100 microM of Hg2+, Zn2+, or Ni2+ at the basolateral side, and by DCCD (10(-5) M) or Hg2+ (100 microM) from the apical side. The net hydroosmotic water flux (JH2O) induced by oxytocin in frog bladder sacs was blocked by inhibitors of H(+)-adenosine triphosphatase (ATPase). Diethylstilbestrol (DES 10(-5) M), oligomycin (10(-8) M), and DCCD (10(-5) M) prevented JH2O when present in the lumen. These effects cannot be attributed to inhibition of metabolism since cyanide (10(-4) M), or 2-deoxyglucose (10(-3) M) had no effect on JH2O.(ABSTRACT TRUNCATED AT 400 WORDS)

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34

Budd, K., and G. W. Kerson. "Uptake of phosphate by two cyanophytes: cation effects and energetics." Canadian Journal of Botany 65, no. 9 (September 1, 1987): 1901–7. http://dx.doi.org/10.1139/b87-260.

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Phosphate uptake in the cyanophytes Synechococcus leopoliensis and Oscillatoria limnetica did not require exogenous metallic cations. In O. limnetica phosphate uptake was described by a single Michaelis–Menten relationship between 0.2 and 10.0 μM phosphate. Calcium increased the maximum velocity and decreased the half-saturation concentration for this system; phosphate uptake was also enhanced by Sr2+ and by Mg2+ but not by Na+, K+, or Zn2+ at up to 1 mM. Calcium appeared to act upon the phosphate transporter and its action is suggested to be ecologically significant. Uptake of phosphate in the light by both cyanophytes was unaffected by 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) but was abolished by carbonylcyanide m-chlorophenylhydrazone (CCCP) or dicyclohexylcarbodiimide (DCCD) at concentrations that abolished apparent photosynthesis; however, phosphate uptake was not inhibited by concentrations of CCCP or DCCD that were only slightly inhibitory to apparent photosynthesis. At 5 μM, CCCP abolished light hyperpolarization of the membrane potential but was noninhibitory to phosphate uptake. Phosphate uptake in O. limnetica was accompanied by hyperpolarization of the membrane potential. Gramicidin hyperpolarized the membrane but did not influence phosphate uptake. It is suggested that phosphate uptake in both cyanophytes is independent of the proton motive force.

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35

Shinkarev, Vladimir P., Natalia B. Ugulava, Antony R. Crofts, and Colin A. Wraight. "DCCD Inhibits the Reactions of the Iron−Sulfur Protein inRhodobacter sphaeroidesChromatophores†." Biochemistry 39, no. 51 (December 2000): 16206–12. http://dx.doi.org/10.1021/bi001482u.

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36

Suresh, N., R. Warburg, M. Timmerman, J. Wells, M. Coccia, M. F. Roberts, and H. O. Halvorson. "New Strategies for the Isolation of Microorganisms Responsible for Phosphate Accumulation." Water Science and Technology 17, no. 11-12 (November 1, 1985): 99–111. http://dx.doi.org/10.2166/wst.1985.0224.

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Several strategies were used to isolate organisms involved in the uptake and subsequent release of inorganic phosphate from waste water sludge. These included direct staining for polyphosphates (polyP), growing in 32P inorganic phosphate followed by autoradiography, resistance to dicyclohexyl carbodiimide (DCCD), an ATPase inhibitor, and isolation on the basis of the buoyant density of the cell. Among those microorganisms isolated, three were identified as Acinetobacter lwoffii, A. calcoaceticus and Pseudomqnas vesicularis. The Ps. vesicularis culture had 31% of phosphate as polyP. 31P NMR analysis of the whole cells revealed the presence of polyP when the cultures were grown aerobic-ally to the late stationary phase and its subsequent loss during anaerobic incubation. Loss of polyP was also associated with a decrease in buoyant density of the cell. In the presence of DCCD, there was a decrease in the polyP peak, but a substantial increase in the sugar phosphates which is consistent with a hypothesis that polyP is used as a reserve energy source, Ps. vesicularis cells showed a two-fold increase in the level of polyphosphatase during early stationary phase, but a thirty fold increase in polyphosphate kinase activity during late stationary phase. This increased enzyme activity is consistent with the increased polyP synthesis during late stationary phase.

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37

Murakami, Naoyuki, and Tetsuya Konishi. "DCCD-Sensitive Na+-Transport in the Membrane Vesicles of Halo bacterium halobium." Journal of Biochemistry 103, no. 2 (February 1988): 231–36. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a122253.

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38

GROTMOL, T., T. BUANES, and M. G. RAEDER. "NN′-dicyclohexylcarbodiimide (DCCD) reduces pancreatic NaHCO3secretion without changing pancreatic tissue ATP levels." Acta Physiologica Scandinavica 128, no. 4 (December 1986): 547–54. http://dx.doi.org/10.1111/j.1748-1716.1986.tb08011.x.

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39

Carrasquer, G., M. Li, and M. A. Dinno. "Effect of Dicyclohexylcarbodiimide (DCCD) on Transport Parameters in the Frog Cornea Epithelium." Journal of Membrane Biology 174, no. 2 (March 15, 2000): 97–103. http://dx.doi.org/10.1007/s002320001035.

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40

Dane, Michaela, Kerstin Steinert, Kordula Esser, Susanne Bickel-Sandkötter, and Francisco Rodriguez-Valera. "Properties Of The Plasma Membrane Atpases Of The Halophilic Archaebacteria Haloferax Mediterranei And Haloferax Volcanii." Zeitschrift für Naturforschung C 47, no. 11-12 (December 1, 1992): 835–44. http://dx.doi.org/10.1515/znc-1992-11-1209.

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Both, Haloferax mediterranei and Haloferax volcanii membranes contain ATPases which are capable of hydrolyzing ATP in presence of Mg2+ or Mn2+. The ATPases require high concentrations of NaCl, a pH value of 9, and high temperatures up to 60 °C. Free manganese ions inhibited the enzyme activity of either ATPase. The ATPases of Hf. mediterranei and Hf. volcanii, respectively, show different sensitivities to inhibitors of ATP hydrolysis. ATP hydrolysis of isolated Hf. mediterranei ATPase was inhibited by NaN3, which was reported to be specific for F-ATPases, by nitrate and N-ethylmaleimide (NEM), which are specific inhibitors of V-ATPases. ATP hydrolysis of Haloferax mediterranei membranes was not inhibited by DCCD , but [14C]DCCD was bound to a 14 kDa peptide of the isolated, partially purified enzyme. Furthermore, the ATPase was inactivated by preincubation with 7-chloro-4-nitrobenzofurazan (NBD-Cl). The ATPase activity of Hf. volcanii membranes was inhibited by NEM but not by nitrate and NaN3. SDS gel electrophoresis of the partially purified enzyme of Haloferax mediterranei showed putative ATPase subunits of 53.5, 49, 42, 22, 21, 14, 12, and 7.5 kDa. Immunoblots showed cross reactivity between a 53 kDa peptide and anti-β (chloroplast F1), as well as between 53, 50 and 47 kDa peptides and an ATPase antibody of Methanosarcina barkeri. The results will be discussed in context with the placement of the archaebacterial ATPases (A-ATPases) between F- and V-ATPases

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41

Paerregaard, A., V. Wewer, L. B. Riis, I. Vind, P. Munkholm, P. Schlichting, and F. Moesgaard. "P0672 THE DANISH CROHN COLITIS DATABASE (DCCD): CONTINUITY FROM CHILDHOOD TO OLD AGE." Journal of Pediatric Gastroenterology and Nutrition 39, Supplement 1 (June 2004): S312. http://dx.doi.org/10.1097/00005176-200406001-00796.

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42

Lehninger, Albert L., Baltazar Reynafarje, and Lidia Costa. "Action of DCCD on the H+O stoichiometry of mitoplast cytochrome c oxidase." Journal of Inorganic Biochemistry 23, no. 3-4 (March 1985): 335–40. http://dx.doi.org/10.1016/0162-0134(85)85043-1.

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43

Du, Peng, Jieyi Zhao, Weijuan Cao, and Yigang Wang. "DCCD: Distributed N-Body Rigid Continuous Collision Detection for Large-Scale Virtual Environments." Arabian Journal for Science and Engineering 42, no. 8 (January 28, 2017): 3141–47. http://dx.doi.org/10.1007/s13369-016-2411-0.

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44

Murakami, Naoyuki, and Tetsuya Konishi. "Functional comparison of DCCD-sensitive Na+/H+ antiporter in Halobacterium halobium with monensin." Biochimie 70, no. 6 (June 1988): 819–26. http://dx.doi.org/10.1016/0300-9084(88)90112-5.

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45

Mau, J., S. Menzie, Y. Huang, and S. Hunyor. "Direct Cardiac Compression Device (DCCD) Demonstrates Frank–Starling Enhancement and Preload Recruitment Capability." Heart, Lung and Circulation 16 (January 2007): S180. http://dx.doi.org/10.1016/j.hlc.2007.06.449.

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46

Kopcewicz, Jan, Mariusz Cymerski, and Kazimierz Madela. "Influence of growth regulators and respiration inhibitors on dark transformation of phytochrome in coleoptiles of oat seedlings." Acta Societatis Botanicorum Poloniae 52, no. 2 (2014): 139–48. http://dx.doi.org/10.5586/asbp.1983.016.

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Irradiation with red light leads to the formation of an unstable, undergoing gradual destruction, physiologically active PFR form of phytochrome in the coleoptiles of oat seedlings. Growth substances: IAA, GA3, kinetin, ABA, ethrel as well acetylcholine do not influence the nature and rate of phytochrome dark transformation. Inhibitors of energy-producing processes such as KCN, 2,4-DNP, DCCD and antimycin A inhibit the process of dark destruction of the PFR form of phytochrome.

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47

Aslangul, Elisabeth, Laurent Massias, Alain Meulemans, Françoise Chau, Antoine Andremont, Patrice Courvalin, Bruno Fantin, and Raymond Ruimy. "Acquired Gentamicin Resistance by Permeability Impairment in Enterococcus faecalis." Antimicrobial Agents and Chemotherapy 50, no. 11 (November 2006): 3615–21. http://dx.doi.org/10.1128/aac.00390-06.

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ABSTRACT Enterococci are intrinsically resistant to low levels of aminoglycosides. We previously selected in vitro and in vivo Enterococcus faecalis with intermediate-level resistance to gentamicin that did not abolish synergism with a cell-wall-active agent (E. Aslangul et al., Antimicrob. Agents Chemother. 49:4144-4148, 2005). The aim of this study was to investigate the mechanism of resistance to gentamicin in the 1688-G3 third-step mutant (MIC, 512 μg/ml) of E. faecalis JH2-2. No mutations were found in the genes for L6 ribosomal protein and the four copies of 16S rRNA. Production of a known aminoglycoside-modifying enzyme was unlikely due to the distinct resistance phenotype and absence of the corresponding genes. Efflux was also unlikely since ethidium bromide MICs were similar for JH2-2 and 1688-G3 and since the pump inhibitors reserpine and verapamil had no effect on gentamicin resistance in both strains. To study gentamicin accumulation, we developed a nonisotopic method based on a fluorescent polarization immunoassay. Impaired gentamicin accumulation was observed in 1688-G3 compared to JH2-2 and was only partially reversible by the N,N′-dicyclohexylcarbodiimide (DCCD) uncoupler agent. The lower sensitivity of 1688-G3 to DCCD suggested alteration of the FoF1-ATPase. However, no mutations were detected in the structural genes (atp) for the Fo channel and no difference in transcript levels of atpB and atpE was found between 1688-G3 and JH2-2. Our data are compatible with acquisition of intermediate-level gentamicin resistance by uptake impairment in E. faecalis.

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SIEVERT, K. Michael, S. David THIRIOT, H. Robert EDWARDS, and E. Arnold RUOHO. "High-efficiency expression and characterization of the synaptic-vesicle monoamine transporter from baculovirus-infected insect cells." Biochemical Journal 330, no. 2 (March 1, 1998): 959–66. http://dx.doi.org/10.1042/bj3300959.

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The full-length cDNA for the rat synaptic-vesicle monoamine transporter (VMAT2) containing a C-terminal polyhistidine epitope has been engineered into baculovirus DNA for expression in Spodoptera frugiperda (Sf9) insect cells. Using this recombinant baculovirus and cultured Sf9 cells, rVMAT2 has been expressed at levels of 7.8×106 transporters per cell, as assessed by [3H]dihydrotetrabenazine binding. A 1 l culture of infected cells produced approx. 15 nmol (900 μg) of transporter. rVMAT2 expressed in the Sf9 cells bound [3H]dihydrotetrabenazine with a KD of 31.2 nM and a Bmax of 19.9 pmol/mg. Two polypeptides of 55 and 63 kDa were identified using the photolabel, 7-azido-8-[125I]iodoketanserin ([125I]AZIK). Photoaffinity labelling of rVMAT2 by 1 nM [125I]AZIK was protectable by 10 μM tetrabenazine and 10 μM 7-aminoketanserin. Digitonin-solubilized VMAT2 was purified to greater than 95% homogeneity using immobilized Ni2+-affinity chromatography, followed by lectin (Concanavalin A) chromatography. The purified transporter migrates as a single broad band with a molecular mass of approx. 63 kDa, as analyzed by SDS/PAGE. The purified transporter retained the ability to bind ligands ([125I]AZIK and [3H]dihydrotetrabenazine). The purified VMAT2 bound [3H]dihydrotetrabenazine with a KD of 86.2 nM. As is the case with the monoamine transporter from bovine chromaffin granule membranes, purified VMAT2 is covalently modified by dicyclohexylcarbodi-imide (DCCD) and is specifically labelled by [14C]DCCD. This labelling is inhibited by tetrabenazine and ketanserin. These data indicate that VMAT2 can be overexpressed using the baculovirus expression system and purified.

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Ferguson, Scott A., Stefanie Keis, and Gregory M. Cook. "Biochemical and Molecular Characterization of a Na+-Translocating F1Fo-ATPase from the Thermoalkaliphilic Bacterium Clostridium paradoxum." Journal of Bacteriology 188, no. 14 (July 15, 2006): 5045–54. http://dx.doi.org/10.1128/jb.00128-06.

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ABSTRACT Clostridium paradoxum is an anaerobic thermoalkaliphilic bacterium that grows rapidly at pH 9.8 and 56°C. Under these conditions, growth is sensitive to the F-type ATP synthase inhibitor N,N′-dicyclohexylcarbodiimide (DCCD), suggesting an important role for this enzyme in the physiology of C. paradoxum. The ATP synthase was characterized at the biochemical and molecular levels. The purified enzyme (30-fold purification) displayed the typical subunit pattern for an F1Fo-ATP synthase but also included the presence of a stable oligomeric c-ring that could be dissociated by trichloroacetic acid treatment into its monomeric c subunits. The purified ATPase was stimulated by sodium ions, and sodium provided protection against inhibition by DCCD that was pH dependent. ATP synthesis in inverted membrane vesicles was driven by an artificially imposed chemical gradient of sodium ions in the presence of a transmembrane electrical potential that was sensitive to monensin. Cloning and sequencing of the atp operon revealed the presence of a sodium-binding motif in the membrane-bound c subunit (viz., Q28, E61, and S62). On the basis of these properties, the F1Fo-ATP synthase of C. paradoxum is a sodium-translocating ATPase that is used to generate an electrochemical gradient of Na+ that could be used to drive other membrane-bound bioenergetic processes (e.g., solute transport or flagellar rotation). In support of this proposal are the low rates of ATP synthesis catalyzed by the enzyme and the lack of the C-terminal region of the ε subunit that has been shown to be essential for coupled ATP synthesis.

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50

Shinkarev, Vladimir P., Natalia B. Ugulava, Eiji Takahashi, Antony R. Crofts, and Colin A. Wraight. "Aspartate-187 of CytochromebIs Not Needed for DCCD Inhibition of Ubiquinol: CytochromecOxidoreductase inRhodobacter sphaeroidesChromatophores†." Biochemistry 39, no. 46 (November 2000): 14232–37. http://dx.doi.org/10.1021/bi001179t.

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Journal articles on the topic 'DCCD'

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