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Journal articles on the topic 'FAD (flavin adenine dinucleotide)'

Author: Grafiati

Published: 4 June 2021

Last updated: 15 February 2022

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1

Birss, V. I., H. Elzanowska, and R. A. Turner. "The electrochemical behavior of flavin adenine dinucleotide in neutral solutions." Canadian Journal of Chemistry 66, no. 1 (1988): 86–96. http://dx.doi.org/10.1139/v88-013.

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A detailed investigation of the electrochemical behavior of flavin adenine dinucleotide (FAD) in neutral solutions has been carried out at Hg and glassy carbon electrodes. At FAD concentrations of about 10−4 M, cyclic voltammetry (CV) shows a pair of anodic and cathodic peaks having a peak separation at low sweep rates indicative of a two-electron transfer process and yielding a formal redox potential for FAD of −0.206 ± 0.003 V vs. NHE at pH 7. Evidence for FAD adsorption was obtained in experiments at high sweep rates, from the effect of time of exposure of the electrode surface to FAD in so

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2

Mondal, Padmabati, and Miquel Huix-Rotllant. "Theoretical insights into the formation and stability of radical oxygen species in cryptochromes." Physical Chemistry Chemical Physics 21, no. 17 (2019): 8874–82. http://dx.doi.org/10.1039/c9cp00782b.

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3

van Schie, Morten M. C. H., Caroline E. Paul, Isabel W. C. E. Arends, and Frank Hollmann. "Photoenzymatic epoxidation of styrenes." Chemical Communications 55, no. 12 (2019): 1790–92. http://dx.doi.org/10.1039/c8cc08149b.

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4

Wu, M., B. Repetto, D. M. Glerum, and A. Tzagoloff. "Cloning and characterization of FAD1, the structural gene for flavin adenine dinucleotide synthetase of Saccharomyces cerevisiae." Molecular and Cellular Biology 15, no. 1 (1995): 264–71. http://dx.doi.org/10.1128/mcb.15.1.264.

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The FAD1 gene of Saccharomyces cerevisiae has been selected from a genomic library on the basis of its ability to partially correct the respiratory defect of pet mutants previously assigned to complementation group G178. Mutants in this group display a reduced level of flavin adenine dinucleotide (FAD) and an increased level of flavin mononucleotide (FMN) in mitochondria. The restoration of respiratory capability by FAD1 is shown to be due to extragenic suppression. FAD1 codes for an essential yeast protein, since disruption of the gene induces a lethal phenotype. The FAD1 product has been inf

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5

Kieninger, Martina, Oscar N. Ventura, and Tilman Kottke. "Calculation of the Geometries and Infrared Spectra of the Stacked Cofactor Flavin Adenine Dinucleotide (FAD) as the Prerequisite for Studies of Light-Triggered Proton and Electron Transfer." Biomolecules 10, no. 4 (2020): 573. http://dx.doi.org/10.3390/biom10040573.

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Flavin cofactors, like flavin adenine dinucleotide (FAD), are important electron shuttles in living systems. They catalyze a wide range of one- or two-electron redox reactions. Experimental investigations include UV-vis as well as infrared spectroscopy. FAD in aqueous solution exhibits a significantly shorter excited state lifetime than its analog, the flavin mononucleotide. This finding is explained by the presence of a “stacked” FAD conformation, in which isoalloxazine and adenine moieties form a π-complex. Stacking of the isoalloxazine and adenine rings should have an influence on the frequ

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6

Li, Meng-Yin, Ya-Qian Wang, Yi-Lun Ying, and Yi-Tao Long. "Revealing the transient conformations of a single flavin adenine dinucleotide using an aerolysin nanopore." Chemical Science 10, no. 44 (2019): 10400–10404. http://dx.doi.org/10.1039/c9sc03163d.

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7

Wang, Yan, Min Sun, Jinping Qiao, Jin Ouyang, and Na Na. "FAD roles in glucose catalytic oxidation studied by multiphase flow of extractive electrospray ionization (MF-EESI) mass spectrometry." Chemical Science 9, no. 3 (2018): 594–99. http://dx.doi.org/10.1039/c7sc04259k.

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8

Matern, Andreas, Danielle Pedrolli, Stephanie Großhennig, Jörgen Johansson, and Matthias Mack. "Uptake and Metabolism of Antibiotics Roseoflavin and 8-Demethyl-8-Aminoriboflavin in Riboflavin-Auxotrophic Listeria monocytogenes." Journal of Bacteriology 198, no. 23 (2016): 3233–43. http://dx.doi.org/10.1128/jb.00388-16.

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ABSTRACTThe riboflavin analogs roseoflavin (RoF) and 8-demethyl-8-aminoriboflavin (AF) are produced by the bacteriaStreptomyces davawensisandStreptomyces cinnabarinus. Riboflavin analogs have the potential to be used as broad-spectrum antibiotics, and we therefore studied the metabolism of riboflavin (vitamin B2), RoF, and AF in the human pathogenListeria monocytogenes, a bacterium which is a riboflavin auxotroph. We show that theL. monocytogenesprotein Lmo1945 is responsible for the uptake of riboflavin, RoF, and AF. Following import, these flavins are phosphorylated/adenylylated by the bifun

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9

Giancaspero, Teresa Anna, Vittoria Locato, and Maria Barile. "A Regulatory Role of NAD Redox Status on Flavin Cofactor Homeostasis inS. cerevisiaeMitochondria." Oxidative Medicine and Cellular Longevity 2013 (2013): 1–16. http://dx.doi.org/10.1155/2013/612784.

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Flavin adenine dinucleotide (FAD) and nicotinamide adenine dinucleotide (NAD) are two redox cofactors of pivotal importance for mitochondrial functionality and cellular redox balance. Despite their relevance, the mechanism by which intramitochondrial NAD(H) and FAD levels are maintained remains quite unclear inSaccharomyces cerevisiae. We investigated here the ability of isolated mitochondria to degrade externally added FAD and NAD (in both its reduced and oxidized forms). A set of kinetic experiments demonstrated that mitochondrial FAD and NAD(H) destroying enzymes are different from each oth

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10

Zhukov, Ivan V., Alexey S. Kiryutin, Mikhail S. Panov, et al. "Exchange interaction in short-lived flavine adenine dinucleotide biradical in aqueous solution revisited by CIDNP (chemically induced dynamic nuclear polarization) and nuclear magnetic relaxation dispersion." Magnetic Resonance 2, no. 1 (2021): 139–48. http://dx.doi.org/10.5194/mr-2-139-2021.

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Abstract. Flavin adenine dinucleotide (FAD) is an important cofactor in many light-sensitive enzymes. The role of the adenine moiety of FAD in light-induced electron transfer was obscured, because it involves an adenine radical, which is short-lived with a weak chromophore. However, an intramolecular electron transfer from adenine to flavin was revealed several years ago by Robert Kaptein by using chemically induced dynamic nuclear polarization (CIDNP). The question of whether one or two types of biradicals of FAD in aqueous solution are formed stays unresolved so far. In the present work, we

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11

Moon, Shin, and Choe. "Crystal Structures of Putative Flavin Dependent Monooxygenase from Alicyclobacillus Acidocaldarius." Crystals 9, no. 11 (2019): 548. http://dx.doi.org/10.3390/cryst9110548.

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Flavin dependent monooxygenases catalyze various reactions to play a key role in biological processes, such as catabolism, detoxification, and biosynthesis. Group D flavin dependent monooxygenases are enzymes with an Acyl-CoA dehydrogenase (ACAD) fold and use Flavin adenine dinucleotide (FAD) or Flavin mononucleotide (FMN) as a cofactor. In this research, crystal structures of Alicyclobacillus acidocaldarius protein formerly annotated as an ACAD were determined in Apo and FAD bound state. Although our structure showed high structural similarity to other ACADs, close comparison of substrate bin

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12

Kalinina, Sviatlana, Christian Freymueller, Nilanjon Naskar, et al. "Bioenergetic Alterations of Metabolic Redox Coenzymes as NADH, FAD and FMN by Means of Fluorescence Lifetime Imaging Techniques." International Journal of Molecular Sciences 22, no. 11 (2021): 5952. http://dx.doi.org/10.3390/ijms22115952.

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Metabolic FLIM (fluorescence lifetime imaging) is used to image bioenergetic status in cells and tissue. Whereas an attribution of the fluorescence lifetime of coenzymes as an indicator for cell metabolism is mainly accepted, it is debated whether this is valid for the redox state of cells. In this regard, an innovative algorithm using the lifetime characteristics of nicotinamide adenine dinucleotide (phosphate) (NAD(P)H) and flavin adenine dinucleotide (FAD) to calculate the fluorescence lifetime induced redox ratio (FLIRR) has been reported so far. We extended the FLIRR approach and present

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13

Zhou, Li, Yawei Kong, Junxin Wu, et al. "Metabolic Changes in Maternal and Cord Blood in One Case of Pregnancy-Associated Breast Cancer Seen by Fluorescence Lifetime Imaging Microscopy." Diagnostics 11, no. 8 (2021): 1494. http://dx.doi.org/10.3390/diagnostics11081494.

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Pregnancy-associated breast cancer (PABC) is a rare disease, which is frequently diagnosed at an advanced stage due to limitations in current diagnostic methods. In this study, fluorescence lifetime imaging microscopy (FLIM) was used to study the metabolic changes by measuring maternal blood and umbilical cord blood via the autofluorescence of coenzymes, reduced nicotinamide adenine dinucleotide (phosphate) (NAD(P)H), and flavin adenine dinucleotide (FAD). The NAD(P)H data showed that a PABC case had significant differences compared with normal cases, which may indicate increased glycolysis. T

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14

Shi, Rong, Magda Villarroya, Rafael Ruiz-Partida, et al. "Structure-Function Analysis of Escherichia coli MnmG (GidA), a Highly Conserved tRNA-Modifying Enzyme." Journal of Bacteriology 191, no. 24 (2009): 7614–19. http://dx.doi.org/10.1128/jb.00650-09.

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ABSTRACT The MnmE-MnmG complex is involved in tRNA modification. We have determined the crystal structure of Escherichia coli MnmG at 2.4-Å resolution, mutated highly conserved residues with putative roles in flavin adenine dinucleotide (FAD) or tRNA binding and MnmE interaction, and analyzed the effects of these mutations in vivo and in vitro. Limited trypsinolysis of MnmG suggests significant conformational changes upon FAD binding.

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15

Berndt, Nikolaus, Richard Kovács, Jörg Rösner, Iwona Wallach, Jens P. Dreier, and Agustin Liotta. "Flavin Adenine Dinucleotide Fluorescence as an Early Marker of Mitochondrial Impairment During Brain Hypoxia." International Journal of Molecular Sciences 21, no. 11 (2020): 3977. http://dx.doi.org/10.3390/ijms21113977.

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Multimodal continuous bedside monitoring is increasingly recognized as a promising option for early treatment stratification in patients at risk for ischemia during neurocritical care. Modalities used at present are, for example, oxygen availability and subdural electrocorticography. The assessment of mitochondrial function could be an interesting complement to these modalities. For instance, flavin adenine dinucleotide (FAD) fluorescence permits direct insight into the mitochondrial redox state. Therefore, we explored the possibility of using FAD fluorometry to monitor consequences of hypoxia

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16

Mayeno, Arthur N., Kimm J. Hamann, and Gerald J. Gleich. "Granule-associated flavin adenine dinucleotide (FAD) is responsible for eosinophil autofluorescence." Journal of Leukocyte Biology 51, no. 2 (1992): 172–75. http://dx.doi.org/10.1002/jlb.51.2.172.

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17

Краснопевцева, М. К., В. П. Белик, А. А. Богданов, И. В. Семенова, А. Г. Смолин та О. С. Васютинский. "Определение времен затухания и анизотропии поляризованной флуоресценции флавинадениндинуклеотида с субнаносекундным разрешением". Письма в журнал технической физики 46, № 12 (2020): 43. http://dx.doi.org/10.21883/pjtf.2020.12.49528.18234.

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Optical properties of the biological coenzyme flavin adenine dinucleotide (FAD) in an aqueous solution were investigated. The time-resolved decay of polarized fluorescence excited by picosecond laser pulses provided data on two fluorescence lifetimes, rotational diffusion time and anisotropy parameter. The results obtained are compared with those obtained by other researchers.

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18

Hustad, Steinar, Michelle C. McKinley, Helene McNulty, et al. "Riboflavin, Flavin Mononucleotide, and Flavin Adenine Dinucleotide in Human Plasma and Erythrocytes at Baseline and after Low-Dose Riboflavin Supplementation." Clinical Chemistry 48, no. 9 (2002): 1571–77. http://dx.doi.org/10.1093/clinchem/48.9.1571.

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Abstract Background: Vitamin B2 exists in blood as riboflavin and its cofactors, flavin mononucleotide (FMN) and FAD. The erythrocyte glutathione reductase activation coefficient (EGRAC) has traditionally been used to assess vitamin B2 status in humans. We investigated the relationships of EGRAC and plasma and erythrocyte concentrations of riboflavin, FMN, and FAD in elderly volunteers and their responses to riboflavin administration. Methods: EGRAC and plasma and erythrocyte concentrations of riboflavin, FMN, and FAD were determined in 124 healthy individuals with a mean age of 69 years. The

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19

Heine, Thomas, Willem van Berkel, George Gassner, Karl-Heinz van Pée, and Dirk Tischler. "Two-Component FAD-Dependent Monooxygenases: Current Knowledge and Biotechnological Opportunities." Biology 7, no. 3 (2018): 42. http://dx.doi.org/10.3390/biology7030042.

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Flavoprotein monooxygenases create valuable compounds that are of high interest for the chemical, pharmaceutical, and agrochemical industries, among others. Monooxygenases that use flavin as cofactor are either single- or two-component systems. Here we summarize the current knowledge about two-component flavin adenine dinucleotide (FAD)-dependent monooxygenases and describe their biotechnological relevance. Two-component FAD-dependent monooxygenases catalyze hydroxylation, epoxidation, and halogenation reactions and are physiologically involved in amino acid metabolism, mineralization of aroma

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20

Mack, Matthias, Adolphus P. G. M. van Loon, and Hans-Peter Hohmann. "Regulation of Riboflavin Biosynthesis inBacillus subtilis Is Affected by the Activity of the Flavokinase/Flavin Adenine Dinucleotide Synthetase Encoded byribC." Journal of Bacteriology 180, no. 4 (1998): 950–55. http://dx.doi.org/10.1128/jb.180.4.950-955.1998.

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ABSTRACT This work shows that the ribC wild-type gene product has both flavokinase and flavin adenine dinucleotide synthetase (FAD-synthetase) activities. RibC plays an essential role in the flavin metabolism of Bacillus subtilis, as growth of aribC deletion mutant strain was dependent on exogenous supply of FMN and the presence of a heterologous FAD-synthetase gene in its chromosome. Upon cultivation with growth-limiting amounts of FMN, this ribC deletion mutant strain overproduced riboflavin, while with elevated amounts of FMN in the culture medium, no riboflavin overproduction was observed.

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21

Lu, Chih-Hao, Chin-Sheng Yu, Yu-Feng Lin, and Jin-Yi Chen. "Predicting Flavin and Nicotinamide Adenine Dinucleotide-Binding Sites in Proteins Using the Fragment Transformation Method." BioMed Research International 2015 (2015): 1–13. http://dx.doi.org/10.1155/2015/402536.

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We developed a computational method to identify NAD- and FAD-binding sites in proteins. First, we extracted from the Protein Data Bank structures of proteins that bind to at least one of these ligands. NAD-/FAD-binding residue templates were then constructed by identifying binding residues through the ligand-binding database BioLiP. The fragment transformation method was used to identify structures within query proteins that resembled the ligand-binding templates. By comparing residue types and their relative spatial positions, potential binding sites were identified and a ligand-binding poten

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22

Smelt, M. J., M. M. Faas, B. J. de Haan, and P. de Vos. "Pancreatic Beta-Cell Purification by Altering FAD and NAD(P)H Metabolism." Experimental Diabetes Research 2008 (2008): 1–11. http://dx.doi.org/10.1155/2008/165360.

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Isolation of primary beta cells from other cells within in the pancreatic islets is of importance for many fields of islet research. However, up to now, no satisfactory method has been developed that gained high numbers of viable beta cells, without considerable alpha-cell contamination. In this study, we investigated whether rat beta cells can be isolated from nonbeta endocrine cells by manipulating the flavin adenine dinucleotide (FAD) and nicotinamide-adenine dinucleotide phosphate (NAD(P)H) autofluorescence. Beta cells were isolated from dispersed islets by flow cytometry, based on their h

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23

Liang, E. J., D. Göttges, and W. Kiefer. "Surface-Enhanced Resonance Raman Spectroscopy of Flavins on Silver Nitrate-Modified Cu and Fe as Well as Cu-Zn-Pb and Fe-C-Cr-Ni Surfaces." Applied Spectroscopy 48, no. 9 (1994): 1088–94. http://dx.doi.org/10.1366/0003702944029451.

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Surface-enhanced resonance Raman spectroscopy (SERRS) of riboflavin, flavin adenine dinucleotide (FAD), and flavin mononucleotide (FMN) on Cu, Cu-Zn-Pb, and Fe as well as Fe-C-Cr-Ni has been performed by means of the modification of these substrates with silver nitrate. It is found that the SERR spectrum of a flavin molecule on the alloy Cu-Zn-Pb is different from that on the pure Cu, and this is also the case for a flavin molecule on the alloy Fe-C-Cr-Ni and on pure Fe. This result indicates possibly that Zn, rather than Cu, and Ni or Cr, rather than Fe, in the alloys also interact with the f

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Wei, Haizhen, and Sasha Omanovic. "Interaction of Flavin Adenine Dinucleotide (FAD) with a Glassy Carbon Electrode Surface." Chemistry & Biodiversity 5, no. 8 (2008): 1622–39. http://dx.doi.org/10.1002/cbdv.200890150.

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25

Serra, Stefano, Davide De Simeis, Stefano Marzorati, and Mattia Valentino. "Oleate Hydratase from Lactobacillus rhamnosus ATCC 53103: A FADH2-Dependent Enzyme with Remarkable Industrial Potential." Catalysts 11, no. 9 (2021): 1051. http://dx.doi.org/10.3390/catal11091051.

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Recently, we described the preparation of the recombinant oleate hydratase from Lactobacillus rhamnosus ATCC 53103. We observed that the purified C-terminal His-tagged enzyme was completely inactive and the catalytic activity was partially restored only in presence of a large amount of flavin adenine dinucleotide (FAD). In the present work, we assess that this hydratase in the presence of the reduced form of flavin adenine dinucleotide (FADH2) is at least one hundred times as active as in the presence of the same concentration of FAD. By means of two different biochemical processes, we demonst

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26

Grill, Simon, Simone Busenbender, Matthias Pfeiffer, Uwe Köhler, and Matthias Mack. "The Bifunctional Flavokinase/Flavin Adenine Dinucleotide Synthetase from Streptomyces davawensis Produces Inactive Flavin Cofactors and Is Not Involved in Resistance to the Antibiotic Roseoflavin." Journal of Bacteriology 190, no. 5 (2007): 1546–53. http://dx.doi.org/10.1128/jb.01586-07.

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ABSTRACT Streptomyces davawensis synthesizes the antibiotic roseoflavin, one of the few known natural riboflavin analogs, and is roseoflavin resistant. It is thought that the endogenous flavokinase (EC 2.7.1.26)/flavin adenine dinucleotide (FAD) synthetase (EC 2.7.7.2) activities of roseoflavin-sensitive organisms are responsible for the antibiotic effect of roseoflavin, producing the inactive cofactors roseoflavin-5′-monophosphate (RoFMN) and roseoflavin adenine dinucleotide (RoFAD) from roseoflavin. To confirm this, the FAD-dependent Sus scrofa d-amino acid oxidase (EC 1.4.3.3) was tested wi

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Sharma, Sunny, Ewa Grudzien-Nogalska, Keith Hamilton, et al. "Mammalian Nudix proteins cleave nucleotide metabolite caps on RNAs." Nucleic Acids Research 48, no. 12 (2020): 6788–98. http://dx.doi.org/10.1093/nar/gkaa402.

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Abstract We recently reported the presence of nicotinamide adenine dinucleotide (NAD)-capped RNAs in mammalian cells and a role for DXO and the Nudix hydrolase Nudt12 in decapping NAD-capped RNAs (deNADding) in cells. Analysis of 5′caps has revealed that in addition to NAD, mammalian RNAs also contain other metabolite caps including flavin adenine dinucleotide (FAD) and dephosphoCoA (dpCoA). In the present study we systematically screened all mammalian Nudix proteins for their potential deNADing, FAD cap decapping (deFADding) and dpCoA cap decapping (deCoAping) activity. We demonstrate that Nu

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28

Wu, Binlin, Xin Gao, and Jason Smith. "Optical Biopsy for Prostate Cancer Diagnosis Using Fluorescence Spectroscopy." International Journal of High Speed Electronics and Systems 27, no. 03n04 (2018): 1840026. http://dx.doi.org/10.1142/s0129156418400268.

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Native fluorescence spectra are acquired from fresh normal and cancerous human prostate tissues. The fluorescence data are analyzed using an unsupervised machine learning algorithm such as non-negative matrix factorization. The nonnegative spectral components are retrieved and attributed to the native fluorophores such as collagen, reduced nicotinamide adenine dinucleotide (NADH), and flavin adenine dinucleotide (FAD) in tissue. The retrieved scores of the components are used to estimate the relative concentrations of the native fluorophores such as NADH and FAD and the redox ratio. A supervis

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29

Huang, Maojia, Zixiao Zhang, Xinyi Wang, et al. "Detecting benign uterine tumors by autofluorescence lifetime imaging microscopy through adjacent healthy cervical tissues." Journal of Innovative Optical Health Sciences 12, no. 05 (2019): 1940006. http://dx.doi.org/10.1142/s1793545819400066.

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The endogenous fluorophores such as reduced nicotinamide adenine dinucleotide (phosphate) (NAD(P)H) and flavin adenine dinucleotide (FAD) in cells and tissues can be imaged by fluorescence lifetime imaging microscopy (FLIM) to show the tissue morphology features, as well as the biomolecular changes in microenvironment. The two important coenzymes in cellular metabolism, NAD(P)H and FAD, can be used to monitor the cellular metabolic status. This work proposed a novel method to study the uterine metabolism at the adjacent site of healthy cervix. It was found that the benign uterine tumors such a

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Škodová, Ingrid, Zdeněk Verner, Fréderic Bringaud, Peter Fabian, Julius Lukeš, and Anton Horváth. "Characterization of Two Mitochondrial Flavin Adenine Dinucleotide-Dependent Glycerol-3-Phosphate Dehydrogenases in Trypanosoma brucei." Eukaryotic Cell 12, no. 12 (2013): 1664–73. http://dx.doi.org/10.1128/ec.00152-13.

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ABSTRACT Glycerol-3-phosphate dehydrogenases (G3PDHs) constitute a shuttle that serves for regeneration of NAD + reduced during glycolysis. This NAD-dependent enzyme is employed in glycolysis and produces glycerol-3-phosphate from dihydroxyacetone phosphate, while its flavin adenine dinucleotide (FAD)-dependent homologue catalyzes a reverse reaction coupled to the respiratory chain. Trypanosoma brucei possesses two FAD-dependent G3PDHs. While one of them (mitochondrial G3PDH [mtG3PDH]) has been attributed to the mitochondrion and seems to be directly involved in G3PDH shuttle reactions, the fu

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Wang, Wei-Jun, Jing-Quan Huang, Chong Yang, Jiu-Jiu Huang, and Ming-Qi Li. "The Recognition of Glycolate Oxidase Apoprotein with Flavin Analogs in Higher Plants." Acta Biochimica et Biophysica Sinica 36, no. 4 (2004): 290–96. http://dx.doi.org/10.1093/abbs/36.4.290.

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Abstract The dependence of glycolate oxidase apoprotein (apoGO) activity on flavin analogs was surveyed in 9 higher plants from 7 families. Activities of all apoGOs depended not only on flavin mononucleotide (FMN) but also on flavin adenine dinucleotide (FAD), but not on riboflavin. The kinetic analysis showed that FMN was the optimum cofactor for apoGO from leaves of Brassica campestris. In plant kingdom, FMN, FAD and riboflavin are three flavin analogs with very similar structure, and they could coexist and be inter-converted from each other, so the question is how the apoprotein of glycolat

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32

Gaweska, Helena, and Paul F. Fitzpatrick. "Structures and mechanism of the monoamine oxidase family." BioMolecular Concepts 2, no. 5 (2011): 365–77. http://dx.doi.org/10.1515/bmc.2011.030.

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AbstractMembers of the monoamine oxidase family of flavoproteins catalyze the oxidation of primary and secondary amines, polyamines, amino acids, and methylated lysine side chains in proteins. The enzymes have similar overall structures, with conserved flavin adenine dinucleotide (FAD)-binding domains and varied substrate-binding sites. Multiple mechanisms have been proposed for the catalytic reactions of these enzymes. The present review compares the structures of different members of the family and the various mechanistic proposals.

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33

Gisi, Michelle R., and Luying Xun. "Characterization of Chlorophenol 4-Monooxygenase (TftD) and NADH:Flavin Adenine Dinucleotide Oxidoreductase (TftC) of Burkholderia cepacia AC1100." Journal of Bacteriology 185, no. 9 (2003): 2786–92. http://dx.doi.org/10.1128/jb.185.9.2786-2792.2003.

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ABSTRACT Burkholderia cepacia AC1100 uses 2,4,5-trichlorophenoxyacetic acid, an environmental pollutant, as a sole carbon and energy source. Chlorophenol 4-monooxygenase is a key enzyme in the degradation of 2,4,5-trichlorophenoxyacetic acid, and it was originally characterized as a two-component enzyme (TftC and TftD). Sequence analysis suggests that they are separate enzymes. The two proteins were separately produced in Escherichia coli, purified, and characterized. TftC was an NADH:flavin adenine dinucleotide (FAD) oxidoreductase. A C-terminally His-tagged fusion TftC used NADH to reduce ei

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34

Eggerichs, Daniel, Carolin Mügge, Julia Mayweg, Ulf-Peter Apfel, and Dirk Tischler. "Enantioselective Epoxidation by Flavoprotein Monooxygenases Supported by Organic Solvents." Catalysts 10, no. 5 (2020): 568. http://dx.doi.org/10.3390/catal10050568.

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Styrene and indole monooxygenases (SMO and IMO) are two-component flavoprotein monooxygenases composed of a nicotinamide adenine dinucleotide (NADH)-dependent flavin adenine dinucleotide (FAD)-reductase (StyB or IndB) and a monooxygenase (StyA or IndA). The latter uses reduced FAD to activate oxygen and to oxygenate the substrate while releasing water. We circumvented the need for the reductase by direct FAD reduction in solution using the NAD(P)H-mimic 1-benzyl-1,4-dihydronicotinamide (BNAH) to fuel monooxygenases without NADH requirement. Herein, we report on the hitherto unknown solvent tol

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Lee, Alpha A., Jason C. S. Lau, Hannah J. Hogben, Till Biskup, Daniel R. Kattnig, and P. J. Hore. "Alternative radical pairs for cryptochrome-based magnetoreception." Journal of The Royal Society Interface 11, no. 95 (2014): 20131063. http://dx.doi.org/10.1098/rsif.2013.1063.

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There is growing evidence that the remarkable ability of animals, in particular birds, to sense the direction of the Earth's magnetic field relies on magnetically sensitive photochemical reactions of the protein cryptochrome. It is generally assumed that the magnetic field acts on the radical pair [FAD •− TrpH • + ] formed by the transfer of an electron from a group of three tryptophan residues to the photo-excited flavin adenine dinucleotide cofactor within the protein. Here, we examine the suitability of an [FAD •− Z • ] radical pair as a compass magnetoreceptor, where Z • is a radical in wh

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Nagarajan, Ramila D., Preethika Murugan, Kanagaraj Palaniyandi, Raji Atchudan, and Ashok K. Sundramoorthy. "Biocompatible MXene (Ti3C2Tx) Immobilized with Flavin Adenine Dinucleotide as an Electrochemical Transducer for Hydrogen Peroxide Detection in Ovarian Cancer Cell Lines." Micromachines 12, no. 8 (2021): 862. http://dx.doi.org/10.3390/mi12080862.

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Flavin adenine dinucleotide (FAD) is a coenzyme and acts as a redox cofactor in metabolic process. Owing to such problems as poor electron transfer properties, unfavorable adsorption, and lack of stability on rigid electrodes, the bio-electrochemical applications of FAD have been limited. Herein, a novel fabrication method was developed for the immobilization process using 2D MXene (Ti3C2Tx), which enhanced the redox property of FAD and improved the electro-catalytic reduction of hydrogen peroxide (H2O2) in neutral medium. The FAD-immobilized Ti3C2Tx electrode (FAD/Ti3C2Tx) was studied by UV-V

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Sengupta, Abhigyan, Krishna Gavvala, Raj Kumar Koninti, Haribandhu Chaudhuri, and Partha Hazra. "Folding dynamics of flavin adenine dinucleotide (FAD) inside non-aqueous and aqueous reverse micelles." Chemical Physics Letters 584 (October 2013): 67–73. http://dx.doi.org/10.1016/j.cplett.2013.08.028.

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Esmaeili, Sajjad, Maryam Amoushahi, Hamzeh Barati, Mohabbat Ansari та Soodabeh Shafiee. "Anti-Diabetic Potential of Anti-Oxidant Compounds "Riboflavin, Flavin Mononucleotide and Flavin Adenine Dinucleotide" with High Therapeutic Potency through Inhibition of α-Amylase and α-Glucosidase Enzymes at Sub-Micromolar Concentrations". SDRP Journal of Food Science & Technology 5, № 3 (2020): 146–61. http://dx.doi.org/10.25177/jfst.5.3.ra.10638.

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Diabetes is a group of metabolic disorders characterized by a high blood sugar level over a prolonged period of time. Inhibition of carbohydrate hydrolyzing enzymes leads to decrease in the absorption of glucose which is considered as one of the effective managements of diabetes mellitus. Vegetable, fruit, milk, and fish are good sources of riboflavin (RF) and vitamin B5 with versatile health benefits. The well-adapted structural features of these compounds for the inhibition/activation of enzymes include several available hydrogen bond (H-bond) acceptors and donors, flexible backbone, and hyd

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Schall, Patrick, Lucas Marutschke, and Bernhard Grimm. "The Flavoproteome of the Model Plant Arabidopsis thaliana." International Journal of Molecular Sciences 21, no. 15 (2020): 5371. http://dx.doi.org/10.3390/ijms21155371.

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Flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) are essential cofactors for enzymes, which catalyze a broad spectrum of vital reactions. This paper intends to compile all potential FAD/FMN-binding proteins encoded by the genome of Arabidopsis thaliana. Several computational approaches were applied to group the entire flavoproteome according to (i) different catalytic reactions in enzyme classes, (ii) the localization in subcellular compartments, (iii) different protein families and subclasses, and (iv) their classification to structural properties. Subsequently, the physiolog

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Moritzer, Ann-Christin, Tina Prior, and Hartmut H. Niemann. "Not Cleaving the His-tag of Thal Results in More Tightly Packed and Better-Diffracting Crystals." Crystals 10, no. 12 (2020): 1135. http://dx.doi.org/10.3390/cryst10121135.

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Flavin-dependent halogenases chlorinate or brominate their substrates in an environmentally friendly manner, only requiring the cofactor reduced flavin adenine dinucleotide (FADH2), oxygen, and halide salts. The tryptophan 6-halogenase Thal exhibits two flexible loops, which become ordered (substrate-binding loop) or adopt a closed conformation (FAD loop) upon substrate or cofactor binding. Here, we describe the structure of NHis-Thal-RebH5 containing an N-terminal His-tag from pET28a, which crystallized in a different space group (P21) and, surprisingly, diffracted to a higher resolution of 1

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Kuppuraj, Gopi, Fumiko Suzuki, Masahiko Ikeuchi, and Kei Yura. "3P050 Structural insights into enzyme-bound flavin adenine dinucleotides (FAD)(01A. Protein: Structure,Poster)." Seibutsu Butsuri 53, supplement1-2 (2013): S220. http://dx.doi.org/10.2142/biophys.53.s220_2.

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Bowles, Timothy, Audrey H. Metz, Jami O'Quin, Zdzislaw Wawrzak, and Brandt F. Eichman. "Structure and DNA binding of alkylation response protein AidB." Proceedings of the National Academy of Sciences 105, no. 40 (2008): 15299–304. http://dx.doi.org/10.1073/pnas.0806521105.

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Exposure of Escherichia coli to alkylating agents activates expression of AidB in addition to DNA repair proteins Ada, AlkA, and AlkB. AidB was recently shown to possess a flavin adenine dinucleotide (FAD) cofactor and to bind to dsDNA, implicating it as a flavin-dependent DNA repair enzyme. However, the molecular mechanism by which AidB acts to reduce the mutagenic effects of specific DNA alkylators is unknown. We present a 1.7-Å crystal structure of AidB, which bears superficial resemblance to the acyl-CoA dehydrogenase superfamily of flavoproteins. The structure reveals a unique quaternary

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Buey, Rubén, Ruth Schmitz, Bob Buchanan, and Monica Balsera. "Crystal Structure of the Apo-Form of NADPH-Dependent Thioredoxin Reductase from a Methane-Producing Archaeon." Antioxidants 7, no. 11 (2018): 166. http://dx.doi.org/10.3390/antiox7110166.

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The redox regulation of proteins via reversible dithiol/disulfide exchange reactions involves the thioredoxin system, which is composed of a reductant, a thioredoxin reductase (TR), and thioredoxin (Trx). In the pyridine nucleotide-dependent Trx reduction pathway, reducing equivalents, typically from reduced nicotinamide adenine dinucleotide phosphate (NADPH), are transferred from NADPH-TR (NTR) to Trx and, in turn, to target proteins, thus resulting in the reversible modification of the structural and functional properties of the targets. NTR enzymes contain three functional sites: an NADPH b

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Baitsch, Daniel, Cristinel Sandu, Roderich Brandsch, and Gabor L. Igloi. "Gene Cluster on pAO1 of Arthrobacter nicotinovorans Involved in Degradation of the Plant Alkaloid Nicotine: Cloning, Purification, and Characterization of 2,6-Dihydroxypyridine 3-Hydroxylase." Journal of Bacteriology 183, no. 18 (2001): 5262–67. http://dx.doi.org/10.1128/jb.183.18.5262-5267.2001.

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ABSTRACT A 27,690-bp gene cluster involved in the degradation of the plant alkaloid nicotine was characterized from the plasmid pAO1 ofArthrobacter nicotinovorans. The genes of the heterotrimeric, molybdopterin cofactor (MoCo)-, flavin adenine dinucleotide (FAD)-, and [Fe-S] cluster-dependent 6-hydroxypseudooxynicotine (ketone) dehydrogenase (KDH) were identified within this cluster. The gene of the large MoCo subunit of KDH was located 4,266 bp from the FAD and [Fe-S] cluster subunit genes. Deduced functions of proteins encoded by open reading frames (ORFs) of the cluster were correlated to i

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Otto, Katja, Karin Hofstetter, Martina Röthlisberger, Bernard Witholt, and Andreas Schmid. "Biochemical Characterization of StyAB from Pseudomonas sp. Strain VLB120 as a Two-Component Flavin-Diffusible Monooxygenase." Journal of Bacteriology 186, no. 16 (2004): 5292–302. http://dx.doi.org/10.1128/jb.186.16.5292-5302.2004.

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ABSTRACT Pseudomonas sp. VLB120 uses styrene as a sole source of carbon and energy. The first step in this metabolic pathway is catalyzed by an oxygenase (StyA) and a NADH-flavin oxidoreductase (StyB). Both components have been isolated from wild-type Pseudomonas strain VLB120 as well as from recombinant Escherichia coli. StyA from both sources is a dimer, with a subunit size of 47 kDa, and catalyzes the enantioselective epoxidation of C═C double bonds. Styrene is exclusively converted to S-styrene oxide with a specific activity of 2.1 U mg−1 (k cat = 1.6 s−1) and Km values for styrene of 0.45

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Beneš, Martin, Jiří Hudeček, Pavel Anzenbacher, and Martin Hof. "Coumarin 6, Hypericin, Resorufins, and Flavins: Suitable Chromophores for Fluorescence Correlation Spectroscopy of Biological Molecules." Collection of Czechoslovak Chemical Communications 66, no. 6 (2001): 855–69. http://dx.doi.org/10.1135/cccc20010855.

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In this work we show that the dyes coumarin 6, hypericin, 7-O-ethylresorufin and resorufin are suitable for fluorescence correlation spectroscopy (FCS) and demonstrate the use of these dyes in physiologically relevant protein studies. Since coumarins are metabolised by cytochromes P450, the binding of coumarin 6 to cytochrome P450 3A4 was investigated by FCS. Coumarin 6 appears to be a very bright non-covalent cytochrome P450 label. When titrating cytochrome P450 3A4 with coumarin 6, the diffusion time of the coumarin 6/ cytochrome P450 3A4 complex increases roughly two-fold at protein concent

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Lee, Jung-Kul, and Huimin Zhao. "Identification and Characterization of the Flavin:NADH Reductase (PrnF) Involved in a Novel Two-Component Arylamine Oxygenase." Journal of Bacteriology 189, no. 23 (2007): 8556–63. http://dx.doi.org/10.1128/jb.01050-07.

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ABSTRACT Two-component oxygenases catalyze a wide variety of important oxidation reactions. Recently we characterized a novel arylamine N-oxygenase (PrnD), a new member of the two-component oxygenase family (J. Lee et al., J. Biol. Chem. 280:36719-36728, 2005). Although arylamine N-oxygenases are widespread in nature, aminopyrrolnitrin N-oxygenase (PrnD) represents the only biochemically and mechanistically characterized arylamine N-oxygenase to date. Here we report the use of bioinformatic and biochemical tools to identify and characterize the reductase component (PrnF) involved in the PrnD-c

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Mewies, Martin, William S. McIntire, and Nigel S. Scrutton. "Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: The current state of affairs." Protein Science 7, no. 1 (1998): 7–20. http://dx.doi.org/10.1002/pro.5560070102.

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Hustad, Steinar, Per Magne Ueland, and Jørn Schneede. "Quantification of Riboflavin, Flavin Mononucleotide, and Flavin Adenine Dinucleotide in Human Plasma by Capillary Electrophoresis and Laser-induced Fluorescence Detection." Clinical Chemistry 45, no. 6 (1999): 862–68. http://dx.doi.org/10.1093/clinchem/45.6.862.

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Abstract Background: Riboflavin is the precursor of flavin mononucleotide (FMN) and FAD, which serve as cofactors for several redox enzymes. We have developed a capillary electrophoresis method for the determination of riboflavin and its two coenzyme forms in human plasma. Methods: Trichloroacetic acid-treated plasma was subjected to solid-phase extraction on reversed-phase columns. The analytes were separated by micellar electrokinetic capillary chromatography in uncoated fused- silica capillaries filled with borate buffer containing 50 mmol/L sodium dodecyl sulfate, methanol, and N-methylfor

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Wang, Yingjie, Gianluigi Veglia, Dongping Zhong, and Jiali Gao. "Activation mechanism of Drosophila cryptochrome through an allosteric switch." Science Advances 7, no. 25 (2021): eabg3815. http://dx.doi.org/10.1126/sciadv.abg3815.

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Cryptochromes are signaling proteins activated by photoexcitation of the flavin adenine dinucleotide (FAD) cofactor. Although extensive research has been performed, the mechanism for this allosteric process is still unknown. We constructed three computational models, corresponding to different redox states of the FAD cofactor in Drosophila cryptochrome (dCRY). Analyses of the dynamics trajectories reveal that the activation process occurs in the semiquinone state FAD−●, resulting from excited-state electron transfer. The Arg381-Asp410 salt bridge acts as an allosteric switch, regulated by the

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