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Journal articles on the topic 'Hemeprotein'

Author: Grafiati

Published: 4 June 2021

Last updated: 14 February 2022

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1

Ascenzi, Paolo, and Maurizio Brunori. "A molecule for all seasons: The heme." Journal of Porphyrins and Phthalocyanines 20, no. 01n04 (January 2016): 134–49. http://dx.doi.org/10.1142/s1088424616300081.

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If life without heme-Fe were at all possible, it would definitely be different. Indeed this complex and versatile iron-porphyrin macrocycle upon binding to different “globins” yields hemeproteins crucial to sustain a variety of vital functions, generally classified, for convenience, in a limited number of functional families. Over-and-above the array of functions briefly outlined below, the spectacular progress in molecular genetics seen over the last 30 years led to the discovery of many hitherto unknown novel hemeproteins in prokaryotes and eukaryotes. Here, we highlight a few basic aspects of the chemistry of the hemeprotein universe, in particular those that are relevant to the control of heme-Fe reactivity and specialization, as sculpted by a variety of interactions with the protein moiety.

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2

Frauenfelder, H., and P. Wolynes. "Rate theories and puzzles of hemeprotein kinetics." Science 229, no. 4711 (July 26, 1985): 337–45. http://dx.doi.org/10.1126/science.4012322.

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3

Madhavi Sastry, G., and V. Sabareesh. "The Lie-algebraic approach to hemeprotein-ligand dynamics." Chemical Physics Letters 369, no. 5-6 (February 2003): 691–97. http://dx.doi.org/10.1016/s0009-2614(03)00041-1.

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4

Díaz-Quintana, Antonio, Gonzalo Pérez-Mejías, Alejandra Guerra-Castellano, Miguel A. De la Rosa, and Irene Díaz-Moreno. "Wheel and Deal in the Mitochondrial Inner Membranes: The Tale of Cytochrome c and Cardiolipin." Oxidative Medicine and Cellular Longevity 2020 (April 22, 2020): 1–20. http://dx.doi.org/10.1155/2020/6813405.

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Cardiolipin oxidation and degradation by different factors under severe cell stress serve as a trigger for genetically encoded cell death programs. In this context, the interplay between cardiolipin and another mitochondrial factor—cytochrome c—is a key process in the early stages of apoptosis, and it is a matter of intense research. Cytochrome c interacts with lipid membranes by electrostatic interactions, hydrogen bonds, and hydrophobic effects. Experimental conditions (including pH, lipid composition, and post-translational modifications) determine which specific amino acid residues are involved in the interaction and influence the heme iron coordination state. In fact, up to four binding sites (A, C, N, and L), driven by different interactions, have been reported. Nevertheless, key aspects of the mechanism for cardiolipin oxidation by the hemeprotein are well established. First, cytochrome c acts as a pseudoperoxidase, a process orchestrated by tyrosine residues which are crucial for peroxygenase activity and sensitivity towards oxidation caused by protein self-degradation. Second, flexibility of two weakest folding units of the hemeprotein correlates with its peroxidase activity and the stability of the iron coordination sphere. Third, the diversity of the mode of interaction parallels a broad diversity in the specific reaction pathway. Thus, current knowledge has already enabled the design of novel drugs designed to successfully inhibit cardiolipin oxidation.

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5

IZUMIMOTO, Masatoshi, and Yongning ZHU. "Influence of Saccharides on the Stabilization of Frozen Hemeprotein." NIPPON SHOKUHIN KAGAKU KOGAKU KAISHI 45, no. 9 (1998): 539–44. http://dx.doi.org/10.3136/nskkk.45.539.

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6

Sasaki, Tomikazu, and Emil T. Kaiser. "Helichrome: synthesis and enzymic activity of a designed hemeprotein." Journal of the American Chemical Society 111, no. 1 (January 1989): 380–81. http://dx.doi.org/10.1021/ja00183a065.

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7

Young, Lawrence J., and Lewis M. Siegel. "Alkaline low spin form of sulfite reductase hemeprotein subunit." Biochemical and Biophysical Research Communications 169, no. 1 (May 1990): 39–45. http://dx.doi.org/10.1016/0006-291x(90)91429-v.

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8

Ikeda-Saito, M., H. C. Lee, K. Adachi, H. S. Eck, R. C. Prince, K. S. Booth, W. S. Caughey, and S. Kimura. "Demonstration that spleen green hemeprotein is identical to granulocyte myeloperoxidase." Journal of Biological Chemistry 264, no. 8 (March 1989): 4559–63. http://dx.doi.org/10.1016/s0021-9258(18)83779-6.

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9

Dal Farra, Maria Giulia, Sabine Richert, Caterina Martin, Charles Larminie, Marina Gobbo, Elisabetta Bergantino, Christiane R. Timmel, Alice M. Bowen, and Marilena Di Valentin. "Light‐Induced Pulsed EPR Dipolar Spectroscopy on a Paradigmatic Hemeprotein." ChemPhysChem 20, no. 7 (March 21, 2019): 931–35. http://dx.doi.org/10.1002/cphc.201900139.

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10

Morishima, Yoshihiro, Haoming Zhang, Miranda Lau, and Yoichi Osawa. "Improved method for assembly of hemeprotein neuronal NO-synthase heterodimers." Analytical Biochemistry 511 (October 2016): 24–26. http://dx.doi.org/10.1016/j.ab.2016.07.031.

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11

Macías, Pedro, M. Carmen Pinto, and Carlos Gutiérrez-Merino. "Hemin and hemeprotein bleaching during linoleic acid oxidation by lipoxygenases." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 1082, no. 3 (April 1991): 310–18. http://dx.doi.org/10.1016/0005-2760(91)90207-x.

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12

Kaufman, Jeffrey, Leonard D. Spicer, and Lewis M. Siegel. "Proton NMR of Escherichia coli sulfite reductase: The unligated hemeprotein subunit." Biochemistry 32, no. 11 (March 23, 1993): 2853–67. http://dx.doi.org/10.1021/bi00062a017.

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13

Estabrook, Ronald W. "The remarkable P450s: a historical overview of these versatile hemeprotein catalysts." FASEB Journal 10, no. 2 (February 1996): 202–4. http://dx.doi.org/10.1096/fasebj.10.2.8641552.

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14

Tsuji, A., and H. Sakurai. "Nitric oxide generation in the reaction of hemeprotein and streptozotocin (STZ)." Journal of Inorganic Biochemistry 59, no. 2-3 (August 1995): 457. http://dx.doi.org/10.1016/0162-0134(95)97553-3.

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15

Alzahrani, Eman. "Incorporation of silver stearate nanoparticles in methacrylate polymeric monoliths for hemeprotein isolation." Open Chemistry 18, no. 1 (April 27, 2020): 399–411. http://dx.doi.org/10.1515/chem-2020-0051.

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AbstractA unique method was used to synthesize extremely stable silver stearate nanoparticles (AgStNPs) incorporated in an organic-based monolith. The facile strategy was then used to selectively isolate hemeproteins, myoglobin (Myo) and hemoglobin (Hb). Ethyl alcohol, silver nitrate, and stearic acid were, respectively, utilized as reducing agents, silver precursors, and capping agents. The color changed to cloudy from transparent, indicating that AgStNPs had been formed. AgStNP nanostructures were then distinctly integrated into the natural polymeric scaffold. To characterize the AgStNP–methacrylate polymeric monolith and the silver nanoparticles, energy-dispersive X-ray (EDX), scanning electron microscopy (SEM), and Fourier-transform infrared (FT-IR) spectroscopy were used. The results of the SEM analysis indicated that the AgStNP–methacrylate polymeric monolith’s texture was so rough in comparison with that of the methacrylate polymeric monolith, indicating that the extraction process of the monolith materials would be more efficient because of the extended surface area of the absorbent. The comparison between the FT-IR spectra of AgStNPs, the bare organic monolith, and AgStNP–methacrylate polymeric monolith confirms that the AgStNPs were immobilized on the surface of the organic monolith. The EDX profile of the built materials indicated an advanced peak of the Ag sequence which represented an Ag atom of 3.27%. The results therefore established that the AgStNPs had been successfully integrated into the monolithic materials. Extraction efficiencies of 92% and 97% were used to, respectively, recover preconcentrated Myo and Hb. An uncomplicated method is a unique approach of both fabrication and utilization of the nanosorbent to selectively isolate hemeproteins. The process can further be implemented by using other noble metals.

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16

Yoshikawa, S., D. H. O'Keeffe, and W. S. Caughey. "Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites." Journal of Biological Chemistry 260, no. 6 (March 1985): 3518–28. http://dx.doi.org/10.1016/s0021-9258(19)83653-0.

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17

Akhtar, Naeem, Sherif A. El-Safty, Mamdouh E. Abdelsalam, and Hiroshi Kawarada. "Electron transport dependence of nanoscale hemeprotein molecular structures for engineering electrochemical nanosensor." Nano-Structures & Nano-Objects 2 (August 2015): 35–44. http://dx.doi.org/10.1016/j.nanoso.2015.08.001.

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18

Montgomery, Heather J., Andrea L. Dupont, Hilary E. Leivo, and J. Guy Guillemette. "Cloning, Expression, and Purification of a Nitric Oxide Synthase-Like Protein fromBacillus cereus." Biochemistry Research International 2010 (2010): 1–4. http://dx.doi.org/10.1155/2010/489892.

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The nitric oxide synthase-like protein fromBacillus cereus(bcNOS) has been cloned, expressed, and characterized. This small hemeprotein (356 amino acids in length) has a mass of 43 kDa and forms a dimer. The recombinant protein showed similar spectral shifts to the mammalian NOS proteins and could bind the substrates L-arginine andNG-hydroxy-L-arginine as well as the ligand imidazole. Low levels of activity were recorded for the hydrogen peroxide-dependent oxidation ofNG-hydroxy-L-arginine and L-arginine by bcNOS, while a reconstituted system with the rat neuronal NOS reductase domain showed no activity. The recombinant bcNOS protein adds to the complement of bacterial NOS-like proteins that are used for the investigation of the mechanism and function of NO in microorganisms.

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19

Rose, Eric, Michèle Soleilhavoup, Lorraine Christ-Tommasino, Gilles Moreau, James P. Collman, Mélanie Quelquejeu, and Andrei Straumanis. "Bis-Faced Aminoporphyrin Templates for the Synthesis of Chiral Catalysts and Hemeprotein Analogues." Journal of Organic Chemistry 63, no. 6 (March 1998): 2042–44. http://dx.doi.org/10.1021/jo9718713.

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20

De Jesús-Bonilla, Walleska, Anthony Cruz, Ariel Lewis, José Cerda, Daniel E. Bacelo, Carmen L. Cadilla, and Juan López-Garriga. "Hydrogen-bonding conformations of tyrosine B10 tailor the hemeprotein reactivity of ferryl species." JBIC Journal of Biological Inorganic Chemistry 11, no. 3 (February 9, 2006): 334–42. http://dx.doi.org/10.1007/s00775-006-0082-0.

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21

Abbruzzetti, Stefania, Francesca Spyrakis, Axel Bidon-Chanal, F. Javier Luque, and Cristiano Viappiani. "Ligand migration through hemeprotein cavities: insights from laser flash photolysis and molecular dynamics simulations." Physical Chemistry Chemical Physics 15, no. 26 (2013): 10686. http://dx.doi.org/10.1039/c3cp51149a.

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22

Mandel, Mark L., Susan J. Swartz, and Jacob G. Ghazarian. "Avian kidney mitochondrial hemeprotein P-4501α: isolation, characterization and NADPH-ferredoxin reductase-dependent activity." Biochimica et Biophysica Acta (BBA) - General Subjects 1034, no. 3 (June 1990): 239–46. http://dx.doi.org/10.1016/0304-4165(90)90044-w.

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23

Lin, W. L., and E. Essner. "Diffuse cytoplasmic staining of retinal capillary endothelium." Journal of Histochemistry & Cytochemistry 34, no. 10 (October 1986): 1325–30. http://dx.doi.org/10.1177/34.10.2427569.

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The distribution of several hemeprotein tracers in retinal capillaries of Wistar-Furth rats was studied by electron microscopic cytochemistry after incubation in 3,3'-diaminobenzidine. Diffuse cytoplasmic reaction product was frequently observed in the endothelial cells after intravenous injection of horseradish peroxidase (HRP) or lactoperoxidase (LP), or after perfusion of HRP. Occasionally, pericytes were also diffusely stained. In contrast, injection of microperoxidase, catalase, or hemoglobin did not cause diffuse staining. The diffuse staining was similar with HRP types II, VI, and VIII, and at concentrations of 2.5, 5, and 10 mg/100 g body weight. Despite the staining, the blood-retinal barrier remained intact. The findings indicate that HRP and LP are capable of causing diffuse nonspecific staining of retinal capillary endothelial cells, even at relatively low concentrations. Since these tracers are frequently used in studies of the blood-retinal barrier, the results of such studies should be interpreted with caution.

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24

Moreno-Beltrán, Blas, Alejandra Guerra-Castellano, Antonio Díaz-Quintana, Rebecca Del Conte, Sofía M. García-Mauriño, Sofía Díaz-Moreno, Katiuska González-Arzola, et al. "Structural basis of mitochondrial dysfunction in response to cytochrome c phosphorylation at tyrosine 48." Proceedings of the National Academy of Sciences 114, no. 15 (March 27, 2017): E3041—E3050. http://dx.doi.org/10.1073/pnas.1618008114.

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Regulation of mitochondrial activity allows cells to adapt to changing conditions and to control oxidative stress, and its dysfunction can lead to hypoxia-dependent pathologies such as ischemia and cancer. Although cytochrome c phosphorylation—in particular, at tyrosine 48—is a key modulator of mitochondrial signaling, its action and molecular basis remain unknown. Here we mimic phosphorylation of cytochrome c by replacing tyrosine 48 with p-carboxy-methyl-l-phenylalanine (pCMF). The NMR structure of the resulting mutant reveals significant conformational shifts and enhanced dynamics around pCMF that could explain changes observed in its functionality: The phosphomimetic mutation impairs cytochrome c diffusion between respiratory complexes, enhances hemeprotein peroxidase and reactive oxygen species scavenging activities, and hinders caspase-dependent apoptosis. Our findings provide a framework to further investigate the modulation of mitochondrial activity by phosphorylated cytochrome c and to develop novel therapeutic approaches based on its prosurvival effects.

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25

Ikeda-Saito, M. "Spectroscopic, ligand binding, and enzymatic properties of the spleen green hemeprotein. A comparison with myeloperoxidase." Journal of Biological Chemistry 260, no. 21 (September 1985): 11688–96. http://dx.doi.org/10.1016/s0021-9258(17)39085-3.

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26

Faiella, Marina, Ornella Maglio, Flavia Nastri, Angela Lombardi, Liliana Lista, Wilfred R. Hagen, and Vincenzo Pavone. "De Novo Design, Synthesis and Characterisation of MP3, A New Catalytic Four-Helix Bundle Hemeprotein." Chemistry - A European Journal 18, no. 50 (November 13, 2012): 15960–71. http://dx.doi.org/10.1002/chem.201201404.

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27

Sastry, G. Madhavi. "Application of N-particle random walk to geminate recombination of a hemeprotein with a ligand." Chemical Physics Letters 379, no. 5-6 (October 2003): 547–54. http://dx.doi.org/10.1016/j.cplett.2003.08.092.

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28

Alexandre, Marta R., Alexandra I. Costa, Mário N. Berberan-Santos, and José V. Prata. "Finding Value in Wastewaters from the Cork Industry: Carbon Dots Synthesis and Fluorescence for Hemeprotein Detection." Molecules 25, no. 10 (May 15, 2020): 2320. http://dx.doi.org/10.3390/molecules25102320.

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Valorisation of industrial low-value waste residues was preconized. Hence, carbon dots (C-dots) were synthesized from wastewaters of the cork industry—an abundant and affordable, but environmentally-problematic industrial effluent. The carbon nanomaterials were structurally and morphologically characterised, and their photophysical properties were analysed by an ensemble of spectroscopy techniques. Afterwards, they were successfully applied as highly-sensitive fluorescence probes for the direct detection of haemproteins. Haemoglobin, cytochrome c and myoglobin were selected as specific targets owing to their relevant roles in living organisms, wherein their deficiencies or surpluses are associated with several medical conditions. For all of them, remarkable responses were achieved, allowing their detection at nanomolar levels. Steady-state and time-resolved fluorescence, ground-state UV–Vis absorption and electronic circular dichroism techniques were used to investigate the probable mechanisms behind the fluorescence turn-off of C-dots. Extensive experimental evidence points to a static quenching mechanism. Likewise, resonance energy transfer and collisional quenching have been discarded as excited-state deactivating mechanisms. It was additionally found that an oxidative, photoinduced electron transfer occurs for cytochrome c, the most electron-deficient protein. Besides, C-dots prepared from citric acid/ethylenediamine were comparatively assayed for protein detection and the differences between the two types of nanomaterials highlighted.

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29

Xu, F., L. J. Defilippi, D. P. Ballou, and D. E. Hultquist. "Hydrogen Peroxide-Dependent Formation and Bleaching of the Higher Oxidation States of Bovine Erythrocyte Green Hemeprotein." Archives of Biochemistry and Biophysics 301, no. 1 (February 1993): 184–89. http://dx.doi.org/10.1006/abbi.1993.1131.

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30

Ramos, Cacimar, Ruth Pietri, Wilmarie Lorenzo, Elddie Roman, Laura B. Granell, Carmen L. Cadilla, and Juan López-Garriga. "Recombinant Hemoglobin II From Lucina pectinata: A Large-Scale Method For Hemeprotein Expression in E. coli." Protein Journal 29, no. 2 (February 2010): 143–51. http://dx.doi.org/10.1007/s10930-010-9234-8.

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31

Cotes, N. J., and Mark G. Sceats. "Recombination dynamics in a hemispherical cage. A model of geminate ligand binding in the hemeprotein pocket." Chemical Physics Letters 141, no. 5 (November 1987): 405–10. http://dx.doi.org/10.1016/0009-2614(87)85049-2.

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32

Shumyantseva, V. V., T. V. Bulko, A. Yu Misharin, and A. I. Archakov. "Screening of potential substrates or inhibitors of cytochrome P450 17a1 (CYP17a1) by electrochemical methods." Biomeditsinskaya Khimiya 57, no. 4 (2011): 402–9. http://dx.doi.org/10.18097/pbmc20115704402.

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The electrochemical reduction of the recombinant form of human cytochrome P450 17A1 (CYP17A1) was investigated. Hemeprotein was immobilized on electrode modified with biocompatable nanocomposite material based on the membrane-like synthetic surfactant didodecyldimethylammonium bromide (DDAB) and gold nanoparticles. Analytical characteristics of DDAB/Au/CYP17A1 electrodes were investigated with cyclic voltammetry, square wave voltammetry, and differential pulse voltammetry. Analysis of electrochemical behaviour of cytochrome P450 17A1 was conducted in the presence of substrate pregnenolone (1), inhibitor ketoconazole (2), and in the presence of synthetic derivatives of pregnenolone: acetylpregnenolone (3), cyclopregnenolone (4), and tetrabrompregnenolone (5). Ketoconazole, azole inhibitor of cytochromes P450, blocked catalytic current in the presence of substrate pregnenolone (1). Compounds 3-5 did not demonstrate substrate properties towards electrode/CYP17A1 system. Compound 3 did not block catalytic activity towards pregnenolone, but compounds 4 and 5 inhibited such activity. Electrochemical reduction of CYP17A1 may serve as an adequate substitution of the reconstituted system which requires additional redox partners - for the exhibition of catalytic activity of hemoproteins of the cytochrome P450 superfamily.

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33

Schlater, Amber E., Michael A. De Miranda, Melinda A. Frye, Stephen J. Trumble, and Shane B. Kanatous. "Changing the paradigm for myoglobin: a novel link between lipids and myoglobin." Journal of Applied Physiology 117, no. 3 (August 1, 2014): 307–15. http://dx.doi.org/10.1152/japplphysiol.00973.2013.

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Myoglobin (Mb) is an oxygen-binding muscular hemeprotein regulated via Ca2+-signaling pathways involving calcineurin (CN), with Mb increases attributed to hypoxia, exercise, and nitric oxide. Here, we show a link between lipid supplementation and increased Mb in skeletal muscle. C2C12 cells were cultured in normoxia or hypoxia with glucose or 5% lipid. Mb assays revealed that lipid cohorts had higher Mb than control cohorts in both normoxia and hypoxia, whereas Mb Western blots showed lipid cohorts having higher Mb than control cohorts exclusively under hypoxia. Normoxic cells were compared with soleus tissue from normoxic rats fed high-fat diets; whereas tissue sample cohorts showed no difference in CO-binding Mb, fat-fed rats showed increases in total Mb protein (similar to hypoxic cells), suggesting increases in modified Mb. Moreover, Mb increases did not parallel CN increases but did, however, parallel oxidative stress marker augmentation. Addition of antioxidant prevented Mb increases in lipid-supplemented normoxic cells and mitigated Mb increases in lipid-supplemented hypoxic cells, suggesting a pathway for Mb regulation through redox signaling independent of CN.

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34

Vilchis, F., R. Damsky, Y. Heuze, J. Enrı́quez, and B. Chávez. "Identification and Androgen Regulation of a 156-kDa Hemeprotein in the Harderian Gland of the Syrian Hamster." General and Comparative Endocrinology 101, no. 3 (March 1996): 297–303. http://dx.doi.org/10.1006/gcen.1996.0032.

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35

Yu, L., H. Liu, J. Wang, G. Jiang, and G. Cheng. "213 Effects of Different Levels of Hemeprotein Supplementation on Performance and Blood Physicochemical Parameters in Weaned Piglets." Journal of Animal Science 96, suppl_2 (April 2018): 113–14. http://dx.doi.org/10.1093/jas/sky073.210.

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36

Oyenarte, Iker, Tomas Majtan, June Ereño, María Angeles Corral-Rodríguez, Jan P. Kraus, and Luis Alfonso Martínez-Cruz. "Purification, crystallization and preliminary crystallographic analysis of human cystathionine β-synthase." Acta Crystallographica Section F Structural Biology and Crystallization Communications 68, no. 11 (October 30, 2012): 1318–22. http://dx.doi.org/10.1107/s1744309112037219.

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Human cystathionine β-synthase (CBS) is a pyridoxal-5′-phosphate-dependent hemeprotein, whose catalytic activity is regulated byS-adenosylmethionine. CBS catalyzes the β-replacement reaction of homocysteine (Hcy) with serine to yield cystathionine. CBS is a key regulator of plasma levels of the thrombogenic Hcy and deficiency in CBS is the single most common cause of homocystinuria, an inherited metabolic disorder of sulfur amino acids. The properties of CBS enzymes, such as domain organization, oligomerization degree or regulatory mechanisms, are not conserved across the eukaryotes. The current body of knowledge is insufficient to understand these differences and their impact on CBS function and physiology. To overcome this deficiency, we have addressed the crystallization and preliminary crystallographic analysis of a protein construct (hCBS516–525) that contains the full-length CBS fromHomo sapiens(hCBS) and just lacks amino-acid residues 516–525, which are located in a disordered loop. The human enzyme yielded crystals belonging to space groupI222, with unit-cell parametersa= 124.98,b= 136.33,c= 169.83 Å and diffracting X-rays to a resolution of 3.0 Å. The crystal structure appears to contain two molecules in the asymmetric unit which presumably correspond to a dimeric form of the enzyme.

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37

Kiselyova, O. I., O. L. Guryev, A. V. Krivosheev, S. A. Usanov, and I. V. Yaminsky. "Atomic Force Microscopy Studies of Langmuir−Blodgett Films of Cytochrome P450scc: Hemeprotein Aggregation States and Interaction with Lipids." Langmuir 15, no. 4 (February 1999): 1353–59. http://dx.doi.org/10.1021/la980726x.

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38

Peng, Wei, Fei Ding, Yu-Kui Peng, and Yong Xie. "Biological effects of α -adrenergic phentolamine on erythrocyte hemeprotein: Molecular insights from biorecognition behavior, protein dynamics and flexibility." Journal of Photochemistry and Photobiology B: Biology 171 (June 2017): 75–84. http://dx.doi.org/10.1016/j.jphotobiol.2017.04.035.

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39

Pikuleva, I. A., A. G. Lapko, and V. L. Chashchin. "Functional reconstitution of cytochrome P-450scc with hemin activated with Woodward's reagent K. Formation of a hemeprotein cross-link." Journal of Biological Chemistry 267, no. 3 (January 1992): 1438–42. http://dx.doi.org/10.1016/s0021-9258(18)45964-9.

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40

Taira, Junsei, Chika Miyagi, and Yoko Aniya. "Dimerumic acid as an antioxidant from the mold, Monascus anka: the inhibition mechanisms against lipid peroxidation and hemeprotein-mediated oxidation." Biochemical Pharmacology 63, no. 5 (March 2002): 1019–26. http://dx.doi.org/10.1016/s0006-2952(01)00923-6.

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41

Su, Chao, Margareta Sahlin, and Ernst H. Oliw. "A Protein Radical and Ferryl Intermediates Are Generated by Linoleate Diol Synthase, a Ferric Hemeprotein with Dioxygenase and Hydroperoxide Isomerase Activities." Journal of Biological Chemistry 273, no. 33 (August 14, 1998): 20744–51. http://dx.doi.org/10.1074/jbc.273.33.20744.

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42

Sono, Masanori, John H. Dawson, and Masao Ikeda-Saito. "Characterization of the spleen green hemeprotein with magnetic and natural circular dichroism spectroscopy: positive evidence for a myeloperoxidase-type active site." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 873, no. 1 (September 1986): 62–72. http://dx.doi.org/10.1016/0167-4838(86)90190-1.

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43

Lu, Zhijie, Meizhen Tang, Menglan Zhang, Yanan Li, Fei Shi, Fanbin Zhan, Lijuan Zhao, Jun Li, Li Lin, and Zhendong Qin. "Hemeprotein amplifies the innate immune receptors of Ctenopharyngodon idellus kidney cells through NF-κB- and MAPK-dependent reactive oxygen species generation." Developmental & Comparative Immunology 126 (January 2022): 104207. http://dx.doi.org/10.1016/j.dci.2021.104207.

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44

Jia, Yiping, Paul W. Buehler, Robert A. Boykins, Richard M. Venable, and Abdu I. Alayash. "Structural Basis of Peroxide-mediated Changes in Human Hemoglobin." Journal of Biological Chemistry 282, no. 7 (December 17, 2006): 4894–907. http://dx.doi.org/10.1074/jbc.m609955200.

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Hydrogen peroxide (H2O2) triggers a redox cycle between ferric and ferryl hemoglobin (Hb) leading to the formation of a transient protein radical and a covalent hemeprotein cross-link. Addition of H2O2 to highly purified human hemoglobin (HbA0) induced structural changes that primarily resided within β subunits followed by the internalization of the heme moiety within α subunits. These modifications were observed when an equal molar concentration of H2O2 was added to HbA0 yet became more abundant with greater concentrations of H2O2. Mass spectrometric and amino acid analysis revealed for the first time that βCys-93 and βCys-112 were oxidized extensively and irreversibly to cysteic acid when HbA0 was treated with H2O2. Oxidation of further amino acids in HbA0 exclusive to the β-globin chain included modification of βTrp-15 to oxyindolyl and kynureninyl products as well as βMet-55 to methionine sulfoxide. These findings may therefore explain the premature collapse of the β subunits as a result of the H2O2 attack. Analysis of a tryptic digest of the main reversed phase-high pressure liquid chromatography fraction revealed two α-peptide fragments (α128 - α139) and a heme moiety with the loss of iron, cross-linked between αSer-138 and the porphyrin ring. The novel oxidative pathway of HbA0 modification detailed here may explain the diverse oxidative, toxic, and potentially immunogenic effects associated with the release of hemoglobin from red blood cells during hemolytic diseases and/or when cell-free Hb is used as a blood substitute.

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45

Faiella, Marina, Ornella Maglio, Flavia Nastri, Angela Lombardi, Liliana Lista, Wilfred R. Hagen, and Vincenzo Pavone. "Inside Cover: De Novo Design, Synthesis and Characterisation of MP3, A New Catalytic Four-Helix Bundle Hemeprotein (Chem. Eur. J. 50/2012)." Chemistry - A European Journal 18, no. 50 (December 4, 2012): 15890. http://dx.doi.org/10.1002/chem.201290213.

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46

García-Rubio, Inés, Pablo J. Alonso, Milagros Medina, and Jesús I. Martínez. "Hyperfine Correlation Spectroscopy and Electron Spin Echo Envelope Modulation Spectroscopy Study of the Two Coexisting Forms of the Hemeprotein Cytochrome c6 from Anabaena Pcc7119." Biophysical Journal 96, no. 1 (January 2009): 141–52. http://dx.doi.org/10.1529/biophysj.108.133272.

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47

Baldwin, David A., Helder M. Marques, and John M. Pratt. "Hemes and hemeproteins." Journal of Inorganic Biochemistry 27, no. 4 (August 1986): 245–54. http://dx.doi.org/10.1016/0162-0134(86)80065-4.

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48

Dolphin, David. "Biomimetic chemistry of hemeproteins." Keio Journal of Medicine 38, no. 1 (1989): 65–69. http://dx.doi.org/10.2302/kjm.38.65.

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49

Tsai, Ah-lim. "How does NO activate hemeproteins?" FEBS Letters 341, no. 2-3 (March 21, 1994): 141–45. http://dx.doi.org/10.1016/0014-5793(94)80445-1.

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50

Parashar, Abhinav, Daniel Andrew Gideon, and Kelath Murali Manoj. "Murburn Concept: A Molecular Explanation for Hormetic and Idiosyncratic Dose Responses." Dose-Response 16, no. 2 (April 1, 2018): 155932581877442. http://dx.doi.org/10.1177/1559325818774421.

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Recently, electron transfers and catalyses in a bevy of redox reactions mediated by hemeproteins were explained by murburn concept. The term “murburn” is abstracted from “ mur ed burn ing” or “ m ild u n r estricted burn ing” and connotes a novel “ m olecule- u nbound ion– r adical” interaction paradigm. Quite unlike the genetic regulations and protein-level affinity-based controls that govern order and specificity/selectivity in conventional treatments, murburn concept is based on stochastic/thermodynamic regulatory principles. The novel insight necessitates a “reactivity outside the active-site” perspective, because select redox enzymatic activity is obligatorily mediated via diffusible radical/species. Herein, reactions employing key hemeproteins (as exemplified by CYP2E1) establish direct experimental connection between “additive-influenced redox catalysis” and “unusual dose responses” in reductionist and physiological milieu. Thus, direct and conclusive molecular-level experimental evidence is presented, supporting the mechanistic relevance of murburn concept in “maverick” concentration-based effects brought about by additives. Therefore, murburn concept could potentially explain several physiological hormetic and idiosyncratic dose responses.

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