Inactivation of the 2‐oxo acid dehydrogenase complexes upon generation of intrinsic radical species
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Self‐regulation of the 2‐oxo acid dehydrogenase complexes during catalysis was studied. Radical species as side products of catalysis were detected by spin trapping, lucigenin fluorescence and ferricytochrome c reduction. Studies of the complexes after converting the bound lipoate or FAD cofactors to nonfunctional derivatives indicated that radicals are generated via FAD. In the presence of oxygen, the 2‐oxo acid, CoA‐dependent production of the superoxide anion radical was detected. In the absence of oxygen, a protein‐bound radical concluded to be the thiyl radical of the complex‐bound dihydrolipoate was trapped by α‐phenyl‐ N ‐ tert ‐butylnitrone. Another, carbon‐centered, radical was trapped in anaerobic reaction of the complex with 2‐oxoglutarate and CoA by 5,5′‐dimethyl‐1‐pyrroline‐ N ‐oxide (DMPO). Generation of radical species was accompanied by the enzyme inactivation. A superoxide scavenger, superoxide dismutase, did not protect the enzyme. However, a thiyl radical scavenger, thioredoxin, prevented the inactivation. It was concluded that the thiyl radical of the complex‐bound dihydrolipoate induces the inactivation by 1e – oxidation of the 2‐oxo acid dehydrogenase catalytic intermediate. A product of this oxidation, the DMPO‐trapped radical fragment of the 2‐oxo acid substrate, inactivates the first component of the complex. The inactivation prevents transformation of the 2‐oxo acids in the absence of terminal substrate, NAD + . The self‐regulation is modulated by thioredoxin which alleviates the adverse effect of the dihydrolipoate intermediate, thus stimulating production of reactive oxygen species by the complexes. The data point to a dual pro‐oxidant action of the complex‐bound dihydrolipoate, propagated through the first and third component enzymes and controlled by thioredoxin and the (NAD + + NADH) pool.
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Mitochondrial enzymes beyond the ETC-pyruvate dehydrogenase, α-ketoglutarate dehydrogenase, and monoamine oxygenase A and B-have been reported to generate ROS.
“Pyruvate dehydrogenase (887), α-ketoglutarate dehydrogenase (130, 887, 952), and monoamine oxygenase A and B (290) have all been demonstrated to serve as ROS sources.”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [130]
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Cites
Oxygen free radicals and iron in relation to biology and medicine: Some problems and concepts
Halliwell, B., & Gutteridge, J. M. C. (1986) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(86)90305-x · Cited by 2,038 · see citing works
Alpha-lipoic acid as a biological antioxidant
Packer, L., Witt, E. H., & Tritschler, H. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)00017-r · Cited by 1,995 · see citing works
The Reduction of Cytochrome c by Milk Xanthine Oxidase
McCord, J. M., & Fridovich, I. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91929-0 · Cited by 1,205 · see citing works
The pharmacology of the antioxidant lipoic acid
Biewenga, G. P., Haenen, G. R. M. M., & Bast, A. (1997) · General Pharmacology The Vascular System · doi:10.1016/s0306-3623(96)00474-0 · Cited by 844 · see citing works
Perham, R. N. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.961 · Cited by 613 · see citing works
Massey, V., Strickland, S., Mayhew, S. G., Howell, L. G., Engel, P. C., Matthews, R. G., Schuman, M., & Sullivan, P. A. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90287-3 · Cited by 426 · see citing works
Gibson, G. E., Sheu, K. ‐. R., Blass, J. P., Baker, A., Carlson, K., Harding, B. N., & Perrino, P. (1988) · Archives of Neurology · doi:10.1001/archneur.1988.00520320022009 · Cited by 425 · see citing works
Perham, R. N. (1991) · Biochemistry · doi:10.1021/bi00099a001 · Cited by 422 · see citing works
Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae
Cabiscol, E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003140200 · Cited by 418 · see citing works
Harbour, J. R., Chow, V., & Bolton, J. R. (1974) · Canadian Journal of Chemistry · doi:10.1139/v74-527 · Cited by 414 · see citing works
Metabolic Enzymes of Mycobacteria Linked to Antioxidant Defense by a Thioredoxin-Like Protein
Bryk, R., Lima, C. D., Erdjument‐Bromage, H., Tempst, P., & Nathan, C. (2002) · Science · doi:10.1126/science.1067798 · Cited by 400 · see citing works
Mitochondrial Oxidative Stress Plays a Key Role in Aging and Apoptosis
Sastre, J., Pallardó, F. V., & Viña, J. (2000) · IUBMB Life · doi:10.1080/152165400410281 · Cited by 386 · see citing works
Structure-function relationships in dihydrolipoamide acyltransferases.
Reed, L. J., & Hackert, M. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38795-2 · Cited by 381 · see citing works
Humphries, K. M., & Szweda, L. I. (1998) · Biochemistry · doi:10.1021/bi981512h · Cited by 357 · see citing works
The Reactivity of Flavoproteins with Sulfite
Massey, V., Müller, F., Feldberg, R. S., Schuman, M., Sullivan, P. A., Howell, L. G., Mayhew, S. G., Matthews, R. G., & Foust, G. P. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36376-7 · Cited by 343 · see citing works
Oxidative Stress Promotes Specific Protein Damage inSaccharomyces cerevisiae
Cabiscol, E., Piulats, E., Echave, P., Herrero, E., & Ros, J. (2000) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)61523-1 · Cited by 334 · see citing works
Mitochondrial Aconitase Is a Source of Hydroxyl Radical
Vasquez-Vivar, J. M., Kalyanaraman, B., & Kennedy, M. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14064 · Cited by 317 · see citing works
Lipoic and Dihydrolipoic Acids as Antioxidants. a Critical Evaluation
Scott, B. C., Aruoma, O. I., Evans, P., O’neill, C. A., van der Vliet, A., Cross, C. E., Tritschler, H., & Halliwell, B. B. (1994) · Free Radical Research · doi:10.3109/10715769409147509 · Cited by 302 · see citing works
Sáez, G. T., Thornalley, P. J., Hill, H. A. O., Hems, R., & Bannister, J. V. (1982) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(82)90302-6 · Cited by 279 · see citing works
Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase)
Massey, V., Gibson, Q. H., & Veeger, C. (1960) · Biochemical Journal · doi:10.1042/bj0770341 · Cited by 238 · see citing works
Ballou, D. P., Palmer, G., & Massey, V. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90288-5 · Cited by 223 · see citing works
Reactive oxygen species as cellular messengers
Khan, A. U., & Wilson, T. (1995) · Chemistry & Biology · doi:10.1016/1074-5521(95)90259-7 · Cited by 215 · see citing works
Purification of 2-oxo acid dehydrogenase multienzyme complexes from ox heart by a new method
Stanley, C. J., & Perham, R. N. (1980) · Biochemical Journal · doi:10.1042/bj1910147 · Cited by 203 · see citing works
An immunohistochemical study on α‐ketoglutarate dehydrogenase complex in Parkinson's disease
Mizuno, Y., Matuda, S., Yoshino, H., Mori, H., Hattori, N., & Ikebe, S. (1994) · Annals of Neurology · doi:10.1002/ana.410350212 · Cited by 199 · see citing works
Butterworth, R. F., Kril, J. J., & Harper, C. G. (1993) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.1993.tb05668.x · Cited by 197 · see citing works
The pyruvate dehydrogenase multi-enzyme complex from Gram-negative bacteria
de Kok, A., Hengeveld, A. F., Martin, A., & Westphal, A. H. (1998) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(98)00079-x · Cited by 174 · see citing works
Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase
Chabrière, É., Vernède, X., Guigliarelli, B., Charon, M., Hatchikian, E. C., & Fontecilla-Camps, J. C. (2001) · Science · doi:10.1126/science.1066198 · Cited by 168 · see citing works
On spin trapping hydroxyl and hydroperoxyl radicals
Janzen, E. G., Nutter, D. E., Davis, E. R., Blackburn, B. J., Poyer, J. L., & McCay, P. B. (1978) · Canadian Journal of Chemistry · doi:10.1139/v78-368 · Cited by 156 · see citing works
Peroxynitrite‐mediated oxidation of albumin to the protein‐thiyl free radical
Gatti, R. M., Radí, R., & Augusto, O. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00625-3 · Cited by 146 · see citing works
A method for the detection of superoxide in biological systems
Rosen, G. M., Finkelstein, E., & Rauckman, E. J. (1982) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(82)90097-2 · Cited by 137 · see citing works
[15] Sulfur-centered free radicals
Asmus, K. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)86107-7 · Cited by 135 · see citing works
Brain protein and α‐ketoglutarate dehydrogenase complex activity in alzheimer‐s disease
Mastrogiacomo, F., LINDSAY, J. G., Bettendorff, L., Rice, J., & Kish, S. J. (1996) · Annals of Neurology · doi:10.1002/ana.410390508 · Cited by 132 · see citing works
Hol, W. G. J., Aevarsson, A., Seger, K., Turley, S., & Sokatch, J. R. (1999) · Nature Structural Biology · doi:10.1038/11563 · Cited by 127 · see citing works
Contribution of different enzymes to flavoprotein fluorescence of isolated rat liver mitochondria
Kunz, W. S., & Kunz, W. (1985) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(85)90064-9 · Cited by 126 · see citing works
Millar, A. H., & Leaver, C. J. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01976-1 · Cited by 114 · see citing works
Skulachev, V. P. (2000) · IUBMB Life · doi:10.1080/152165400410209 · Cited by 113 · see citing works
Romero, F. J., Ordonez, I., Arduini, A., & Cadenas, E. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45999-6 · Cited by 109 · see citing works
Collins, J. H., & Reed, L. J. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.10.4223 · Cited by 109 · see citing works
Searls, R. L., & Peters, J. M. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64078-5 · Cited by 109 · see citing works
Kotake, Y., & Janzen, E. G. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00025a013 · Cited by 107 · see citing works
Superoxide generation by the respiratory chain of tumor mitochondria
Konstantinov, A. A., Peskin, A. V., Popova, E. Y., Khomutov, G. B., & Ruuge, E. K. (1987) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(87)90206-4 · Cited by 103 · see citing works
Andersson-Hall, U. K., Leighton, B., Young, M. E., Blomstrand, E., & Newsholme, E. A. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9171 · Cited by 99 · see citing works
Britigan, B. E., Coffman, T. J., & Buettner, G. R. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39850-3 · Cited by 94 · see citing works
Shi, X., & Dalal, N. S. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)80815-5 · Cited by 94 · see citing works
Britigan, B. E., Pou, S., Rosen, G. M., Lilleg, D. M., & Buettner, G. R. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)38197-3 · Cited by 89 · see citing works
Reactive Oxygen Species-Mediated Inactivation of Pyruvate Dehydrogenase
Tabatabaie, T., Potts, J. D., & Floyd, R. A. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0560 · Cited by 82 · see citing works
Substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli.
Bisswanger, H. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70050-7 · Cited by 81 · see citing works
Danson, M. J., Fersht, A. R., & Perham, R. N. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.11.5386 · Cited by 80 · see citing works
Menon, S., & Ragsdale, S. W. (1997) · Biochemistry · doi:10.1021/bi970403k · Cited by 76 · see citing works
Li, Y., Stansbury, K. H., Zhu, H., & Trush, M. A. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1174 · Cited by 70 · see citing works
Ross, D., Albano, E., Nilsson, U. A., & Moldéus, P. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80341-1 · Cited by 68 · see citing works
Stoyanovsky, D. A., Goldman, R., Claycamp, H. G., & Kagan, V. E. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1169 · Cited by 59 · see citing works
Matthews, R. G., Ballou, D. P., Thorpe, C., & Williams, C. H. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40371-1 · Cited by 56 · see citing works
Ambrose, M. C., & Perham, R. N. (1976) · Biochemical Journal · doi:10.1042/bj1550429 · Cited by 56 · see citing works
Sankarapandi, S., & Zweier, J. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.49.34576 · Cited by 53 · see citing works
Electron transfer properties of active aldehydes derived from thiamin coenzyme analogues
Nakanishi, I., & Itoh, S. (1997) · Chemical Communications · doi:10.1039/a704559j · Cited by 51 · see citing works
Skatchkov, M. P., Sperling, D., Hink, U., Änggård, E., & Münzel, T. F. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8963 · Cited by 50 · see citing works
The reduction of nitroso-spin traps in chemical and biological sysetms. A cautionary note
Kalyanaraman, B., Perez‐Reyes, E., & Mason, R. P. (1979) · Tetrahedron Letters · doi:10.1016/s0040-4039(01)86718-6 · Cited by 49 · see citing works
Barletta, G. L., Chung, A. C., Ríos, C. B., Jordan, F., & Schlegel, J. M. (1990) · Journal of the American Chemical Society · doi:10.1021/ja00178a044 · Cited by 46 · see citing works
Graceffa, P. (1983) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(83)90092-9 · Cited by 44 · see citing works
Docampo, R., Moreno, S. N. J., & Mason, R. P. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45219-2 · Cited by 43 · see citing works
Akiyama, S. K., & Hammes, G. G. (1980) · Biochemistry · doi:10.1021/bi00559a011 · Cited by 41 · see citing works
Stoyanovsky, D. A., Melnikov, Z., & Cederbaum, A. I. (1998) · Analytical Chemistry · doi:10.1021/ac980657r · Cited by 40 · see citing works
Thioredoxin reduction dependent on α‐ketoacid oxidation by α‐ketoacid dehydrogenase complexes
Bunik, V. I., & Follmann, H. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80801-z · Cited by 39 · see citing works
Self-citationHydroxyl radical is not a product of the reaction of xanthine oxidase and xanthine
Britigan, B. E., Pou, S., Rosen, G. M., Lilleg, D. M., & Buettner, G. R. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90807-u · Cited by 38 · see citing works
Mitochondrial stress protein recognition of inactivated dehydrogenases during mammalian cell death
Bruschi, S. A., LINDSAY, J. G., & Crabb, J. W. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13413 · Cited by 38 · see citing works
Buettner, G. R. (1984) · FEBS Letters · doi:10.1016/0014-5793(84)81303-4 · Cited by 38 · see citing works
Bunik, V. I., Raddatz, G., Bisswanger, H., Lemaire, S. D., Meyer, Y., & Jacquot, J. (1999) · Protein Science · doi:10.1110/ps.8.1.65 · Cited by 38 · see citing works
Self-citationROKUTAN, K., Kawai, K., & Asada, K. (1987) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a121926 · Cited by 36 · see citing works
Hanine‐Lmoumene, C. E., Conte, D., Jacquot, J., & Houée‐Levin, C. (2000) · Biochemistry · doi:10.1021/bi000468e · Cited by 36 · see citing works
[33] Thiyl free radical metabolites of thiol drugs, glutathione, and proteins
Mason, R. P., & Rao, D. N. R. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)86125-f · Cited by 35 · see citing works
Ambrose-Griffin, M. C., Danson, M. J., Griffin, W. G., Hale, G., & Perham, R. N. (1980) · Biochemical Journal · doi:10.1042/bj1870393 · Cited by 35 · see citing works
Grande, H. J., van Telgen, H. J., & Veeger, C. (1976) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1976.tb11139.x · Cited by 34 · see citing works
Molecular aspects of the removal of ferritin-bound iron bydl-dihydrolipoate
Bonomi, F., Cerioli, A., & Pagani, S. (1989) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(89)90158-1 · Cited by 32 · see citing works
Waskiewicz, D. E., & Hammes, G. G. (1984) · Biochemistry · doi:10.1021/bi00309a005 · Cited by 31 · see citing works
The mechanism of the quinone reductase reaction of pig heart lipoamide dehydrogenase
Vienozinskis, J., Butkus, A., Cenas, N., & Kulys, J. J. (1990) · Biochemical Journal · doi:10.1042/bj2690101 · Cited by 30 · see citing works
Studies on the lipoic acid free radical
CHAN, S., CHAN, P., & Bielski, B. H. J. (1974) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(74)90350-x · Cited by 30 · see citing works
Intermediates in Reductive Transacetylation Catalyzed by Pyruvate Dehydrogenase Complexa
Frey, P. A., Flournoy, D. S., Gruys, K. J., & Yang, Y. (1989) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1989.tb14984.x · Cited by 29 · see citing works
Hackert, M. L., Oliver, R. M., & Reed, L. J. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.10.2907 · Cited by 25 · see citing works
Kotake, Y., & Janzen, E. G. (1992) · ChemInform · doi:10.1002/chin.199213116 · Cited by 25 · see citing works
Bunik, V. I., Shoubnikova, A., Loeffelhardt, S., Bisswanger, H., Borbe, H. O., & Follmann, H. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00904-n · Cited by 22 · see citing works
Self-citationPark, L. C. H., Gibson, G. E., Bunik, V. I., & Cooper, A. J. L. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00247-6 · Cited by 21 · see citing works
Self-citationDihydrolipoamide-Mediated Redox Cycling of Quinones
Anusevičius, Ž., & Cenas, N. K. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1234 · Cited by 20 · see citing works
Reduction of aryl-nitroso compounds by pyridine and flavin coenzymes
Leskovac, V., Svirčević, J., Trivić, S., Popović, M., & Radulović, M. (1989) · International Journal of Biochemistry · doi:10.1016/0020-711x(89)90279-6 · Cited by 19 · see citing works
Bunik, V. I. (2000) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/s1381-1177(99)00054-5 · Cited by 17 · see citing works
Self-citationWestphal, A. H., Fabisz‐Kijowska, A., Kester, H. A., Obels, P. P., & de Kok, A. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.861_a.x · Cited by 14 · see citing works
Sreider, C. M., Grinblat, L., & Stoppani, A. O. M. (1992) · PubMed · Cited by 14 · see citing works
Magnetic circular dichroism studies on the active-site flavin of lipoamide dehydrogenase
Templeton, D. M., Hollebone, B. R., & Tsai, C. S. (1980) · Biochemistry · doi:10.1021/bi00557a035 · Cited by 11 · see citing works
Spin trapping the cysteine thiyl radical with phenyl-N-t-butylnitrone
Graceffa, P. (1988) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(88)90076-3 · Cited by 11 · see citing works
Reactions of oxidizing and reducing radical probes with lipoamide dehydrogenase
Elliot, A. J., Munk, P. L., Stevenson, K. J., & Armstrong, D. A. (1980) · Biochemistry · doi:10.1021/bi00563a001 · Cited by 7 · see citing works
ChemInform Abstract: Redox Behavior of Active Aldehydes Derived from Thiamin Coenzyme Analogues.
Nakanishi, I., Itoh, S., Suenobu, T., INOUE, H., & Fukuzumi, S. (1997) · ChemInform · doi:10.1002/chin.199749066 · Cited by 2 · see citing works
Nakanishi, I., Itoh, S., Suenobu, T., & Fukuzumi, S. (1998) · ChemInform · doi:10.1002/chin.199803030 · Cited by 1 · see citing works
Flagged first, then by citations
1 of the 93 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- [42]42. Guest, J.R., A li, S.T., A rtymiuk, P., Ford, G.C., Green, J. & Russel, G.C. (1990) Site-directed mutagenesis of dihydrolipoamide acetyltransferase and post-translational modification of its lipoyl domains. In Biochemistry and Physiology of Thiamin Diphosphate Enzymes (Bisswanger, H. & Ullrich, J., eds), pp. 176-193. Chemie, Weinheim.
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Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works
Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release
Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383 · see citing works
Mitochondrial metabolism of reactive oxygen species
Andreyev, A. Y., Kushnareva, Y. E., & Starkov, A. A. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0102-7 · Cited by 1,336 · see citing works
Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063 · see citing works
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Starkov, A. A., Fiskum, G. M., Chinopoulos, C., Lorenzo, B. J., Browne, S. E., Patel, M. S., & Beal, M. F. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1899-04.2004 · Cited by 692 · see citing works
Quinlan, C. L., Orr, A. L., Perevoshchikova, I. V., Treberg, J. R., Ackrell, B. A., & Brand, M. D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.374629 · Cited by 670 · see citing works
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Quinlan, C. L., Perevoshchikova, I. V., Hey‐Mogensen, M., Orr, A. L., & Brand, M. D. (2013) · Redox Biology · doi:10.1016/j.redox.2013.04.005 · Cited by 595 · see citing works
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Tretter, L., & Ádám‐Vizi, V. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1842-04.2004 · Cited by 455 · see citing works
Blue Light Induces Mitochondrial DNA Damage and Free Radical Production in Epithelial Cells
Godley, B. F., Shamsi, F. A., Liang, F.-Q., Jarrett, S. G., Davies, S., & Boulton, M. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502194200 · Cited by 443 · see citing works
Adam-Vizi, V. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.1140 · Cited by 439 · see citing works
Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress
Tretter, L., & Adam-Vizi, V. (2005) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2005.1764 · Cited by 434 · see citing works
Rigoulet, M., Yoboue, E. D., & Devin, A. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3363 · Cited by 394 · see citing works
Interactions between mitochondrial reactive oxygen species and cellular glucose metabolism
Liemburg-Apers, D. C., Willems, P. H. G. M., Koopman, W. J. H., & Grefte, S. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1520-y · Cited by 391 · see citing works
Price‐Whelan, A., Dietrich, L. E. P., & Newman, D. K. (2007) · Journal of Bacteriology · doi:10.1128/jb.00505-07 · Cited by 309 · see citing works
Quinlan, C. L., Goncalves, R. L. S., Hey-Mogensen, M., Yadava, N., Bunik, V. I., & Brand, M. D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.545301 · Cited by 310 · see citing works
Self-citationThe role of mitochondrial function and cellular bioenergetics in ageing and disease
Brand, M. D., Orr, A. L., Perevoshchikova, I. V., & Quinlan, C. L. (2013) · British Journal of Dermatology · doi:10.1111/bjd.12208 · Cited by 292 · see citing works
Aitken, R. J., Whiting, S., Iuliis, G. N. D., McClymont, S., Mitchell, L. A., & Baker, M. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.366690 · Cited by 266 · see citing works
Calcium and Mitochondrial Reactive Oxygen Species Generation: How to Read the Facts
Ádám‐Vizi, V., & Starkov, A. A. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100465 · Cited by 250 · see citing works
Calcium, mitochondria and oxidative stress in neuronal pathology
Chinopoulos, C., & Ádám‐Vizi, V. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2005.05103.x · Cited by 239 · see citing works
Cunha‐Oliveira, T., Montezinho, L., Mendes, C., Firuzi, O., Saso, L., Oliveira, P. J., & Silva, F. S. G. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/5021694 · Cited by 214 · see citing works
Gibson, G. E., Blass, J. P., Beal, M. F., & Bunik, V. I. (2005) · Molecular Neurobiology · doi:10.1385/mn:31:1-3:043 · Cited by 178 · see citing works
Self-citationα-Ketoglutarate dehydrogenase: A mitochondrial redox sensor
McLain, A. L., Szweda, P. A., & Szweda, L. I. (2010) · Free Radical Research · doi:10.3109/10715762.2010.534163 · Cited by 170 · see citing works
Quinlan, C. L., Treberg, J. R., Perevoshchikova, I. V., Orr, A. L., & Brand, M. D. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.08.015 · Cited by 151 · see citing works
Salminen, A., Kauppinen, A., Hiltunen, M. O., & Kaarniranta, K. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.05.004 · Cited by 142 · see citing works
Gibson, G. E., Xu, H., Chen, H., Chen, W., Denton, T. T., & Zhang, S. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13096 · Cited by 137 · see citing works
Free radical oxidation of proteins and its relationship with functional state of organisms
Lushchak, V. I. (2007) · Biochemistry (Moscow) · doi:10.1134/s0006297907080020 · Cited by 131 · see citing works
Bunik, V. I., & Fernie, A. R. (2009) · Biochemical Journal · doi:10.1042/bj20090722 · Cited by 128 · see citing works
Self-citationMkrtchyan, G. V., Aleshin, V. A., IuM, P., Kaehne, T., di Salvo, M. L., Parroni, A., Contestabile, R., Vovk, A. I., Bettendorff, L., & Bunik, V. I. (2015) · Scientific Reports · doi:10.1038/srep12583 · Cited by 128 · see citing works
Self-citationRalph, S. J., Moreno-Sánchez, R., Neuzil, J., & Rodríguez-Enríquez, S. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0566-7 · Cited by 126 · see citing works
2‐Oxo acid dehydrogenase complexes in redox regulation
Bunik, V. I. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03470.x · Cited by 125 · see citing works
Self-citationA Mitocentric View of Alzheimer's Disease Suggests Multi-Faceted Treatments
Gibson, G. E., & Shi, Q. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-100336 · Cited by 124 · see citing works
Fisher‐Wellman, K. H., Lin, C., RYAN, T. E., Reese, L., Gilliam, L. A. A., Cathey, B. L., Lark, D. S., Smith, C. D., Muoio, D. M., & Neufer, P. D. (2015) · Biochemical Journal · doi:10.1042/bj20141447 · Cited by 121 · see citing works
Fisher‐Wellman, K. H., Gilliam, L. A. A., Lin, C., Cathey, B. L., Lark, D. S., & Neufer, P. D. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.09.008 · Cited by 115 · see citing works
Bunik, V. I., Tylicki, A., & Lukashev, N. V. (2013) · FEBS Journal · doi:10.1111/febs.12512 · Cited by 115 · see citing works
Self-citationPro-oxidant actions of α-lipoic acid and dihydrolipoic acid
Çakatay, U. (2005) · Medical Hypotheses · doi:10.1016/j.mehy.2005.07.020 · Cited by 112 · see citing works
Characteristics of α‐glycerophosphate‐evoked H2O2 generation in brain mitochondria
Tretter, L., Takacs, K., Hegedus, V., & Ádám‐Vizi, V. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04223.x · Cited by 109 · see citing works
Thiamine-Dependent Processes and Treatment Strategies in Neurodegeneration
Gibson, G. E., & Blass, J. P. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1766 · Cited by 107 · see citing works
Quinlan, C. L., Perevoschikova, I. V., Goncalves, R. L. S., Hey‐Mogensen, M., & Brand, M. D. (2013) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-405883-5.00012-0 · Cited by 98 · see citing works
Fernández-Checa, J. C., Fernandez, A., Morales, A., Marı́, M., García‐Ruiz, C., & Colell, A. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710791556113 · Cited by 98 · see citing works
Mailloux, R. J., Ayre, D. C., & Christian, S. L. (2016) · Redox Biology · doi:10.1016/j.redox.2016.02.002 · Cited by 97 · see citing works
Mitochondrial production of reactive oxygen species
Grivennikova, V. G., & Vinogradov, A. D. (2013) · Biochemistry (Moscow) · doi:10.1134/s0006297913130087 · Cited by 96 · see citing works
Zündorf, G., Kahlert, S., Bunik, V. I., & Reiser, G. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.10.015 · Cited by 76 · see citing works
Self-citationHansen, G. E., & Gibson, G. E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012403 · Cited by 77 · see citing works
Lord, T., Martin, J. H., & Aitken, R. J. (2014) · Biology of Reproduction · doi:10.1095/biolreprod.114.122820 · Cited by 71 · see citing works
The role of mitochondrial dehydrogenases in the generation of oxidative stress
Ádám‐Vizi, V., & Tretter, L. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.01.012 · Cited by 69 · see citing works
Oxidative Stress and Redox Signaling in the Pathophysiology of Liver Diseases
Mooli, R. G. R., Mukhi, D., & Ramakrishnan, S. K. (2022) · Comprehensive physiology · doi:10.1002/cphy.c200021 · Cited by 128 · see citing works
Reactive Oxygen Species in intestinal stem cell metabolism, fate and function
Morris, O., & Jasper, H. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.02.015 · Cited by 68 · see citing works
McLain, A. L., Cormier, P. J., Kinter, M. T., & Szweda, L. I. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.03.020 · Cited by 65 · see citing works
Aging: A shift from redox regulation to oxidative damage
Humphries, K. M., Szweda, P. A., & Szweda, L. I. (2006) · Free Radical Research · doi:10.1080/10715760600913184 · Cited by 64 · see citing works
Ambrus, A., Nemeria, N. S., Törőcsik, B., Tretter, L., Nilsson, M., Jordan, F., & Ádám‐Vizi, V. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.10.001 · Cited by 64 · see citing works
Huang, H.-M., Ou, H., Xu, H., Chen, H.-L., Fowler, C., & Gibson, G. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10756 · Cited by 61 · see citing works
Carrozzo, R., Torraco, A., Fiermonte, G., Martinelli, D., Nottia, M. D., Rizza, T., Vozza, A., Verrigni, D., Diodato, D., Parisi, G., et al. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.09.006 · Cited by 61 · see citing works
An update on the role of mitochondrial α-ketoglutarate dehydrogenase in oxidative stress
Starkov, A. A. (2012) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2012.07.005 · Cited by 60 · see citing works
Ambrus, A., Tretter, L., & Ádám‐Vizi, V. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05942.x · Cited by 58 · see citing works
Ambrus, A., & Ádám‐Vizi, V. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.05.018 · Cited by 54 · see citing works
Ambrus, A., Törőcsik, B., Tretter, L., Ozohanics, O., & Ádám‐Vizi, V. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr202 · Cited by 54 · see citing works
Nemeria, N. S., Ambrus, A., Patel, H., Gerfen, G. J., Ádám‐Vizi, V., Tretter, L., Zhou, J., Wang, J., & Jordan, F. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.591073 · Cited by 53 · see citing works
Lipoic acid and lipoic acid analogs in cancer metabolism and chemotherapy
Bingham, P. M., Stuart, S. D., & Zachar, Z. (2014) · Expert Review of Clinical Pharmacology · doi:10.1586/17512433.2014.966816 · Cited by 53 · see citing works
Oxidative Stress and Redox Signaling in the Pathophysiology of Liver Diseases
Mooli, R. G. R., Mukhi, D., & Ramakrishnan, S. K. (2022) · Comprehensive physiology · doi:10.1002/j.2040-4603.2022.tb00210.x · Cited by 53 · see citing works
Martin, J. H., Nixon, B., Cafe, S. L., Aitken, R. J., Bromfield, E. G., & Lord, T. (2022) · Reproduction · doi:10.1530/rep-22-0206 · Cited by 50 · see citing works
Cerebrometabolic abnormalities in Alzheimer's disease
Blass, J. P. (2003) · Neurological Research · doi:10.1179/016164103101201995 · Cited by 49 · see citing works
Bunik, V. I., Schloss, J. V., Pinto, J. T., Gibson, G. E., & Cooper, A. J. L. (2007) · Neurochemical Research · doi:10.1007/s11064-006-9239-z · Cited by 43 · see citing works
Self-citationBunik, V. I., Mkrtchyan, G. V., Grabarska, A., Oppermann, H., Daloso, D. M., Araújo, W. L., Juszczak, M., Rzeski, W., Bettendorff, L., Fernie, A. R., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.8387 · Cited by 43 · see citing works
Self-citationHughey, C. C., Puchalska, P., & Crawford, P. A. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2022.159209 · Cited by 42 · see citing works
Enzyme Complexes Important for the Glutamate–Glutamine Cycle
McKenna, M. C., & Ferreira, G. C. (2016) · Advances in neurobiology · doi:10.1007/978-3-319-45096-4_4 · Cited by 35 · see citing works
Shi, Q., Chen, H., Xu, H., & Gibson, G. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409064200 · Cited by 38 · see citing works
Bunik, V. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7311 · Cited by 38 · see citing works
Self-citationStrumiło, S. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0177-1 · Cited by 37 · see citing works
Komary, Z., Tretter, L., & Ádám‐Vizi, V. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.03.010 · Cited by 35 · see citing works
[Mitochondrial reactive oxygen species].
Nishikawa, T., Kukidome, D., & Araki, E. (2016) · PubMed · Cited by 38 · see citing works
Nagy, B., Polak, M., Ozohanics, O., Zámbó, Z., Szabó, E., Hubert, Á., Jordan, F., Nováček, J., Ádám‐Vizi, V., & Ambrus, A. (2021) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2021.129889 · Cited by 33 · see citing works
Ambrus, A., & Ádám‐Vizi, V. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.08.015 · Cited by 31 · see citing works
Bonke, E., Siebels, I., Zwicker, K., & Dröse, S. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.07.026 · Cited by 30 · see citing works
Bunik, V. I., & Brand, M. D. (2018) · Biological Chemistry · doi:10.1515/hsz-2017-0284 · Cited by 29 · see citing works
Self-citationMatesanz, N., Lafuente, N., Azcutia, V., Martı́n, D., Cuadrado, A., Nevado, J. B., Rodríguez‐Mañas, L., Sánchez‐Ferrer, C. F., & Peiró, C. (2007) · Journal of Hypertension · doi:10.1097/hjh.0b013e328013e7c4 · Cited by 29 · see citing works
Nemeria, N. S., Gerfen, G. J., Yang, L., Zhang, X., & Jordan, F. (2018) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2018.05.001 · Cited by 28 · see citing works
Mailloux, R. J. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103155 · Cited by 27 · see citing works
Measurement of ROS Homeostasis in Isolated Mitochondria
Tretter, L., & Ambrus, A. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801415-8.00012-6 · Cited by 27 · see citing works
Kabysheva, M. S., Storozhevykh, T. P., Pinelis, V. G., & Bunik, V. I. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.02.001 · Cited by 27 · see citing works
Self-citationBunik, V. I., Schloss, J. V., Pinto, J. T., Dudareva, N., & Cooper, A. J. L. (2011) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470920541.ch7 · Cited by 27 · see citing works
Self-citationBezerra, G. A., Foster, W. R., Bailey, H., Hicks, K. G., Sauer, S. W., Dimitrov, B., McCorvie, T. J., Okun, J. G., Rutter, J. P., Kölker, S., et al. (2020) · IUCrJ · doi:10.1107/s205225252000696x · Cited by 26 · see citing works
Fleminger, G., & Dayan, A. (2021) · Journal of Molecular Recognition · doi:10.1002/jmr.2924 · Cited by 26 · see citing works
Parkhomenko, Y. M., Kudryavtsev, P. A., Pylypchuk, S. Y., Chekhivska, L. I., Stepanenko, S. P., Sergiichuk, A. A., & Bunik, V. I. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07283.x · Cited by 26 · see citing works
Self-citationDuong, Q. V., Levitsky, Y., Dessinger, M. J., Strubbe, J. O., & Bazil, J. N. (2021) · Function · doi:10.1093/function/zqab050 · Cited by 26 · see citing works
Ammonium‐dependent hydrogen peroxide production by mitochondria
Grivennikova, V. G., Cecchini, G., & Vinogradov, A. D. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.06.054 · Cited by 25 · see citing works
Role of 2-oxoglutarate dehydrogenase in brain pathologies involving glutamate neurotoxicity
Graf, A. V., Kabysheva, M. S., Klimuk, E. I., Trofimova, L. K., Dunaeva, T. Y., Zündorf, G., Kahlert, S., Reiser, G., Storozhevykh, T. P., Pinelis, V. G., et al. (2009) · Journal of Molecular Catalysis B Enzymatic · doi:10.1016/j.molcatb.2009.02.016 · Cited by 24 · see citing works
Self-citationGonzález-Fernández, R., Martı́nez-Galisteo, E., Gaytán, F., Bárcena, J. A., & Sánchez‐Criado, J. E. (2008) · Biology of Reproduction · doi:10.1095/biolreprod.107.065474 · Cited by 24 · see citing works
Trofimova, L. K., Lovat, M. L., Groznaya, A., Efimova, E. V., Dunaeva, T. Y., Maslova, M. V., Graf, A. V., & Bunik, V. I. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2010/749061 · Cited by 23 · see citing works
Self-citationHorváth, G., Sváb, G., Komlódi, T., Ravasz, D., Kacsó, G., Dóczi, J., Chinopoulos, C., Ambrus, A., & Tretter, L. (2022) · Antioxidants · doi:10.3390/antiox11081487 · Cited by 21 · see citing works
Grayson, C., Faerman, B., Koufos, O., & Mailloux, R. J. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107159 · Cited by 21 · see citing works
Jordan, F., Nemeria, N. S., & Gerfen, G. J. (2019) · Neurochemical Research · doi:10.1007/s11064-019-02765-w · Cited by 21 · see citing works
Bunik, V. I., & Strumiło, S. (2009) · Current Chemical Biology · doi:10.2174/187231309789054904 · Cited by 20 · see citing works
Self-citationBunik, V. I., Raddatz, G., Wanders, R. J. A., & Reiser, G. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.05.040 · Cited by 20 · see citing works
Self-citationEffect of metformin on intact mitochondria from liver and brain: Concept revisited
Yoval‐Sánchez, B., Ansari, F., Lange, D., & Galkin, A. S. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.175177 · Cited by 20 · see citing works
Das, S., Bhattacharyya, J., & Mukhopadhyay, S. (2006) · Helvetica Chimica Acta · doi:10.1002/hlca.200690186 · Cited by 19 · see citing works
Brain bioenergetics in rats with acute hyperphenylalaninemia
Dimer, N. W., Ferreira, B. K., Agostini, J. F., Gomes, M. L., Kist, L. W., Malgarin, F., Carvalho‐Silva, M., Gomes, L. M., Rebelo, J., Frederico, M. J. S., et al. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2018.01.001 · Cited by 17 · see citing works
Bunik, V. I., Aleshin, V. A., Zhou, X., Tabakov, V. Y., & Karlsson, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113759 · Cited by 17 · see citing works
Self-citationArtiukhov, A. V., Graf, A. V., & Bunik, V. I. (2016) · Biochemistry (Moscow) · doi:10.1134/s0006297916120129 · Cited by 17 · see citing works
Self-citation
- Authors
- Bunik, V. I., & Sievers, C.
- Affiliations
- Lomonosov Moscow State University (RU)
- University of Tübingen (DE)
- ORCID
- Bunik, Victoria I.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 2002-09-27
- Volume
- 269
- Issue
- 20
- Pages
- 5004-5015
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1488079166
- Cited by
- 134
- References
- 93
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 3 · 2023: 2 · 2022: 7 · 2021: 9 · 2020: 3 · 2019: 2 · 2018: 6 · 2017: 2 · 2016: 7 · 2015: 7 · 2014: 8 · 2013: 10 · 2012: 6
- FWCI
- 2.39
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- European Journal of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- enzyme inactivation, thiyl radicals, FAD, superoxide, thioredoxin, reactive oxygen species, spin trapping, DMPO, alpha-ketoglutarate, NAD+, pro-oxidant activity
- MeSH terms
- Catalysis, Coenzyme A, Cyclic N-Oxides, Electron Spin Resonance Spectroscopy, Enzyme Activation, Flavin-Adenine Dinucleotide, Free Radicals, Ketone Oxidoreductases, Thioctic Acid, Multienzyme Complexes, NAD, Nitrogen Oxides, Spin Labels, Superoxides, Thioredoxins, 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)
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