The inactivation of Fe-S cluster containing hydro-lyases by superoxide
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We report in this paper that highly purified Escherichia coli dihydroxy-acid dehydratase, fumarase A, fumarase B, and mammalian aconitase are inactivated by O2- with second order rate constants in the range of 10(6) to 10(7) M-1 s-1. Each of these enzymes belongs to the hydro-lyase class and contains catalytically active [4Fe-4S] clusters. Simultaneous with inactivation by O2- is the release of iron from their clusters. Our working hypothesis is O2- inactivates these enzymes by oxidizing their clusters to an unstable oxidation state, and cluster degradation follows. Consistent with this hypothesis is our observation that spinach dihydroxy-acid dehydratase, a member of the hydro-lyase class that has a catalytically active [2Fe-2S] cluster, is not inactivated and does not lose iron in the presence of O2-. Porcine fumarase, a member of the hydro-lyase class that does not contain an Fe-S cluster, is also not inactivated by O2-. We also report the rate constants for the inactivation of E. coli dihydroxy-acid dehydratase, fumarase A, fumarase B, and mammalian aconitase by O2 are close to 2 x 10(2) M-1 s-1, and the rate constants for the inactivation of E. coli dihydroxy-acid dehydratase and mammalian aconitase by H2O2 are about 10(3) M-1 s-1. E. coli dihydroxy-acid dehydratase has been reported previously to be inactivated in vivo when cells are grown in hyperbaric O2, presumably due to the increased O2- generated under these conditions. We report here that E. coli fumarase A, fumarase B, and aconitase are also inactivated in vivo by hyperbaric O2. Thermodynamic parameters for the oxidation of the cluster of aconitase by O2- and O2 are calculated.
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Reactions of superoxide with iron/sulphur protein groups have rate constants in excess of 10^6 M−1 s−1 and are highly selective for superoxide.
“These reactions have rate constants in excess of 106 M−1 s−1 and are highly selective for the superoxide [107].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [107]
The best-established detrimental effect of superoxide is inactivation of iron/sulphur protein groups, such as aconitase and bacterial dehydratases required for branched-chain amino acid synthesis.
“The best-established detrimental effect of superoxide is the inactivation of iron/sulphur protein groups, such as aconitase, and bacterial dehydratases required for branched-chain amino acid synthesis.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [107]
Cites
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952 · see citing works
Biological effects of the superoxide radical
Fridovich, I. (1986) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(86)90526-6 · Cited by 1,422 · see citing works
Sawyer, D. T., & Valentine, J. S. (1981) · Accounts of Chemical Research · doi:10.1021/ar00072a005 · Cited by 1,352 · see citing works
An Enzyme-Based Theory of Obligate Anaerobiosis: The Physiological Function of Superoxide Dismutase
McCord, J. M., Keele, B. B., & Fridovich, I. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.5.1024 · Cited by 976 · see citing works
Generation of superoxide by purified brain nitric oxide synthase
Pou, S., Pou, W. S., Bredt, D. S., Snyder, S. H., & Rosen, G. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35745-4 · Cited by 750 · see citing works
Superoxide sensitivity of the Escherichia coli aconitase.
Gardner, P. R., & Fridovich, I. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55001-8 · Cited by 514 · see citing works
Cellular mechanisms of oxygen toxicity.
Haugaard, N. (1968) · Physiological Reviews · doi:10.1152/physrev.1968.48.2.311 · Cited by 513 · see citing works
Klug-Roth, D., Rabani, J., & Fridovich, I. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44987-9 · Cited by 495 · see citing works
Superoxide radical and superoxide dismutase
Fridovich, I. (1972) · Accounts of Chemical Research · doi:10.1021/ar50058a001 · Cited by 472 · see citing works
The role of iron in the activation-inactivation of aconitase.
Kennedy, M. C., Emptage, M. H., Dreyer, J.-L., & Beinert, H. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44390-0 · Cited by 377 · see citing works
Self-citationSuperoxide radical and the oxygen enhancement of the toxicity of paraquat in Escherichia coli.
Hassan, H. M., & Fridovich, I. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34373-9 · Cited by 305 · see citing works
Paraquat and Escherichia coli. Mechanism of production of extracellular superoxide radical.
Hassan, H. M., & Fridovich, I. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86598-5 · Cited by 293 · see citing works
alpha, beta-Dihydroxyisovalerate dehydratase. A superoxide-sensitive enzyme.
Kuo, C. F., Mashino, T., & Fridovich, I. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61255-4 · Cited by 247 · see citing works
Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal.
Robbins, A. H., & Stout, C. D. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.10.3639 · Cited by 245 · see citing works
CRYSTAL STRUCTURES OF ACONITASE WITH ISOCITRATE AND NITROISOCITRATE BOUND
Lauble, H., Kennedy, M. C., Beinert, H., & Stout, C. D. (1991) · Biochemistry · doi:10.1021/bi00125a014 · Cited by 216 · see citing works
Two biochemically distinct classes of fumarase in Escherichia coli
Woods, S. A., Schwartzbach, S. D., & Guest, J. R. (1988) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(88)90050-7 · Cited by 206 · see citing works
The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase
Flint, D. H., Emptage, M. H., Finnegan, M. G., Fu, W., & Johnson, M. K. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82394-8 · Cited by 150 · see citing works
Self-citationOptical and EPR characterization of different species of active and inactive aconitase.
Emptage, M. H., Dreyers, J. L., Kennedy, M. C., & Beinert, H. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44391-2 · Cited by 141 · see citing works
Self-citationEmptage, M. H., Kent, T. A., Kennedy, M. C., Beinert, H., & Münck, E. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.15.4674 · Cited by 133 · see citing works
Self-citationThe kinetics of the reduction of cytochrome c by the superoxide anion radical
Koppenol, W. H., Buuren, K. J. H. V., Butler, J., & Braams, R. (1976) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(76)90130-4 · Cited by 126 · see citing works
Rotilio, G., Calabrese, L., Bossa, F., Barra, D., Finazzi‐Agrò, A., & Mondovı̀, B. (1972) · Biochemistry · doi:10.1021/bi00761a027 · Cited by 124 · see citing works
Biosynthesis of branched chain amino acids
(1991) · International Journal of Biochemistry · doi:10.1016/0020-711x(91)90099-9 · Cited by 121 · see citing works
Flint, D. H., Emptage, M. H., & Guest, J. R. (1992) · Biochemistry · doi:10.1021/bi00157a022 · Cited by 112 · see citing works
Self-citationDihydroxy acid dehydratase from spinach contains a [2Fe-2S] cluster.
Flint, D. H., & Emptage, M. H. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68961-6 · Cited by 102 · see citing works
Self-citationOxygen and toxicity inhibition of amino acid biosynthesis
Boehme, D., VINCENT, K., & Brown, O. R. (1976) · Nature · doi:10.1038/262418a0 · Cited by 101 · see citing works
Effect of Hyperbaric Oxygen on Microorganisms
Gottlieb, S. F. (1971) · Annual Review of Microbiology · doi:10.1146/annurev.mi.25.100171.000551 · Cited by 100 · see citing works
Fridovich, I. (1975) · PubMed · Cited by 96 · see citing works
Lactate reduction in Clostridium propionicum. Purification and properties of lactyl-CoA dehydratase.
Kuchta, R. D., & Abeles, R. H. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38854-3 · Cited by 93 · see citing works
Modulation of the Fumarases of Escherichia coli in Response to Oxidative Stress
Liochev, S. I., & Fridovich, I. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1159 · Cited by 72 · see citing works
Kennedy, M. C., Werst, M., Telser, J., Emptage, M. H., Beinert, H., & Hoffman, B. M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.24.8854 · Cited by 72 · see citing works
Self-citationThe aconitase of Escherichia coli
Prodromou, C., Artymiuk, P. J., & Guest, J. R. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb16673.x · Cited by 71 · see citing works
Scopes, R. K., & Griffiths-Smith, K. (1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90257-4 · Cited by 62 · see citing works
Schweiger, G., Dutscho, R., & Buckel, W. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb13631.x · Cited by 61 · see citing works
Brown, O. R., & Yein, F. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)90672-1 · Cited by 60 · see citing works
Telser, J., Emptage, M. H., Merkle, H., et al. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)89181-0 · Cited by 58 · see citing works
Self-citationGrabowski, R., & Buckel, W. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16095.x · Cited by 49 · see citing works
Isolation and biochemical characterization of maleic‐acid hydratase, an iron‐requiring hydro‐lyase
Dreyer, J. (1985) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1985.tb09000.x · Cited by 43 · see citing works
Max, B. (1992) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(92)90084-j · Cited by 37 · see citing works
Prodromou, C., Haynes, M. J., & Guest, J. R. (1991) · Journal of General Microbiology · doi:10.1099/00221287-137-11-2505 · Cited by 35 · see citing works
L‐(+)‐Tartrate dehydratase from Pseudomonas putida is an iron‐sulphur enzyme
Kelly, J. M., & Scopes, R. K. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)80700-1 · Cited by 22 · see citing works
Near ultraviolet light inactivation of dihydroxyacid dehydratase in Escherichia coli
Smyk-Randall, E. M., Brown, O. R., Wilke, A. L., Eisenstark, A., & Flint, D. H. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90142-h · Cited by 21 · see citing works
Self-citationThe Stereochemistry of 1,2,3-Trihydroxy-3-methylbutane and 2,3-Dihydroxy-3-methylbutyric Acid.
Nielsen, B. E., LARSEN, P., Lemmich, J., et al. (1969) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.23-0967 · Cited by 14 · see citing works
[101] α,β-Dihydroxy acid dehydratase (Neurospora crassa and spinach)
Kiritani, K., & Wagner, R. P. (1970) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(71)17276-x · Cited by 11 · see citing works
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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
The Free Radical Theory of Aging Matures
BECKMAN, K. B., & AMES, B. N. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.2.547 · Cited by 3,879 · see citing works
Reconciling the chemistry and biology of reactive oxygen species
Winterbourn, C. C. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.85 · Cited by 2,504 · see citing works
Antimicrobial reactive oxygen and nitrogen species: concepts and controversies
Fang, F. C. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro1004 · Cited by 1,676 · see citing works
Cellular Defenses against Superoxide and Hydrogen Peroxide
Imlay, J. A. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061606.161055 · Cited by 1,563 · see citing works
Role of oxidative stress in cardiovascular diseases
Dhalla, N. S., Temsah, R. M., & Netticadan, T. (2000) · Journal of Hypertension · doi:10.1097/00004872-200018060-00002 · Cited by 1,467 · see citing works
A Review of the Antioxidant Mechanisms of Polyphenol Compounds Related to Iron Binding
Perron, N. R., & Brumaghim, J. L. (2009) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-009-9043-x · Cited by 1,370 · see citing works
The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
Macomber, L., & Imlay, J. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812808106 · Cited by 1,117 · see citing works
Mitochondria, oxygen free radicals, disease and ageing
Raha, S., & Robinson, B. H. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01674-1 · Cited by 1,066 · see citing works
Superoxide accelerates DNA damage by elevating free-iron levels
Keyer, K., & Imlay, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13635 · Cited by 841 · see citing works
Tarpey, M. M., Wink, D. A., & Grisham, M. B. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00361.2003 · Cited by 673 · see citing works
Elchuri, S., Oberley, T. D., Qi, W., Eisenstein, R. S., Jackson Roberts, L., Van Remmen, H., Epstein, C. J., & Huang, T.-T. (2005) · Oncogene · doi:10.1038/sj.onc.1208207 · Cited by 667 · see citing works
Aconitase as iron–sulfur protein, enzyme, and iron-regulatory protein
Beinert, H., Kennedy, M. C., & Stout, C. D. (1996) · Chemical Reviews · doi:10.1021/cr950040z · Cited by 606 · see citing works
Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide.
Castro, L., Rodriguez, M., & Radi, R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43894-x · Cited by 589 · see citing works
Vardhana, S. A., Hwee, M. A., Berisa, M., Wells, D. K., Yost, K. E., King, B., Smith, M., Herrera, P. S., Chang, H. Y., Satpathy, A. T., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-0725-2 · Cited by 575 · see citing works
Mitochondrial disease in superoxide dismutase 2 mutant mice
Melov, S., Coskun, P., Patel, M., Tuinstra, R., Cottrell, B., Jun, A. S., Zastawny, T. H., Dizdaroglu, M., Goodman, S. I., Huang, T.-T., et al. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.3.846 · Cited by 581 · see citing works
Superoxide dismutases—A review of the metal-associated mechanistic variations
Abreu, I. A., & Cabelli, D. E. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.11.005 · Cited by 563 · see citing works
Somatic mtDNA mutations cause aging phenotypes without affecting reactive oxygen species production
Trifunovic, A., Hansson, A., Wredenberg, A., Rovio, A. T., Dufour, E., Khvorostov, I., Spelbrink, J. N., Wibom, R., Jacobs, H. T., & Larsson, N.-G. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508886102 · Cited by 555 · see citing works
Macomber, L., Rensing, C., & Imlay, J. A. (2007) · Journal of Bacteriology · doi:10.1128/jb.01357-06 · Cited by 356 · see citing works
Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
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When anaerobes encounter oxygen: mechanisms of oxygen toxicity, tolerance and defence
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Raha, S., & Robinson, B. H. (2001) · American Journal of Medical Genetics · doi:10.1002/ajmg.1398 · Cited by 306 · see citing works
Messner, K. R., & Imlay, J. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204958200 · Cited by 301 · see citing works
Rotenone Model of Parkinson Disease
Panov, A., Dikalov, S., Shalbuyeva, N., Taylor, G., Sherer, T., & Greenamyre, J. T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508628200 · Cited by 288 · see citing works
Iron–sulfur proteins with nonredox functions
Flint, D. H., & Allen, R. M. (1996) · Chemical Reviews · doi:10.1021/cr950041r · Cited by 280 · see citing works
Self-citationNrf2-dependent persistent oxidative stress results in stress-induced vulnerability to depression
Bouvier, E., Brouillard, F., Molet, J., Claverie, D., Cabungcal, J.-H., Cresto, N., Doligez, N., Rivat, C., Do, K. Q., Bernard, C., et al. (2017) · Molecular Psychiatry · doi:10.1038/mp.2016.144 · Cited by 248 · see citing works
Staphylococcal response to oxidative stress
Gaupp, R., Ledala, N., & Somerville, G. A. (2012) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00033 · Cited by 253 · see citing works
Oxidative Stress and the Homeodynamics of Iron Metabolism
Bresgen, N., & Eckl, P. (2015) · Biomolecules · doi:10.3390/biom5020808 · Cited by 247 · see citing works
Superoxide-Driven Aconitase FE-S Center Cycling
Gardner, P. R. (1997) · Bioscience Reports · doi:10.1023/a:1027383100936 · Cited by 190 · see citing works
Suppressors of Superoxide Dismutase (SOD1) Deficiency in Saccharomyces cerevisiae
Strain, J., Lorenz, C. R., Bode, J., Garland, S., Smolen, G. A., Ta, D. T., Vickery, L. E., & Culotta, V. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.47.31138 · Cited by 181 · see citing works
Woodmansee, A. N., & Imlay, J. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203977200 · Cited by 152 · see citing works
One- and two-electron oxidation of thiols: mechanisms, kinetics and biological fates
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Castro, L. A., Robalinho, R. L., Cayota, A., Meneghini, R., & Radi, R. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0898 · Cited by 98 · see citing works
Otte, D.-M., Sommersberg, B., Kudin, A., Guerrero, C., Albayram, Ö., Filiou, M. D., Frisch, P., Yilmaz, Ö., Drews, E., Turck, C. W., et al. (2011) · Neuropsychopharmacology · doi:10.1038/npp.2011.109 · Cited by 97 · see citing works
Roberts, C. A., Al-Tameemi, H. M., Mashruwala, A. A., Rosario-Cruz, Z., Chauhan, U., Sause, W. E., Torres, V. J., Belden, W. J., & Boyd, J. M. (2017) · Infection and Immunity · doi:10.1128/iai.00100-17 · Cited by 84 · see citing works
Mashruwala, A. A., Pang, Y. Y., Rosario‐Cruz, Z., Chahal, H. K., Benson, M. A., Mike, L. A., Skaar, E. P., Torres, V. J., Nauseef, W. M., & Boyd, J. M. (2015) · Molecular Microbiology · doi:10.1111/mmi.12860 · Cited by 79 · see citing works
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Modulation by nitric oxide of metalloprotein regulatory activities
Drapier, J., & Bouton, C. (1996) · BioEssays · doi:10.1002/bies.950180706 · Cited by 71 · see citing works
Ganini, D., Santos, J. H., Bonini, M. G., & Mason, R. P. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2018.01.007 · Cited by 59 · see citing works
Martínez, A., Prolo, C., Estrada, D., Rios, N., Alvarez, M. N., Piñeyro, M. D., Robello, C., Radi, R., & Piacenza, L. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1821487116 · Cited by 41 · see citing works
Martien, J. I., Hebert, A. S., Stevenson, D. M., Regner, M. R., Khana, D. B., Coon, J. J., & Amador-Noguez, D. (2019) · mSystems · doi:10.1128/msystems.00284-18 · Cited by 34 · see citing works
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Briones-Martin-del-Campo, M., Orta-Zavalza, E., Cañas-Villamar, I., Gutiérrez-Escobedo, G., Juárez-Cepeda, J., Robledo-Márquez, K., Arroyo-Helguera, O., Castaño, I., & De Las Peñas, A. (2015) · Microbiology · doi:10.1099/mic.0.000006 · Cited by 29 · see citing works
- Authors
- Flint, D. H., Tuminello, J. F., & Emptage, M. H.
- Affiliations
- DuPont (United States) (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-10
- Volume
- 268
- Issue
- 30
- Pages
- 22369-22376
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1559173033
- Cited by
- 637
- References
- 43
- Citations by year
- 2026: 9 · 2025: 8 · 2024: 17 · 2023: 11 · 2022: 21 · 2021: 17 · 2020: 12 · 2019: 19 · 2018: 20 · 2017: 26 · 2016: 14 · 2015: 28 · 2014: 29 · 2013: 36 · 2012: 20
- FWCI
- 19.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- superoxide, aconitase, [4Fe-4S] cluster, [2Fe-2S] cluster, iron release, hyperbaric oxygen therapy, hydrogen peroxide, enzyme inactivation kinetics, Escherichia coli
- MeSH terms
- Aconitate Hydratase, Animals, Escherichia coli, Fumarate Hydratase, Hydro-Lyases, Iron, Iron-Sulfur Proteins, Isoenzymes, Kinetics, Mammals, Mathematics, Mitochondria, Models, Theoretical, Superoxides, Vegetables
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