Commentary: The Role of Iron-Sulfur Clusters in in vivo Hydroxyl Radical Production

References

• Liochev S. I., Fridovich I. The role of O2 in the production of HO: in vitro and in vivo. Free Radical Biology and Medicine 1994; 16: 29–33
   PubMed Web of Science ®Google Scholar
• McCord J. M., Fridovich I. Superoxide dis-mutase. An enzymic function for erythrocuprein (hemocuprein). Journal of Biological Chemistry 1969; 244: 6049–6055
   PubMed Web of Science ®Google Scholar
• McCord J. M., Keele B. B., Jr., Fridovich I. An enzyme based theory of obligate anaerobiosis: the physiological function of superoxide dismutase. Proceedings of the National Academy of Sciences, U.S.A. 1971; 68: 1024–1027
   PubMed Web of Science ®Google Scholar
• Fee J. A. Is superoxide toxic and are superoxide dismutases essential for aerobic life? (and the following discussion). Oxygen and Oxy-radicals in Chemistry and Biology, M. A. J. Rodgers, E. L. Powers. Academic Press, New York 1981; 205–239
   Google Scholar
• Fee J. A. On the question of superoxide toxicity and the biological function of superoxide dismutase. (and the following discussion). Oxidases and Related Redox Systems, T. E. King, H. S. Mason, M. Morrison. Pergamon Press, Oxford, New York 1982; 101–149
   Google Scholar
• Weser U., Paschen W. Singlet oxygen and superoxide dismutase (cuprein). Biochemical and Biophysical Research Communications 1975; 66: 769–777
   PubMedGoogle Scholar
• Hodgson E. K., Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: chemiluminescence and peroxidation. Biochemistry 1975; 14: 5299–5303
   PubMed Web of Science ®Google Scholar
• Ischiropoulos H., Zhu L., Chen J., Tsai M., Martin J. C., Smith C. D., Beckman J. S. Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase. Archives of Biochemistry and Biophysics 1992; 298: 431–437
   PubMed Web of Science ®Google Scholar
• Crow J. P., Sampson J., Beckman J. S. A gained function for SOD mutants in amyotropic lateral sclerosis (ALS): formation of zinc-deficient SOD enhances nitration of neurofilaments by peroxynitrite. Oxygen 95, The Annual Meeting of the Oxygen Society. Program and Abstracts: A-29 abstr. 1995
   Google Scholar
• Wiedau-Pazos M., Goto J. J., Rabizadeh S., Gralla E. B., Roe J. A., Lee M. K., Valentine J. S., Bredesen D. E. Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science 1996; 271: 515–518
   PubMed Web of Science ®Google Scholar
• Fee J. A. Is superoxide toxic?. Biological and Clinical Aspects of Superoxide and Superoxide Dismutase. Developments in Biochemistry, vol. 11B, W. H. Bannister, J. V. Bannister. Elsevier/North-Holland, New York 1980; 41–48
   Google Scholar
• Fee J. A. Regulation of sod genes in Escherichia coli: relevance to superoxide dismutase function. Molecular Microbiology 1991; 5: 2599–2610
   PubMed Web of Science ®Google Scholar
• Marklund S., Marklund G. Involvement of the superoxide anion radical in the autooxidation of pyrogallol and a convenient assay for superoxide dismutase. European Journal of Biochemistry 1974; 47: 469–474
   PubMedGoogle Scholar
• Cohen G., Heikkila R. The generation of hydrogen peroxide, superoxide radical and hydroxyl radical by 6-hydroxydopamine, dialuric acid, and related cytotoxic agents. Journal of Biological Chemistry 1974; 8: 2447–2452
   Google Scholar
• Winterbourn C. C., Metodiewa D. The reaction of superoxide with reduced glutathione. Archives of Biochemistry and Biophysics 1994; 314: 284–90
   PubMed Web of Science ®Google Scholar
• Bielski B. H. J., Chan P. C. Enzyme catalyzed free radical chain reactions with nitcotinamide nucleotides. I. Lactate dehydrogenase-catalyzed chain oxidation of bound NADH by superoxide radicals. Archives of Biochemistry and Biophysics 1973; 159: 873–879
   Web of Science ®Google Scholar
• Liochev S. I., Fridovich I. Vanadate-stimu-lated oxidation of NAD(P)H in the presence of biological membranes and other sources of O2. Archives of Biochemistry and Biophysics 1990; 279: 1–7
   PubMed Web of Science ®Google Scholar
• Kono Y., Fridovich I. Superoxide radical inhibits catalase. Journal of Biological Chemistry 1982; 257: 5751–5754
   PubMed Web of Science ®Google Scholar
• Blum J., Fridovich I. Inactivation of glutathione peroxidase by superoxide radical. Archives of Biochemistry and Biophysics 1985; 240: 500–508
   PubMed Web of Science ®Google Scholar
• Fridovich I. Superoxide radical and superoxide dismutases. Annual Review of Biochemistry 1993; 64: 97–112
   Google Scholar
• Huie R. E., Padmaja S. The reaction of NO with superoxide. Free Radical Research Communications 1993; 18: 195–199
   PubMed Web of Science ®Google Scholar
• Radi R., Beckman J. S., Bush K. M., Freeman B. A. Peroxynitrite oxidation of sulfhydrils. The cytotoxic potential of superoxide and nitric oxide. Journal of Biological Chemistry 1991; 266: 4244–4250
   PubMed Web of Science ®Google Scholar
• Hausladen A., Fridovich I. Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not. Journal of Biological Chemistry 1994; 269: 29405–29408
   PubMed Web of Science ®Google Scholar
• Castro L., Rodriguez M., Radi R. Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide. Journal of Biological Chemistry 1994; 269: 29409–29415
   PubMed Web of Science ®Google Scholar
• Radi R., Beckman J. S., Bush K. M., Freeman B. A. Peroxynitrite-induced membrane lipid peroxidation: the cytotoxic potential of superoxide and nitric oxide. Archives of Biochemistry and Biophysics 1991; 288: 481–487
   PubMed Web of Science ®Google Scholar
• Wiseman H., Halliwell B. Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer. Biochemical Journal 1996; 313: 17–29
   PubMed Web of Science ®Google Scholar
• Zhu L., Gunn C., Beckman J. S. Bactericidal activity of peroxynitrite. Archives of Biochemistry and Biophysics 1992; 298: 452–457
   PubMed Web of Science ®Google Scholar
• Imlay J. A., Fridovich I. Assay of metabolic superoxide production in Escherichia coli. Journal of Biological Chemistry 1991; 266: 6957–6965
   PubMed Web of Science ®Google Scholar
• Dionisi O., Galeotti T., Terranova T., Azzi A. Superoxide radicals and hydrogen peroxide formation in mitochondria from normal and neoplastic tissues. Biochimica el Biophysica Acta 1975; 403: 292–300
   PubMed Web of Science ®Google Scholar
• Gaudu P., Touati D., Niviere V., Fonetcave M. The NAD(P)H:flavin oxidoreductase from Escherichia coli as a source of superoxide radicals. Journal of Biological Chemistry 1993; 269: 8182–8188
   Google Scholar
• Massey V., Strickland S., Mayhew S. G., Howell L. G., Engel P. C., Matthews R. G., Shuman M., Sullivan P. A. The production of superoxide anion radicals in the reaction of reduced flavins and flavoproteins with molecular oxygen. Biochemical and Biophysical Research Communications 1969; 36: 891–897
   PubMedGoogle Scholar
• Imlay J. A. A metabolic enzyme that rapidly produces superoxide, fumarate reductase of Escherichia coli. Journal of Biological Chemistry 1995; 270: 19767–19777
   PubMedGoogle Scholar
• McCord J. M., Russell W. J. Superoxide inactivates creatine phosphokinase during reperfusion of ischemic heart. Oxy-Radicals in Molecular Biology and Pathology, P. A. Cerutti, I. Fridovich, J. M. McCord. Allan R. Liss, New York 1988; 27–35
   Google Scholar
• Suzuki Y. J., Ford G. D. Mathematical model supporting the superoxide theory of oxygen toxicity. Free Radical Biology and Medicine 1994; 16: 63–72
   PubMed Web of Science ®Google Scholar
• McCord J. M., Fridovich I. Superoxide dismutase: The first twenty years. Free Radical Biology and Medicine 1988; 5: 363–369
   PubMed Web of Science ®Google Scholar
• Fridovich I. Biological effects of the superoxide radical. Archives of Biochemistry and Biophysics 1986; 247: 1–11
   PubMed Web of Science ®Google Scholar
• Carlioz A., Touati D. Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dis-mutase necessary for aerobic life?. EMBO Journal 1986; 5: 623–630
   PubMed Web of Science ®Google Scholar
• Imlay J. A., Fridovich I. Supression of oxidative envelope damage by pseudoreversion of a superoxide dismutase-deficient mutant of Escherichia coli. Journal of Bacteriology 1992; 174: 953–961
   PubMedGoogle Scholar
• Philips J. P., Campbell S. D., Michaud D., Charbonneau M., Hilliker A. J. Null mutation of copper/zinc superoxide dismutase in Drosophila confers hypersensitivity to paraquat and reduced longevity. Proceedings of the National Academy, U.S.A. 1989; 86: 2761–2765
   PubMedGoogle Scholar
• Li Y., Huang T.-T., Carlson E. J., Melov S., Ursell P. C., Olson J. L., Noble L. J., Yoshimura M. P., Berger C., Chan P. H., Wallace D. C., Epstein C. J. Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nature Genetics 1995; 11: 376–381
   PubMed Web of Science ®Google Scholar
• Eisenstark A., Miller C., Jones J., Leven S. Escherichia coli genes involved in cell survival during dormancy: role of oxidative stress. Biochemical and Biophysical Research Communications 1992; 188: 1054–1059
   PubMedGoogle Scholar
• Prieto-Alamo M.-J., Abril N., Pueyo C. Mutagenesis in Escherichia coli K-12 mutants defective in superoxide dismutase or catalase. Carcinogenesis 1993; 14: 237–244
   PubMed Web of Science ®Google Scholar
• Benov L., Fridovich I. A superoxide dismutase mimic protects sodA sodB Escherichia coli against aerobic heating and stationary-phase death. Archives of Biochemistry and Biophysics 1995; 322: 291–294
   PubMedGoogle Scholar
• Farr S. B., D'Ari R., Touati D. Oxygen-dependent mutagenesis in Echerichia coli lacking superoxide dismutase. Proceedings of the National Academy of Sciences, U.S.A. 1986; 83: 8268–8272
   PubMedGoogle Scholar
• Minakami H., Fridovich I. Relationship between growth of Escherichia coli and susceptibility to the lethal effect of paraquat. FASEB Journal 1990; 4: 3239–3244
   PubMed Web of Science ®Google Scholar
• Kitzler J., Fridovich I. The effects of paraquat on Escherichia coli: distinction between bacteriostasis and lethality. Journal of Free Radicals in Biology and Medicine 1986; 2: 245–248
   PubMedGoogle Scholar
• Brown O. R., Yein F. Dihydroxyacid dehydratase: the site of hyperbaric oxygen poisoning in branch-chain amino acid biosynthesis. Biochemical and Biophysical Research Communications 1978; 85: 1219–1224
   PubMed Web of Science ®Google Scholar
• Brown O. R., Seither R. L. Oxygen and redox-active drugs: shared toxicity sites. Fundamental and Applied Toxicology 1983; 3: 209–214
   PubMedGoogle Scholar
• Gardner P. R., Fridovich I. Quinolinate synthetase: the oxygen-sensitive site of de novo NAD(P)+ biosynthesis. Archives of Biochemistry and Biophysics 1991; 284: 106–111
   PubMedGoogle Scholar
• Kuo C. F., Mashino T., Fridovich I. α, β-Dihydroxy isovalerate dehydratase: a superoxide-sensitive enzyme. Journal of Biological Chemistry 1987; 262: 4724–4727
   PubMed Web of Science ®Google Scholar
• Flint D. H., Emptage M. H. Dihydroxy acid dehydratase: isolation characterization as iron-sulfur protein and sensitivity to inactivation by oxygen radicals. Biosynthesis of Branched Chain Amino Acids, Z. Barak, D. Chipman, J. V. Schloss. Balaban, Rehovoth and Philadelphia 1990; 285–314
   Google Scholar
• Flint D. H., Emptage M. H., Finnegan M. G., Fu W., Johnson M. K. The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase. Journal of Biological Chemistry 1993; 268: 14732–14742
   PubMed Web of Science ®Google Scholar
• Gardner P. R., Fridovich I. Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase. Journal of Biological Chemistry 1991; 266: 1478–1483
   PubMed Web of Science ®Google Scholar
• Gardner P. R., Fridovich I. Superoxide sensitivity of the Escherichia coli aconitase. Journal of Biological Chemistry 1991; 266: 19328–19333
   PubMed Web of Science ®Google Scholar
• Gardner P. R., Fridovich I. Inactivation-reactivation of aconitase in Escherichia coli. A sensitive measure of superoxide radical. Journal of Biological Chemistry 1992; 267: 8757–8763
   PubMed Web of Science ®Google Scholar
• Liochev S. I., Fridovich I. Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon. Proceedings of the National Academy of Sciences, U.S.A. 1992; 89: 5892–5896
   PubMed Web of Science ®Google Scholar
• Liochev S. I., Fridovich I. I. Modulation of the fumarases of Escherichia coli in response to oxidative stress. Archives of Biochemistry and Biophysics 1993; 301: 379–384
   PubMed Web of Science ®Google Scholar
• Flint D. H. Initial kinetic and mechanistic characterization of Escherichia coli fumarase A. Archives of Biochemistry and Biophysics 1994; 311: 509–516
   PubMedGoogle Scholar
• Flint D. H., Tuminello J. F., Emptage M. H. The inactivation of Fe-S cluster containing hydrolyases by superoxide. Journal of Biological Chemistry 1993; 268: 22369–22376
   PubMed Web of Science ®Google Scholar
• Flint D. H., Emptage M. H., Guest J. R. Fumarase A from Escherichia coli purification and characterization as an iron cluster containing enzyme. Biochemistry 1992; 31: 10331–10337
   PubMed Web of Science ®Google Scholar
• Brown O. R., Smyk-Randall E., Draczynska-Lusiak B., Fee J. A. Dihydroxy-acid dehydratase, a [4Fe-4S] cluster-containing enzyme in Escherichia coli: Effect of intracellular superoxide dismutase on its inactivation by oxidant stress. Archives of Biochemistry and Biophysics 1995; 319: 10–22
   PubMedGoogle Scholar
• Haber F., Weiss J. The catalytic decomposition of hydrogen peroxide by iron salts. Proceedings of the Royal Society of London [A] 1934; 147: 332–335
   Google Scholar
• Barb W. G., Baxendale J. H., George P., Hargrave K. R. Reactions of ferrous and ferric ions with hydrogen peroxide. Part I. The ferrous ion reaction. Transactions of the Faraday Society 1957; 47: 462–500
   Google Scholar
• Rush J. D., Bielski H. J. Pulse radiolytic studies of the reactions of HO2/O2- with Fe(II)/Fe(III) ions. The reactivity of HO2/O2- with ferric ions and its implication on the occurrence of the Haber-Weiss reaction. Journal of Physical Chemistry 1985; 89: 5062–5066
   Web of Science ®Google Scholar
• Brooks H. B., Sicilio F. Electron spin resonance kinetic studies of the oxidation of vanadium(IV) by hydrogen peroxide. Inorganic Chemistry 1971; 10: 2530–2534
   Web of Science ®Google Scholar
• Liochev S. I., Fridovich I. The roles of O2-, HO, and secondarily derived radicals in oxidation reactionxs catalyzed by vanadium salts. Archives of Biochemistry and Biophysics 1991; 291: 379–382
   PubMed Web of Science ®Google Scholar
• Beauchamp C. O., Fridovich I. A mechanism for the production of ethylene from methional: the generation of hydroxyl radical by xanthine oxidase. Journal of Biological Chemistry 1970; 245: 4641–4646
   PubMed Web of Science ®Google Scholar
• Halliwell B. Superoxide-dependent formation of hydroxyl radicals in the presence of iron chelates: is it a mechanism for hydroxyl radical production in biochemical systems?. FEBS Letters 1978; 92: 321–326
   PubMed Web of Science ®Google Scholar
• McCord J. M., Day E. D., Jr. Superoxide-dependent production of hydroxyl radical catalyzed by iron-EDTA complex. FEBS Letters 1978; 86: 139–142
   PubMed Web of Science ®Google Scholar
• Czapski G., Goldstein S., Meyerstein D. What is unique about superoxide toxicity as compared to other biological reductants: a hypothesis. Free Radicals Research Communications 1988; 4: 231–236
   PubMedGoogle Scholar
• Winterboum C. C. Superoxide as an intracellular sink. Free Radical Biology and Medicine 1993; 14: 85–90
   PubMed Web of Science ®Google Scholar
• Winterboum C. C. Superoxide-dependent production of hydroxyl radicals in the presence of iron salts. Biochemical Journal 1982; 205: 463
   Google Scholar
• Halliwell B. Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts is a feasible source of hydroxyl radicals in vivo. Biochemical Journal 1982; 205: 461–462
   PubMed Web of Science ®Google Scholar
• Repine J. E., Fox R. B., Berger E. M. Hydrogen peroxide kills Staphylococcus aureus by reacting with staphylococcal iron to form hydroxyl radical. Journal of Biological Chemistry 1981; 256: 7094–7096
   PubMed Web of Science ®Google Scholar
• Touati D., Jacques M., Tardat B., Bouchard L., Despied S. Lethal oxidative damage and mutagenesis are generated by iron in fur, mutants of Escherichia coli: protective role of superoxide dismutase. Journal of Bacteriology 1995; 177: 2305–2314
   PubMed Web of Science ®Google Scholar
• Keyer K., Strohmeier-Gort A., Imlay J. A. Superoxide and the production of oxidative DNA damage. Journal of Bacteriology 1995; 177: 6782–6790
   PubMed Web of Science ®Google Scholar
• Böhnke R., Matzanke B. F. The mobile ferrous iron pool in Escherichia coli is bound to a phospho-rylated sugar derivative. BioMetals 1995; 8: 223–230
   PubMedGoogle Scholar
• Monteiro H. P., Winterboum C. C. The superoxide-dependent transfer of iron from ferritin to transferrin and lactoferrin. Biochemical Journal 1988; 256: 923–928
   PubMed Web of Science ®Google Scholar
• Biemond P., Swaak A. J. G., Beindorff M., Koster J. F. Superoxide-dependent and -independent mechanisms of iron mobilization from ferritin by xanthine oxidase. Implications for oxygen-free-radical induced tissue destruction during ischemia and inflammation. Biochemical Journal 1986; 239: 169–173
   PubMed Web of Science ®Google Scholar
• Thomas C. E., Morehouse L. A., Aust S. D. Ferritin and superoxide-dependent lipid peroxidation. Journal of Biological Chemistry 1985; 260: 3275–3280
   PubMed Web of Science ®Google Scholar
• Reif D. W. Ferritin as a source of iron for oxidative damage. Free Radical Biology and Medicine 1992; 12: 417–427
   PubMed Web of Science ®Google Scholar
• Gardner P., Fridovich I. Effect of glutathione on aconitase in Escherichia coli. Archives of Biochemistry and Biophysics 1993; 301: 98–102
   PubMedGoogle Scholar
• Flint D. H., Smyk-Randall E., Tuminello J. F., Draczynska-Lusiak B., Brown O. R. The inacti-vation of dihyrdoxy-acid dehydratase in Escherichia coli treated with hyperbaric oxygen occurs because of the destruction of its Fe-S cluster, but the enzyme remains in the cell in a form that can be reactivated. Journal of Biological Chemistry 1993; 268: 25547–25552
   PubMed Web of Science ®Google Scholar
• Kennedy M. C., Emptage M. H., Dreyer J. L., Beinert H. The role of iron in the activation-inactivation of aconitase. Journal of Biological Chemistry 1983; 258: 11098–11105
   PubMed Web of Science ®Google Scholar
• Klausner R. D., Rouault T. A double life: cytosolic aconitase as a regulatory RNA-binding protein. Molecular Biology of the Cell 1993; 4: 1–5
   PubMed Web of Science ®Google Scholar
• Beinert H., Kennedy M. C. Aconitase, a two-faced protein: enzyme and iron regulatory factor. FASEB Journal 1993; 7: 1442–1449
   PubMed Web of Science ®Google Scholar
• Samaniego F., Chin J., Iwai K., Rouault T. A., Klausner R. D. Molecular characterization of a second iron-responsive element binding protein, iron regulatoray protein. 2. Structure, function, and post-translational regulation. Journal of Biological Chemistry 1994; 269: 30904–30910
   PubMed Web of Science ®Google Scholar
• Siwecki G., Brown O. R. Overproduction of superoxide dismutase does not protect Escherichia coli from stringency-induced growth inhibition by 1 mM paraquat. Biochemistry International 1990; 20: 191–200
   PubMedGoogle Scholar
• Liochev S. I., Fridovich I. Effects of overproduction of superoxide dismutases in Escherichia coli on inhibition of growth and on induction of glucoses-phosphate dehydrogenase by paraquat. Archives of Biochemistry and Biophysics 1992; 294: 138–143
   PubMed Web of Science ®Google Scholar
• Polissi A., Harayama S. In vivo reactivation of catechol 2,3-dioxygenase mediated by a chloroplast-type ferredoxin: a bacterial strategy to expand the substrate specificity of aromatic degradative pathways. EMBO Journal 1993; 12: 3339–3347
   PubMedGoogle Scholar
• Bianchi V., Eliasson R., Fontecave M., Mulliez E., Hoover D. M., Matthews R. G., Reichard P. Flavodoxin is required for the activation of the anaerobic ribonucleotie reductase. Biochemical and Biophysical Research Communications 1993; 197: 792–797
   PubMedGoogle Scholar
• Mulliez E., Fontecave M., Gaillard J., Reichard P. An iron-sulfur center and a free radical in the active anaerobic ribonucleotide reductase of Escherichia coli. Journal of Biological Chemistry 1993; 268: 2296–2299
   PubMedGoogle Scholar
• Ifuku O., Koga N., Haze S., Kishimoto J., Wachi Y. Flavodoxin is required for conversion of dethiobiotin to biotin in Escherichia coli. European Journal of Biochemistry 1994; 224: 173–178
   PubMedGoogle Scholar
• Sanyal I., Cohen G., Flint D. H. Biotin synthase: purification, characterization as a [2Fe-2S] cluster protein, and in vitro activity of the Escherichia coli bioB gene product. Biochemistry 1994; 33: 3625–3631
   PubMedGoogle Scholar
• Liochev S. I., Fridovich I. Paraquat diaphorases in Escherichia coli. Free Radical Biology and Medicine 1994; 16: 555–559
   PubMed Web of Science ®Google Scholar
• Liochev S. I., Hausladen A., Beyer W. F., Fridovich I. NADPH: ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon. Proceedings of the National Academy of Sciences, U.S.A. 1994; 91: 1328–1331
   PubMed Web of Science ®Google Scholar
• Siegel L. M., Davis P. S., Kamin H. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. III. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow. Journal of Biological Chemistry 1974; 249: 1572–1586
   PubMedGoogle Scholar
• Gaudu P., Fontecave M. The NADPH:sulfite reductase of Escherichia coli is a paraquat reductase. European Journal of Biochemistry 1994; 226: 459–463
   PubMedGoogle Scholar
• Blaschkowski H. P., Neuer G., Ludwig-Festl M., Knappe J. Routes of flavodoxin and ferredoxin reduction in Escherichia coli. European Journal of Biochemistry 1982; 123: 563–569
   PubMedGoogle Scholar
• Barman B. G., Tollin G. Flavin-protein interactions in flavoenzymes. Thermodynamics and kinetics of reduction of Azotobacter flavodoxin. Biochemistry 1972; 11: 4755–4759
   PubMedGoogle Scholar
• Mayhew S. G., Ludwig M. L. Flavodoxins and electron-transferring flavoproteins. The Enzymes. Vol. XII, P. D. Boyer. Academic Press, New York 1975; 57–118
   Google Scholar
• Bianchi V., Haggard-Ljungquist E., Pontis E., Reichard P. Interruption of the ferredoxin (flavodoxin) NADP+ oxidoreductase gene of Escherichia coli does not affect anaerobic growth but increases sensitivity to paraquat. Journal of Bacteriology 1995; 177: 4528–4531
   PubMedGoogle Scholar
• Krapp A. R., Carrillo N. Functional complementation of the mvrA mutation of Escherichia coli by plant ferredoxin-NADP+ oxidoreductase. Archives of Biochemistry and Biophysics 1995; 317: 215–221
   PubMedGoogle Scholar
• Fontecave M., Coves J., Pierre J. L. Ferric reductases or flavin reductases?. BioMetals 1994; 7: 3–8
   PubMed Web of Science ®Google Scholar
• Fu W., Jack R. F., Morgan T. V., Dean D. R., Johnson M. K. nifU gene product from Azotobacter vinelandii is a homodimer that contains two identical [2Fe-2S] clusters. Biochemistry 1994; 33: 13455–13463
   PubMed Web of Science ®Google Scholar
• Felix K., Lengfelder E., Hartman H. J., Weser U. A pulse radiolytic study on the reaction of hydroxyl and superoxide radicals with yeast Cu(I)-thionein. Biochimica el Biophysica Acta 1993; 1203: 104–108
   PubMedGoogle Scholar
• Halliwell B., Gurteridge J. M. Role of free radicals and catalytic metal ions in human disease: an overview. Methods in Enzymology 1990; 186: 1–85
   PubMed Web of Science ®Google Scholar
• Martins E. A. L., Robalinho R. L., Meneghini R. Oxidative stress induces activation of a cytosolic protein responsible for control of iron uptake. Archives of Biochemistry and Biophysics 1995; 316: 128–134
   PubMed Web of Science ®Google Scholar
• Gardner P. R., Rained I., Epstein L. B., White C. W. Superoxide radical and iron modulate aconitase activity in mammalian cells. Journal of Biological Chemistry 1995; 270: 13399–13405
   PubMed Web of Science ®Google Scholar
• Storz G., Toledano M. B. Regulation of bacterial gene expression in response to oxidative stress. Methods in Enzymology 1994; 236: 196–207
   PubMedGoogle Scholar
• Demple B. Regulation of bacterial oxidative stress genes. Annual Review of Genetics 1991; 25: 315–337
   PubMed Web of Science ®Google Scholar
• Wu J., Weiss B. Two-stage induction of the soxRS (superoxide response) regulon of Escherichia coli. Journal of Bacteriology 1992; 174: 3915–3920
   PubMed Web of Science ®Google Scholar
• Greenberg J. T., Monach P., Chou J. H., Josephy P. D., Demple B. Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proceedings of the National Academy of Sciences, U.S.A. 1990; 87: 6181–6185
   PubMed Web of Science ®Google Scholar
• Tsaneva I. R., Weiss B. soxR, a locus governing a superoxide response regulon in Escherichia coli K12. Journal of Bacteriology 1990; 172: 41197–41205
   Google Scholar
• Gruer M. J., Guest J. R. Two genetically-distinct and differentially-regulated aconitases (AcnA and AcnB) in Escherichia coli. Microbiology 1994; 140: 2531–2541
   PubMedGoogle Scholar
• Gidrol X., Farr S. Interaction of a redox-sen-sitive DNA-binding factor with the 5- flanking region of the micF gene in Escherichia coli. Molecular Microbiology 1993; 10: 877–884
   PubMedGoogle Scholar
• Gonzalez-Flecha B., Demple B. Intracellular generation of superoxide as a by-product of Vibrio harveyi luciferase expressed in Escherichia coli. Journal of Bacteriology 1994; 176: 2293–2299
   PubMedGoogle Scholar
• Gardner P. R., Fridovich I. NADPH inhibits transcription of the Escherichia coli manganese superoxide dismutase gene (sodA) in vitro. Journal of Biological Chemistry 1993; 268: 12958–12963
   PubMedGoogle Scholar
• Nunoshiba T., DeRojas-Walker T., Wishnok J. S., Tannenbaum S. R., Demple B. Activation by nitric oxide of an oxidative stress response that defends Escherichia coli against activated macrophages. Proceedings of the National Academy of Sciences, U.S.A. 1993; 90: 9993–9997
   PubMed Web of Science ®Google Scholar
• Privalle C. T., Kong S. E., Fridovich I. Induction of manganese-containing superoxide dismutase in anaerobic Escherichia coli by diamide and 1,10-phenanthroline: sites of transcriptional regulation. Proceedings of the National Academy of Sciences, U.S.A. 1993; 90: 2310–2314
   PubMedGoogle Scholar
• Wu J., Dunham W. R., Weiss B. Overproduction and physical characterization of SoxR, a [2Fe-2S] protein that governs an oxidative response regulon in Escherichia coli. Journal of Biological Chemistry 1995; 270: 10323–10327
   PubMedGoogle Scholar
• Hidalgo E., Bollinger J. M., Jr, Bradley T. M., Walsh C. T., Demple B. Binuclear [2Fe-2S] clusters in the Escherichia coli soxR protein and role of the metal centers in transcription. Journal of Biological Chemistry 1995; 270: 20908–20914
   PubMed Web of Science ®Google Scholar
• Hidalgo E., Demple B. An iron-sulfur center essential for transcriptional activation by the redox sensing SoxR protein. EMBO Journal 1994; 13: 138–146
   PubMed Web of Science ®Google Scholar
• Beinert H., Kiley P. Redox control of gene expression involving iron-sulfur proteins. Change of oxidation-state or assembly/disassembly of Fe-S clusters?. FEBS Letters 1996; 382: 218–219
   PubMedGoogle Scholar
• Allen J. F. Reply to commentary by Helmut Beinert and Patricia Kiley. FEBS Letters 1996; 382: 220–221
   Google Scholar
• Carmine T. C., Evans P., Bruchelt G., Evans R., Handgretinger R., Niethammer D., Halliwell B. Presence of iron catalytic for free radical reactions in patients undergoing chemotherapy: implication for therapeutic management. Cancer Letters 1995; 94: 219–226
   PubMed Web of Science ®Google Scholar
• Rowley D. A., Halliwell B. Superoxide-dependent formation of hydroxyl radicals in the presence of thiol compounds. FEBS Letters 1982; 138: 33–36
   PubMed Web of Science ®Google Scholar
• Rowley D. A., Halliwell B. Superoxide-dependent formation of hydroxyl radicals from NADH and NADPH in the presence of iron salts. FEBS Letters 1982; 142: 39–41
   PubMed Web of Science ®Google Scholar
• Koppenol W. H. The chemistry and biochemistry of oxidants derived from nitric oxide. Nitric Oxide and Radicals in the Pulmonary Vasculature, E. K. Weir, S. L. Archer, J. T. Reeves. Futura Publishing Co., New York 1996; 355–362
   Google Scholar
• Ischiropoulos H., Zhu L., Beckman J. S. Peroxynitrite formation from macrophage-derived nitric oxide. Archives of Biochemistry and Biophysics 1992; 298: 446–451
   PubMed Web of Science ®Google Scholar
• Katusic Z. S. Superoxide anion and endothelial regulation of arterial tone. Free Radical Biology and Medicine 1996; 20: 443–448
   PubMed Web of Science ®Google Scholar