Superoxide dismutases—A review of the metal-associated mechanistic variations
Abstract
Superoxide dismutases are enzymes that function to catalytically convert superoxide radical to oxygen and hydrogen peroxide. These enzymes carry out catalysis at near diffusion controlled rate constants via a general mechanism that involves the sequential reduction and oxidation of the metal center, with the concomitant oxidation and reduction of superoxide radicals. That the catalytically active metal can be copper, iron, manganese or, recently, nickel is one of the fascinating features of this class of enzymes. In this review, we describe these enzymes in terms of the details of their catalytic properties, with an emphasis on the mechanistic differences between the enzymes. The focus here will be concentrated mainly on two of these enzymes, copper, zinc superoxide dismutase and manganese superoxide dismutase, and some relatively subtle variations in the mechanisms by which they function.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Fe-SOD is a prokaryotic enzyme, discovered in some bacterial cells and in the cytosol of plants.
“It is a prokaryotic enzyme, discovered in some bacterial cells and in the cytosol of plants [86].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [86]
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
Buxton, G. V., Greenstock, C. L., Helman, W. P., & Ross, A. B. (1988) · Journal of Physical and Chemical Reference Data · doi:10.1063/1.555805 · Cited by 12,332 · see citing works
Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062 · see citing works
Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation
Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143 · see citing works
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455 · see citing works
The Copper Chaperone for Superoxide Dismutase
Culotta, V., Klomp, L. W. J., Strain, J. J., Casareno, R. L. B., Krems, B., & Gitlin, J. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23469 · Cited by 851 · see citing works
COPPER-ZINC SUPEROXIDE DISMUTASE AND AMYOTROPHIC LATERAL SCLEROSIS
Valentine, J. S., Doucette, P. A., & Potter, S. Z. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161647 · Cited by 790 · see citing works
Hodgson, E. K., & Fridovich, I. (1975) · Biochemistry · doi:10.1021/bi00695a010 · Cited by 785 · see citing works
Ripps, M. E., Huntley, G. W., Hof, P. R., Morrison, J., & Gordon, J. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.3.689 · Cited by 725 · see citing works
Altered Reactivity of Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis
Wiedau‐Pazos, M., Goto, J. J., Rabizadeh, S., Gralla, E. B., Roe, J. A., Lee, M. K., Valentine, J. S., & Bredesen, D. E. (1996) · Science · doi:10.1126/science.271.5248.515 · Cited by 720 · see citing works
Williamson, T. L., & Cleveland, D. W. (1999) · Nature Neuroscience · doi:10.1038/4553 · Cited by 638 · see citing works
The inactivation of Fe-S cluster containing hydro-lyases by superoxide
Flint, D. H., Tuminello, J. F., & Emptage, M. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41538-4 · Cited by 637 · see citing works
Accumulation of Mn(II) in Deinococcus radiodurans Facilitates Gamma-Radiation Resistance
Daly, M. J., Gaidamakova, E. K., Matrosova, V. Y., Vasilenko, A., Zhai, M., Venkateswaran, A., Hess, M., Omelchenko, M. V., Kostandarithes, H. M., Makarova, K. S., et al. (2004) · Science · doi:10.1126/science.1103185 · Cited by 622 · see citing works
Superoxide Dismutase from Escherichia coli B
Keele, B. B., McCord, J. M., & Fridovich, I. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62675-4 · Cited by 559 · see citing works
Electrostatic recognition between superoxide and copper, zinc superoxide dismutase
Getzoff, E. D., Tainer, J. A., Weiner, P. K., Kollman, P. A., Richardson, J. S., & Richardson, D. C. (1983) · Nature · doi:10.1038/306287a0 · Cited by 554 · see citing works
Oxidative stress in ALS: A mechanism of neurodegeneration and a therapeutic target
Barber, S. C., Mead, R. J., & Shaw, P. J. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.03.008 · Cited by 475 · see citing works
Borgstahl, G. E. O., Parge, H. E., Hickey, M. J., Beyer, W. F., Hallewell, R. A., & Tainer, J. A. (1992) · Cell · doi:10.1016/0092-8674(92)90270-m · Cited by 472 · see citing works
Yim, M. B., Kang, J. H., Yim, H., Kwak, H. S., Chock, P. B., & Stadtman, E. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.5709 · Cited by 459 · see citing works
The scavenging of superoxide radical by manganous complexes: In vitro
Archibald, F. S., & Fridovich, I. (1982) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(82)90049-2 · Cited by 425 · see citing works
Nickel Superoxide Dismutase Structure and Mechanism
Barondeau, D. P., Kassmann, C. J., Bruns, C. K., Tainer, J. A., & Getzoff, E. D. (2004) · Biochemistry · doi:10.1021/bi0496081 · Cited by 415 · see citing works
Faster superoxide dismutase mutants designed by enhancing electrostatic guidance
Getzoff, E. D., Cabelli, D. E., Fisher, C. L., Parge, H. E., Viezzoli, M. S., Banci, L., & Hallewell, R. A. (1992) · Nature · doi:10.1038/358347a0 · Cited by 399 · see citing works
Self-citationReduction and inactivation of superoxide dismutase by hydrogen peroxide
Bray, R. C., Cockle, S. A., Fielden, E. M., Roberts, P. B., Rotilio, G., & Calabrese, L. (1974) · Biochemical Journal · doi:10.1042/bj1390043 · Cited by 394 · see citing works
Hayward, L. J., Rodriguez, J. A., Kim, J. W., Tiwari, A., Goto, J. J., Cabelli, D. E., Valentine, J. S., & Brown, R. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112087200 · Cited by 377 · see citing works
Self-citationManganese and Defenses against Oxygen Toxicity in Lactobacillus plantarum
Archibald, F. S., & Fridovich, I. (1981) · Journal of Bacteriology · doi:10.1128/jb.145.1.442-451.1981 · Cited by 373 · see citing works
Crystal structure of nickel-containing superoxide dismutase reveals another type of active site
Wuerges, J., Lee, J., Yim, Y.-I., Yim, H., Kang, S.-O., & Djinović‐Carugo, K. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308514101 · Cited by 354 · see citing works
A pulse radiolysis study of superoxide dismutase
Rotilio, G., Bray, R. C., & Fielden, E. M. (1972) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(72)90359-2 · Cited by 324 · see citing works
Lah, M. S., Dixon, M. M., Pattridge, K. A., Stallings, W. C., Fee, J. A., & Ludwig, M. L. (1995) · Biochemistry · doi:10.1021/bi00005a021 · Cited by 299 · see citing works
Klug-Roth, D., Fridovich, I., & Rabani, J. (1973) · Journal of the American Chemical Society · doi:10.1021/ja00790a007 · Cited by 251 · see citing works
Free radicals generated by radiolysis of aqueous solutions
Schwarz, H. A. (1981) · Journal of Chemical Education · doi:10.1021/ed058p101 · Cited by 237 · see citing works
Electrostatic interactions in the reaction mechanism of bovine erythrocyte superoxide dismutase
Cudd, A., & Fridovich, I. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33779-7 · Cited by 211 · see citing works
ALS Mutants of Human Superoxide Dismutase Form Fibrous Aggregates Via Framework Destabilization
DiDonato, M., Craig, L., Huff, M. E., THAYER, M. M., Cardoso, R. M. F., Kassmann, C. J., Lo, T. P., Bruns, C. K., Powers, E. T., Kelly, J. W., et al. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00889-1 · Cited by 205 · see citing works
The carbonate radical and related oxidants derived from bicarbonate buffer
Medinas, D. B., Cerchiaro, G., Trindade, D. F., & Augusto, O. (2007) · IUBMB Life · doi:10.1080/15216540701230511 · Cited by 198 · see citing works
Buettner, G. R., Ng, C. F., Wang, M., Rodgers, V. G. J., & Schafer, F. Q. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.07.015 · Cited by 198 · see citing works
Multiple Protein Domains Contribute to the Action of the Copper Chaperone for Superoxide Dismutase
Schmidt, P. J., Rae, T., Pufahl, R. A., Hamma, T., Strain, J., O’Halloran, T. V., & Culotta, V. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.23719 · Cited by 189 · see citing works
Copper–zinc superoxide dismutase: Why not pH-dependent?
Ellerby, L. M., Cabelli, D. E., Graden, J. A., & Valentine, J. S. (1996) · Journal of the American Chemical Society · doi:10.1021/ja953845x · Cited by 184 · see citing works
Self-citationManganous Phosphate Acts as a Superoxide Dismutase
Barnese, K., Gralla, E. B., Cabelli, D. E., & Valentine, J. S. (2008) · Journal of the American Chemical Society · doi:10.1021/ja710162n · Cited by 183 · see citing works
Self-citationBull, C., & Fee, J. A. (1985) · Journal of the American Chemical Society · doi:10.1021/ja00297a040 · Cited by 174 · see citing works
Goto, J. J., Zhu, H., Sanchez, R. J., Nersissian, A. M., Gralla, E. B., Valentine, J. S., & Cabelli, D. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.1007 · Cited by 166 · see citing works
Self-citationChoudhury, S. B., Lee, J., Davidson, G., Yim, Y.-I., Bose, K. S., Sharma, M. L., Kang, S.-O., Cabelli, D. E., & Maroney, M. J. (1999) · Biochemistry · doi:10.1021/bi982537j · Cited by 164 · see citing works
Self-citationBull, C., Niederhoffer, E. C., Yoshida, T., & Fee, J. A. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00011a003 · Cited by 157 · see citing works
Luk, E., Carroll, M., Baker, M., & Culotta, V. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1632471100 · Cited by 146 · see citing works
Luk, E., & Culotta, V. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108923200 · Cited by 137 · see citing works
Crystal structure of Escherichia coli manganese superoxide dismutase at 2.1-Å resolution
Edwards, R. A., Baker, H. M., Whittaker, M. M., Whittaker, J. W., Jameson, G. B., & Baker, E. N. (1998) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050217 · Cited by 136 · see citing works
Manganese Activation of Superoxide Dismutase 2 in the Mitochondria of Saccharomyces cerevisiae
Luk, E., Yang, M., Jensen, L. T., Bourbonnais, Y., & Culotta, V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504257200 · Cited by 125 · see citing works
Fisher, C. L., Cabelli, D. E., Tainer, J. A., Hallewell, R. A., & Getzoff, E. D. (1994) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340190105 · Cited by 125 · see citing works
Self-citationPick, M. R., Rabani, J., Yost, F., & Fridovich, I. (1974) · Journal of the American Chemical Society · doi:10.1021/ja00830a026 · Cited by 124 · see citing works
McAdam, M. E., Fox, R. A., Lavelle, F., & Fielden, E. M. (1977) · Biochemical Journal · doi:10.1042/bj1650071 · Cited by 123 · see citing works
The overlapping roles of manganese and Cu/Zn SOD in oxidative stress protection
Reddi, A. R., Jensen, L. T., Naranuntarat, A., Rosenfeld, L., Leung, E., Shah, R. R., & Culotta, V. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.09.032 · Cited by 122 · see citing works
Structure and Properties of Copper-Zinc Superoxide Dismutases
Bertini, I., Manganl, S., & Viezzoli, M. S. (1998) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60026-4 · Cited by 119 · see citing works
Flint, D. H., Smyk-Randall, E. M., Tuminello, J. F., Draczynska‐Lusiak, B., & Brown, O. R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74426-3 · Cited by 117 · see citing works
Kurahashi, T., Miyazaki, A., Suwan, S., & Isobe, M. (2001) · Journal of the American Chemical Society · doi:10.1021/ja015953r · Cited by 113 · see citing works
Guan, Y., Hickey, M. J., Borgstahl, G. E. O., Hallewell, R. A., Lepock, J. R., O'Connor, D. E., Hsieh, Y., Nick, H. S., Silverman, D. N., & Tainer, J. A. (1998) · Biochemistry · doi:10.1021/bi972394l · Cited by 112 · see citing works
The Right to Choose: Multiple Pathways for Activating Copper,Zinc Superoxide Dismutase
Leitch, J. M., Yick, P. J., & Culotta, V. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r109.040410 · Cited by 107 · see citing works
Lavelle, F., McAdam, M. E., Fielden, E. M., Roberts, P. B., Puget, K., & Michelson, M. (1977) · Biochemical Journal · doi:10.1042/bj1610003 · Cited by 94 · see citing works
Vance, C. K., & Miller, A.-F. (1998) · Biochemistry · doi:10.1021/bi972580r · Cited by 89 · see citing works
Policastro, L., Molinari, B. L., Larcher, F., Blanco, P., Podhajcer, O. L., Costa, C. S., Rojas, P. A., & Durán, H. (2004) · Molecular Carcinogenesis · doi:10.1002/mc.20001 · Cited by 89 · see citing works
Crystal structure of nitrated human manganese superoxide dismutase: Mechanism of inactivation
Quint, P. S., Reutzel, R., Mikulski, R. L., McKENNA, R. V., & Silverman, D. N. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.045 · Cited by 88 · see citing works
Fee, J. A., & Bull, C. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69261-0 · Cited by 87 · see citing works
Probing the Active Site of Human Manganese Superoxide Dismutase: The Role of Glutamine 143,
Hsieh, Y., Guan, Y., Tu, C., Bratt, P. J., Angerhofer, A., Lepock, J. R., Hickey, M. J., Tainer, J. A., Nick, H. S., & Silverman, D. N. (1998) · Biochemistry · doi:10.1021/bi972395d · Cited by 86 · see citing works
Mechanisms of the Copper-dependent Turnover of the Copper Chaperone for Superoxide Dismutase
Caruano-Yzermans, A. L., Bartnikas, T. B., & Gitlin, J. D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601580200 · Cited by 84 · see citing works
McAdam, M. E., Levelle, F., Fox, R. A., & Fielden, E. M. (1977) · Biochemical Journal · doi:10.1042/bj1650081 · Cited by 83 · see citing works
Shearer, J., & Long, L. M. (2006) · Inorganic Chemistry · doi:10.1021/ic0514344 · Cited by 83 · see citing works
Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 Å
Hough, M. A., & Hasnain, S. S. (2003) · Structure · doi:10.1016/s0969-2126(03)00155-2 · Cited by 80 · see citing works
An Alternative Mechanism of Bicarbonate-mediated Peroxidation by Copper-Zinc Superoxide Dismutase
Elam, J. S., Malek, K., Rodriguez, J. A., Doucette, P. A., Taylor, A. B., Hayward, L. J., Cabelli, D. E., Valentine, J. S., & Hart, P. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300484200 · Cited by 78 · see citing works
Self-citationProton-coupled electron transfer in Fe-superoxide dismutase and Mn-superoxide dismutase
Miller, A., Padmakumar, K., Sorkin, D. L., Karapetyan, A. V., & Vance, C. K. (2003) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(02)00621-9 · Cited by 76 · see citing works
Kinetic Analysis of Product Inhibition in Human Manganese Superoxide Dismutase
Hearn, A. S., Stroupe, M. E., Cabelli, D. E., Lepock, J. R., Tainer, J. A., Nick, H. S., & Silverman, D. N. (2001) · Biochemistry · doi:10.1021/bi011047f · Cited by 69 · see citing works
Self-citation[7] Methods for the study of superoxide chemistry in nonaqueous solutions
Valentine, J. S., Miksztal, A. R., & Sawyer, D. T. (1984) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(84)05010-2 · Cited by 68 · see citing works
Outer Sphere Mutations Perturb Metal Reactivity in Manganese Superoxide Dismutase,
Edwards, R. A., Whittaker, M. M., Whittaker, J. W., Baker, E. N., & Jameson, G. B. (2000) · Biochemistry · doi:10.1021/bi0018943 · Cited by 67 · see citing works
Superoxide dismutase and oxygen toxicity.
Koppenol, W. H. (1981) · PubMed · Cited by 66 · see citing works
Goto, J. J., Gralla, E. B., Valentine, J. S., & Cabelli, D. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.46.30104 · Cited by 64 · see citing works
Self-citationHearn, A. S., Stroupe, M. E., Cabelli, D. E., Ramilo, C. A., Luba, J. P., Tainer, J. A., Nick, H. S., & Silverman, D. N. (2003) · Biochemistry · doi:10.1021/bi0266481 · Cited by 62 · see citing works
Self-citationRedox Properties of Human Manganese Superoxide Dismutase and Active-Site Mutants
Lévêque, V., Vance, C. K., Nick, H. S., & Silverman, D. N. (2001) · Biochemistry · doi:10.1021/bi010792p · Cited by 61 · see citing works
The interaction between Cu(I) superoxide dismutase and hydrogen peroxide
Cabelli, D. E., Allen, D., Bielski, B. H. J., & Holcman, J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81754-9 · Cited by 60 · see citing works
Self-citationJackson, T. A., Karapetyan, A. V., Miller, A., & Brunold, T. C. (2005) · Biochemistry · doi:10.1021/bi048639t · Cited by 59 · see citing works
Lévêque, V., Stroupe, M. E., Lepock, J. R., Cabelli, D. E., Tainer, J. A., Nick, H. S., & Silverman, D. N. (2000) · Biochemistry · doi:10.1021/bi9929958 · Cited by 59 · see citing works
Self-citationContribution of Human Manganese Superoxide Dismutase Tyrosine 34 to Structure and Catalysis
Perry, J. J. P., Hearn, A. S., Cabelli, D. E., Nick, H. S., Tainer, J. A., & Silverman, D. N. (2009) · Biochemistry · doi:10.1021/bi8023288 · Cited by 59 · see citing works
Self-citationThe Iron Superoxide Dismutase from the Filamentous Cyanobacterium Nostoc PCC 7120
Regelsberger, G., Laaha, U., Dietmann, D., Rüker, F., Canini, A., Caiola, M. G., Furtmüller, P. G., Jakopitsch, C., Peschek, G. A., & Obinger, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406254200 · Cited by 51 · see citing works
de Belleroche, J., Orrell, R. W., & Virgo, L. (1996) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199607000-00001 · Cited by 48 · see citing works
Affinity inactivation of bovine Cu, Zn superoxide dismutase by hydroperoxide anion, HO2−
Fuchs, H. J. R., & Borders, C. L. (1983) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(83)80256-3 · Cited by 47 · see citing works
Fast kinetic studies of dioxygen-derived species and their metal complexes
Bielski, B. H. J. (1985) · Philosophical transactions of the Royal Society of London. Series B, Biological sciences · doi:10.1098/rstb.1985.0158 · Cited by 45 · see citing works
Abreu, I. A., Hearn, A. S., An, H., Nick, H. S., Silverman, D. N., & Cabelli, D. E. (2008) · Biochemistry · doi:10.1021/bi7016206 · Cited by 44 · see citing works
Self-citationGrove, L. E., & Brunold, T. C. (2008) · Comments on Inorganic Chemistry · doi:10.1080/02603590802429529 · Cited by 41 · see citing works
Abreu, I. A., Rodríguez, J. A., & Cabelli, D. E. (2005) · The Journal of Physical Chemistry B · doi:10.1021/jp052368u · Cited by 40 · see citing works
Self-citationRole of Hydrogen Bonding in the Active Site of Human Manganese Superoxide Dismutase,
Greenleaf, W. B., Perry, J. J. P., Hearn, A. S., Cabelli, D. E., Lepock, J. R., Stroupe, M. E., Tainer, J. A., Nick, H. S., & Silverman, D. N. (2004) · Biochemistry · doi:10.1021/bi049888k · Cited by 39 · see citing works
Self-citationPotent Anti-tumor Effects of an Active Site Mutant of Human Manganese-Superoxide Dismutase
Davis, C. A., Hearn, A. S., Fletcher, B. S., Bickford, J. S., Garcia, J. E., Lévêque, V., Melendez, J. A., Silverman, D. N., Zucali, J. R., Agarwal, A., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310623200 · Cited by 39 · see citing works
Redox-Genome Interactions in Health and Disease
(2003) · CRC Press eBooks · doi:10.1201/9780203912874 · Cited by 34 · see citing works
Su, Z. Z., Chai, M., Lu, P., An, R. F., Chen, J., & Wang, X. (2007) · Planta · doi:10.1007/s00425-007-0547-6 · Cited by 33 · see citing works
Amino Acid Substitution at the Dimeric Interface of Human Manganese Superoxide Dismutase
Hearn, A. S., Fan, L., Lepock, J. R., Luba, J. P., Greenleaf, W. B., Cabelli, D. E., Tainer, J. A., Nick, H. S., & Silverman, D. N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311310200 · Cited by 31 · see citing works
Self-citationDennis, R. J., Micossi, E., McCarthy, J., Moe, E., Gordon, E. J., Kozielski-Stuhrmann, S., Leonard, G. A., & McSweeney, S. (2006) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309106008402 · Cited by 30 · see citing works
Kinetic Analysis of the Metal Binding Mechanism of Escherichia coli Manganese Superoxide Dismutase
Whittaker, M. M., Mizuno, K., Bächinger, H. P., & Whittaker, J. W. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.071308 · Cited by 29 · see citing works
Bonini, M. G., Gabel, S. A., Ranguelova, K., Stadler, K., DeRose, E. F., London, R. E., & Mason, R. P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m804644200 · Cited by 26 · see citing works
Zheng, J., Domsic, J. F., Cabelli, D. E., McKENNA, R. V., & Silverman, D. N. (2007) · Biochemistry · doi:10.1021/bi7014103 · Cited by 23 · see citing works
Self-citationBicarbonate-enhanced peroxidase activity of Cu, Zn SOD: is the distal oxidant bound or diffusible?
Liochev, S. I., & Fridovich, I. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.11.015 · Cited by 22 · see citing works
Inactivation of Pseudomonas iron-superoxide dismutase by hydrogen peroxide
Yamakura, F., & Suzuki, K. (1986) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(86)90097-x · Cited by 19 · see citing works
CO2 enhanced peroxidase activity of SOD1: the effects of pH
Liochev, S. I., & Fridovich, I. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.03.006 · Cited by 19 · see citing works
Conformationally Gated Metal Uptake by Apomanganese Superoxide Dismutase
Whittaker, M. M., & Whittaker, J. W. (2008) · Biochemistry · doi:10.1021/bi8015636 · Cited by 19 · see citing works
Reevaluation of the reactivity of hydroxylamine with O2−/HO2
Bielski, B. H. J., Arudi, R. L., Cabelli, D. E., & Bors, W. (1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90539-6 · Cited by 17 · see citing works
Self-citationRole of a Glutamate Bridge Spanning the Dimeric Interface of Human Manganese Superoxide Dismutase ,
Quint, P. S., Domsic, J. F., Cabelli, D. E., McKENNA, R. V., & Silverman, D. N. (2008) · Biochemistry · doi:10.1021/bi7024518 · Cited by 17 · see citing works
Self-citationOxidative Stress in Familial Amyotrophic Lateral Sclerosis
Cabelli, D. E. (2003) · doi:10.1201/9780203912874-21 · Cited by 2 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Superoxide Dismutases: Role in Redox Signaling, Vascular Function, and Diseases
Fukai, T., & Ushio‐Fukai, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3999 · Cited by 2,009 · see citing works
Jomova, K., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2024) · Archives of Toxicology · doi:10.1007/s00204-024-03696-4 · Cited by 1,445 · see citing works
13 reasons why the brain is susceptible to oxidative stress
Cobley, J. N., Fiorello, M. L., & Bailey, D. M. (2018) · Redox Biology · doi:10.1016/j.redox.2018.01.008 · Cited by 1,215 · see citing works
Superoxide dismutases and superoxide reductases
Sheng, Y., Abreu, I. A., Cabelli, D. E., Maroney, M. J., Miller, A.-F., Teixeira, M., & Valentine, J. S. (2014) · Chemical Reviews · doi:10.1021/cr4005296 · Cited by 1,081 · see citing works
Self-citationNrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease
Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130 · see citing works
Reactive oxygen species and cancer paradox: To promote or to suppress?
Galadari, S., Rahman, A. U., Pallichankandy, S., & Thayyullathil, F. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.01.004 · Cited by 895 · see citing works
Oxidative stress and its role in cancer
Jelic, M. D., Mandić, A., Maričić, S., & Čonić, B. S. (2019) · Journal of Cancer Research and Therapeutics · doi:10.4103/jcrt.jcrt_862_16 · Cited by 739 · see citing works
Superoxide dismutase nanozymes: an emerging star for anti-oxidation
Zhao, H., Zhang, R., Yan, X., & Fan, K. (2021) · Journal of Materials Chemistry B · doi:10.1039/d1tb00720c · Cited by 536 · see citing works
Biological and physiological role of reactive oxygen species - the good, the bad and the ugly
Zuo, L., Zhou, T., Pannell, B. K., Ziegler, A. C., & Best, T. M. (2015) · Acta Physiologica · doi:10.1111/apha.12515 · Cited by 430 · see citing works
Trace metal metabolism in plants
Andresen, E., Peiter, E., & Küpper, H. (2018) · Journal of Experimental Botany · doi:10.1093/jxb/erx465 · Cited by 431 · see citing works
Manganese superoxide dismutase, MnSOD and its mimics
Miriyala, S., Spasojević, I., Tovmasyan, A. G., Salvemini, D., Vujašković, Ž., Clair, D. K. S., & Batinic̈‐Haberle, I. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.002 · Cited by 400 · see citing works
Raedschelders, K., Ansley, D. M., & Chen, D. D. Y. (2011) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.11.004 · Cited by 387 · see citing works
Redox Signaling by Reactive Electrophiles and Oxidants
Parvez, S., Long, M. J. C., Poganik, J. R., & Aye, Y. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00698 · Cited by 356 · see citing works
Nickel-dependent metalloenzymes
Boer, J. L., Mulrooney, S. B., & Hausinger, R. P. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.09.002 · Cited by 345 · see citing works
Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342 · see citing works
What Are Reactive Oxygen Species, Free Radicals, and Oxidative Stress in Skin Diseases?
Nakai, K., & Tsuruta, D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910799 · Cited by 319 · see citing works
The Biochemical Properties of Manganese in Plants
Schmidt, S. B., & Husted, S. (2019) · Plants · doi:10.3390/plants8100381 · Cited by 279 · see citing works
Copper and Iron Homeostasis in Plants: The Challenges of Oxidative Stress
Ravet, K., & Pilon, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5084 · Cited by 261 · see citing works
Reactive oxygen species and antioxidant defense in human gastrointestinal diseases
Patlevič, P., Vašková, J., Švorc, P., Vaško, L., & Švorc, P. (2016) · Integrative Medicine Research · doi:10.1016/j.imr.2016.07.004 · Cited by 240 · see citing works
A Review of the Catalytic Mechanism of Human Manganese Superoxide Dismutase
Azadmanesh, J., & Borgstahl, G. E. O. (2018) · Antioxidants · doi:10.3390/antiox7020025 · Cited by 212 · see citing works
The biogenesis and physiological function of chloroplast superoxide dismutases
Pilon, M., Ravet, K., & Tapken, W. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.11.002 · Cited by 209 · see citing works
The beneficial roles of trace and ultratrace elements in plants
Kaur, H., Kaur, H., Kaur, H., & Srivastava, S. (2022) · Plant Growth Regulation · doi:10.1007/s10725-022-00837-6 · Cited by 205 · see citing works
The Role of Antioxidant Enzymes in the Ovaries
Wang, S., He, G., Chen, M., Zuo, T., Xu, W., & Liu, X. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/4371714 · Cited by 180 · see citing works
Mysteries of Metals in Metalloenzymes
Valdez, C. E., Smith, Q. A., Nechay, M. R., & Alexandrova, A. N. (2014) · Accounts of Chemical Research · doi:10.1021/ar500227u · Cited by 179 · see citing works
Manganese complexes displaying superoxide dismutase activity: A balance between different factors
Iranzo, O. (2011) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2011.02.001 · Cited by 176 · see citing works
Batinic̈‐Haberle, I., Tovmasyan, A. G., & Spasojević, I. (2015) · Redox Biology · doi:10.1016/j.redox.2015.01.017 · Cited by 170 · see citing works
Oxidative Stress in Healthy and Pathological Red Blood Cells
Orrico, F., Laurance, S., Lopez, A. C., Lefevre, S. D., Thomson, L., Möller, M. N., & Ostuni, M. A. (2023) · Biomolecules · doi:10.3390/biom13081262 · Cited by 171 · see citing works
Diwanji, N., & Bergmann, A. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.07.004 · Cited by 154 · see citing works
Lee, J., Jo, D., Park, D., Chung, H. Y., & Mattson, M. P. (2014) · Pharmacological Reviews · doi:10.1124/pr.113.007757 · Cited by 154 · see citing works
Zhao, Q., Zhou, L., Liu, J., Du, X., Asad, M., Huang, F., Pan, G., & Cheng, F. (2017) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2017.11.009 · Cited by 152 · see citing works
Controlling Redox Status for Stem Cell Survival, Expansion, and Differentiation
Sart, S., Song, L., & Li, Y. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/105135 · Cited by 143 · see citing works
Jurcău, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111847 · Cited by 150 · see citing works
Implications of Antioxidant Systems in Inflammatory Bowel Disease
Guan, G., & Lan, S. (2018) · BioMed Research International · doi:10.1155/2018/1290179 · Cited by 134 · see citing works
Comparative and Functional Algal Genomics
Blaby-Haas, C. E., & Merchant, S. S. (2019) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-050718-095841 · Cited by 131 · see citing works
Grover, K., Koblova, A., Pezacki, A. T., Chang, C. J., & New, E. J. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00819 · Cited by 129 · see citing works
Jiang, W. J., Yang, L., He, Y. H., Zhang, H., Li, W., Chen, H., Ma, D. M., & Yin, J. (2019) · PeerJ · doi:10.7717/peerj.8062 · Cited by 128 · see citing works
Manganese Kβ X-ray Emission Spectroscopy As a Probe of Metal–Ligand Interactions
Beckwith, M. A., Roemelt, M., Collomb, M., Duboc, C., Weng, T., Bergmann, U., Glatzel, P., Neese, F., & DeBeer, S. (2011) · Inorganic Chemistry · doi:10.1021/ic200970t · Cited by 127 · see citing works
Mitochondrial oxidative metabolism and uncoupling proteins in the failing heart
Akhmedov, A. T., Rybin, V. O., & Marı́n-Garcı́a, J. (2014) · Heart Failure Reviews · doi:10.1007/s10741-014-9457-4 · Cited by 125 · see citing works
Chemical Properties, Environmental Fate, and Degradation of Seven Classes of Pollutants
Manzetti, S., van der Spoel, E. R., & van der Spoel, D. (2014) · Chemical Research in Toxicology · doi:10.1021/tx500014w · Cited by 125 · see citing works
Signorella, S., Palopoli, C. M., & Ledesma, G. N. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.03.005 · Cited by 125 · see citing works
Redox regulation of cell state and fate
Lee, B. W. L., Ghode, P. B., & Ong, D. S. T. (2018) · Redox Biology · doi:10.1016/j.redox.2018.11.014 · Cited by 120 · see citing works
Lalaouna, D., Baude, J., Wu, Z., Tomasini, A., Chicher, J., Marzi, S., Vandenesch, F., Romby, P., Caldelari, I., & Moreau, K. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz728 · Cited by 114 · see citing works
Bimetal Biomimetic Engineering Utilizing Metal–Organic Frameworks for Superoxide Dismutase Mimic
Wu, T. S., Huang, S., Yang, H., Ye, N., Tong, L., Chen, G., Zhou, Q., & Ouyang, G. (2022) · ACS Materials Letters · doi:10.1021/acsmaterialslett.2c00075 · Cited by 116 · see citing works
Oxidants and Antioxidants in the Redox Biochemistry of Human Red Blood Cells
Möller, M. N., Orrico, F., Villar, S. F., López, A. C., Silva, N., Donzé, M., Thomson, L., & Denicola, A. (2022) · ACS Omega · doi:10.1021/acsomega.2c06768 · Cited by 116 · see citing works
Complex Regulation of Mitochondrial Function During Cardiac Development
Zhao, Q., Sun, Q., Zhou, L., Liu, K., & Jiao, K. (2019) · Journal of the American Heart Association · doi:10.1161/jaha.119.012731 · Cited by 112 · see citing works
Enzyme Inhibitors and Activators
Şentürk, M. (2017) · InTech eBooks · doi:10.5772/63325 · Cited by 113 · see citing works
Polydopamine, harness of the antibacterial potentials-A review
He, X., Obeng, E., Sun, X., Kwon, N., Shen, J., & Yoon, J. (2022) · Materials Today Bio · doi:10.1016/j.mtbio.2022.100329 · Cited by 112 · see citing works
Çakmak, İ., Brown, P. H., Colmenero-Flores, J. M., Husted, S., Kutman, B. Y., Nikolić, M., Rengel, Z., Schmidt, S. B., & Zhao, F. J. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-819773-8.00017-4 · Cited by 115 · see citing works
Zhang, J., Li, C., Zhang, R., Zhang, F., Liu, W., Liu, X., Lee, S. M., & Zhang, H. (2016) · Chemical Communications · doi:10.1039/c5cc09976e · Cited by 108 · see citing works
Analysis and characterization of coordination compounds by resonance Raman spectroscopy
Wächtler, M., Guthmuller, J., González, L., & Dietzek, B. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.02.004 · Cited by 107 · see citing works
Metal-mediated DNA damage and cell death: mechanisms, detection methods, and cellular consequences
Angelé-Martínez, C., Goodman, C., & Brumaghim, J. L. (2014) · Metallomics · doi:10.1039/c4mt00057a · Cited by 105 · see citing works
Castro-Alférez, M., Polo-López, M. I., Marugán, J., & Fernández‐Ibañez, P. (2016) · Chemical Engineering Journal · doi:10.1016/j.cej.2016.06.093 · Cited by 105 · see citing works
Zhou, Y., Hu, L., Wu, H., Jiang, L., & Liu, S. (2017) · International Journal of Genomics · doi:10.1155/2017/7243973 · Cited by 104 · see citing works
Scavenging of superoxide by a membrane-bound superoxide oxidase
Lundgren, C. A. K., Sjöstrand, D., Biner, O., Bennett, M. D., Rudling, A., Johansson, A.-L., Brzezinski, P., Carlsson, J., von Ballmoos, C., & Högbom, M. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0072-x · Cited by 103 · see citing works
Inhibitors and Activators of SOD, GSH‐Px, and CAT
Ma, X., Deng, D., & Chen, W. (2017) · InTech eBooks · doi:10.5772/65936 · Cited by 100 · see citing works
Shevela, D., Koroidov, S., Najafpour, M. M., Messinger, J., & Kurz, P. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201002548 · Cited by 98 · see citing works
Su, W., Raza, A., Gao, A., Jia, Z., Zhang, Y., Hussain, M. A., Mehmood, S. S., Cheng, Y., Lv, Y., & Zou, X. (2021) · Antioxidants · doi:10.3390/antiox10081182 · Cited by 96 · see citing works
Küçükler, S., Darendelioğlu, E., Çağlayan, C., Ayna, A., Yıldırım, S., & Kandemır, F. M. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118382 · Cited by 94 · see citing works
Huang, X., Shin, J., Pinochet‐Barros, A., Su, T. T., & Helmann, J. D. (2017) · Molecular Microbiology · doi:10.1111/mmi.13554 · Cited by 93 · see citing works
Brophy, M. B., & Nolan, E. M. (2015) · ACS Chemical Biology · doi:10.1021/cb500792b · Cited by 88 · see citing works
Chen, Y., Chen, T., Wu, X., & Yang, G. (2018) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2018.09.120 · Cited by 88 · see citing works
Mahapatra, B., Dhal, N. K., Dash, A. K., Panda, B. P., Panigrahi, K. C. S., & Pradhan, A. (2019) · Environmental Science and Pollution Research · doi:10.1007/s11356-019-06270-z · Cited by 90 · see citing works
Xu, Y., Huang, A., Yi, W., Chen, G., Huang, S., & Chen, G. (2023) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2023.215517 · Cited by 85 · see citing works
Protection Mechanisms of Periphytic Biofilm to Photocatalytic Nanoparticle Exposure
Zhu, N., Wang, S., Tang, C., Duan, P., Yao, L., Tang, J., Wong, P. K., An, T., Dionysiou, D. D., & Wu, Y. (2019) · Environmental Science & Technology · doi:10.1021/acs.est.8b04923 · Cited by 83 · see citing works
Gao, Y., Ray, S., Dai, S., Ivanov, A. R., Abu‐Absi, N. R., Lewis, A. M., Huang, Z., Xing, Z., Borys, M. C., Li, Z. J., et al. (2016) · Biotechnology Journal · doi:10.1002/biot.201600030 · Cited by 76 · see citing works
Catalysis and Electron Transfer in De Novo Designed Metalloproteins
Koebke, K. J., Pinter, T. B. J., Pitts, W. C., & Pecoraro, V. L. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c01025 · Cited by 81 · see citing works
Targeting reactive oxygen species in development and progression of pancreatic cancer
Durand, N., & Störz, P. (2016) · Expert Review of Anticancer Therapy · doi:10.1080/14737140.2017.1261017 · Cited by 78 · see citing works
Iron-containing urease in a pathogenic bacterium
Carter, E. L., Tronrud, D. E., Taber, S. R., Karplus, P. A., & Hausinger, R. P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106915108 · Cited by 79 · see citing works
Houmani, H., Rodríguez-Ruiz, M., Palma, J. M., Abdelly, C., & Corpas, F. J. (2015) · PROTOPLASMA · doi:10.1007/s00709-015-0850-1 · Cited by 79 · see citing works
Umasuthan, N., Bathige, S. D. N. K., Revathy, K. S., Lee, Y., Whang, I., Choi, C. Y., Park, H., & Lee, J. (2012) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2012.06.024 · Cited by 78 · see citing works
Glutathione peroxidase 1 activity dictates the sensitivity of glioblastoma cells to oxidative stress
Đokić, I., Hartmann, C. J., Herold‐Mende, C. C., & Régnier‐Vigouroux, A. (2012) · Glia · doi:10.1002/glia.22397 · Cited by 76 · see citing works
Korschelt, K., Ragg, R., Metzger, C., Kluenker, M., Oster, M., Barton, B., Panthöfer, M., Strand, D. J., Kolb, U., Mondeshki, M., et al. (2017) · Nanoscale · doi:10.1039/c6nr09810j · Cited by 75 · see citing works
Reactive Oxygen Species: A Double-Edged Sword in the Modulation of Cancer Signaling Pathway Dynamics
Nigam, M., Punia, B., Dimri, D. B., Mishra, A. P., Radu, A.-F., & Bungau, G. S. (2025) · Cells · doi:10.3390/cells14151207 · Cited by 77 · see citing works
Zhang, Q., Wu, H., Zou, M., Li, L., Li, Q., Sun, C., Xia, W. T., Cao, Y., & Wu, L. (2019) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2019.05.002 · Cited by 72 · see citing works
Foyet, H. S., Abaïssou, H. H. N., Wado, E. K., Asongalem, E. A., & Ciobica, A. S. (2015) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-015-0864-4 · Cited by 72 · see citing works
Shigemitsu, H., Ohkubo, K., Sato, K., Bunno, A., Mori, T., Osakada, Y., Fujitsuka, M., & Kida, T. (2022) · JACS Au · doi:10.1021/jacsau.2c00243 · Cited by 70 · see citing works
Friedel, F. C., Lieb, D., & Ivanović‐Burmazović, I. (2011) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2011.12.008 · Cited by 70 · see citing works
Han, L., Hua, W., Cao, X., Yan, J., Chen, C., & Wang, Z. (2020) · Gene · doi:10.1016/j.gene.2020.144603 · Cited by 69 · see citing works
Pathways of Superoxide (O2–) Decay in the Eastern Tropical North Atlantic
Wuttig, K., Heller, M. I., & Croot, P. L. (2013) · Environmental Science & Technology · doi:10.1021/es401658t · Cited by 67 · see citing works
Modulation of Superoxide Dismutase Activity by Mercury, Lead, and Arsenic
Kumar, A., Khushboo, Pandey, R., & Sharma, B. (2020) · Biological Trace Element Research · doi:10.1007/s12011-019-01957-3 · Cited by 64 · see citing works
Huang, W., Hutabarat, R. P., Chai, Z., Zheng, T., Zhang, W., & Li, D. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051575 · Cited by 64 · see citing works
Tiwari, M. K., Hägglund, P., Møller, I. M., Davies, M. J., & Bjerrum, M. J. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101262 · Cited by 61 · see citing works
Oxidative stress and aging: Learning from yeast lessons
Eleuthério, E. C. A., Brasil, A. D. A., França, M. B., de Almeida, D. S. G., Rona, G. B., & Magalhães, R. S. S. (2017) · Fungal Biology · doi:10.1016/j.funbio.2017.12.003 · Cited by 63 · see citing works
Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase
Azadmanesh, J., Lutz, W. E., Coates, L., Weiss, K. L., & Borgstahl, G. E. O. (2021) · Nature Communications · doi:10.1038/s41467-021-22290-1 · Cited by 61 · see citing works
A mitochondrion targeting fluorescent probe for imaging of intracellular superoxide radicals
Si, F., Liu, Y., Yan, K., & Zhong, W. (2015) · Chemical Communications · doi:10.1039/c5cc01075f · Cited by 61 · see citing works
Coggins, M. K., & Kovacs, J. A. (2011) · Journal of the American Chemical Society · doi:10.1021/ja205520u · Cited by 60 · see citing works
Biological Functions of the Elements
Lindh, U. (2012) · Springer eBooks · doi:10.1007/978-94-007-4375-5_7 · Cited by 60 · see citing works
Niemann, J., Johne, C., Schröder, S., Koch, F., Ibrahim, S. M., Schultz, J., Tiedge, M., & Baltrusch, S. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.11.035 · Cited by 59 · see citing works
Das, A. K., Anbu, N., Mostakim, S. K., Dhakshinamoorthy, A., & Biswas, S. (2019) · Dalton Transactions · doi:10.1039/c9dt03638e · Cited by 59 · see citing works
Geven, M. A., d’Arcy, R., Turhan, Z. Y., Mohtadi, F. E., Alshamsan, A., & Tirelli, N. (2021) · European Polymer Journal · doi:10.1016/j.eurpolymj.2021.110387 · Cited by 60 · see citing works
Vincent, A., Thauvin, M., Quévrain, E., Mathieu, E., Layani, S., Seksik, P., Batinic-Haberle, I., Vriz, S., Policar, C., & Delsuc, N. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111431 · Cited by 58 · see citing works
Huo, C., He, L., Yu, T., Ji, X., Li, R., Zhu, S., Zhang, F., Xie, H., & Liu, W. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.904105 · Cited by 57 · see citing works
Mn(II)-enhanced oxidation of benzoic acid by Fe(III)/H2O2 system
Zhao, J., Yang, J., & Ma, J. (2013) · Chemical Engineering Journal · doi:10.1016/j.cej.2013.11.014 · Cited by 57 · see citing works
Oliveira, J. T. A., Andrade, N., Martins-Miranda, A. S., Soares, A. A., Gondim, D. M. F., Araújo-Filho, J. H., Freire-Filho, F. R., & Vasconcelos, I. M. (2011) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2011.10.008 · Cited by 57 · see citing works
Redox Signaling from Mitochondria: Signal Propagation and Its Targets
Ježek, P., Holendová, B., & Plecitá-Hlavatá, L. (2020) · Biomolecules · doi:10.3390/biom10010093 · Cited by 54 · see citing works
Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking
Capdevila, D. A., Rondón, J. J., Edmonds, K. A., Rocchio, J. S., Dujovne, M. V., & Giedroc, D. P. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00264 · Cited by 59 · see citing works
Pulse Radiolysis Studies for Mechanism in Biochemical Redox Reactions
Kobayashi, K. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00405 · Cited by 56 · see citing works
Banerjee, A., Mohanty, M., Lima, S., Samanta, R., Garribba, E., Sasamori, T., & Dinda, R. (2020) · New Journal of Chemistry · doi:10.1039/d0nj01246g · Cited by 56 · see citing works
Yadav, S., Gill, S. S., Passricha, N., Gill, R., Badhwar, P., Anjum, N. A., Jiménez-Bremont, J. F., & Tuteja, N. (2018) · Plant Gene · doi:10.1016/j.plgene.2018.10.001 · Cited by 55 · see citing works
Cobley, J. N. (2020) · Antioxidants · doi:10.3390/antiox9100933 · Cited by 56 · see citing works
- Authors
- Abreu, I. A., & Cabelli, D. E.
- Affiliations
- Universidade Nova de Lisboa (PT)
- Brookhaven National Laboratory (US)
- Corresponding author
- Cabelli, Diane E.
- ORCID
- Abreu, Isabel A.
- Venue
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Publisher
- Elsevier BV
- Published
- 2010-02
- Volume
- 1804
- Issue
- 2
- Pages
- 263-274
- ISSN
- 1570-9639 (ISSN-L)
- OpenAlex
- W2028661305
- Cited by
- 563
- References
- 99
- Citations by year
- 2026: 26 · 2025: 44 · 2024: 31 · 2023: 41 · 2022: 47 · 2021: 60 · 2020: 34 · 2019: 38 · 2018: 35 · 2017: 43 · 2016: 43 · 2015: 26 · 2014: 30 · 2013: 19 · 2012: 20
- FWCI
- 0.29
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Fundação para a Ciência e a Tecnologia
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- superoxide dismutase, copper-zinc superoxide dismutase, manganese superoxide dismutase, enzyme mechanism, metalloenzyme catalysis, superoxide, hydrogen peroxide production, copper, iron, manganese, nickel, diffusion-controlled rate constants
- MeSH terms
- Animals, Copper, Humans, Iron, Manganese, Superoxide Dismutase, Zinc, Biocatalysis
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review