The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Superoxide radical inhibits catalase.
Open accessAbstract
Catalase was inhibited by a flux of O2- generated in situ by the aerobic xanthine oxidase reaction. Two distinct types of inhibition could be distinguished. One of these was rapidly established and could be as rapidly reversed by the addition of superoxide dismutase. The second developed slowly and was reversed by ethanol, but not by superoxide dismutase. The rapid inhibition was probably due to conversion of catalase to the ferrooxy state (compound III), while the slow inhibition was due to conversion to the ferryl state (compound II). Since neither compound III nor compound II occurs in the catalatic reaction pathway, they are inactive. This inhibition of catalase by O2- provides the basis for a synergism between superoxide dismutase and catalase. Such synergisms have been observed in vitro and may be significant in vivo.
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Cites
(1975) · Journal of AOAC INTERNATIONAL · doi:10.1093/jaoac/58.5.1085 · Cited by 19,795
A SPECTROPHOTOMETRIC METHOD FOR MEASURING THE BREAKDOWN OF HYDROGEN PEROXIDE BY CATALASE
Beers, R. F., & Sizer, I. W. (1952) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50881-x · Cited by 6,761
Nishikimi, M., Appaji Rao, N., & Yagi, K. (1972) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(72)80218-3 · Cited by 4,075
Quantitative Aspects of the Production of Superoxide Anion Radical by Milk Xanthine Oxidase
Fridovich, I. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62884-4 · Cited by 1,035
Self-citationSuperoxide‐dependent production of hydroxyl radical catalyzed by iron—EDTA complex
McCord, J. M., & Day, E. D. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80116-1 · Cited by 868
Hodgson, E. K., & Fridovich, I. (1975) · Biochemistry · doi:10.1021/bi00695a010 · Cited by 782
Self-citationHalliwell, B. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80779-0 · Cited by 742
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
Self-citationLiposome oxidation and erythrocyte lysis by enzymically generated superoxide and hydrogen peroxide.
Kellogg, E. W., & Fridovich, I. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39909-x · Cited by 509
Self-citationMechanism of the disproportionation of superoxide radicals
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Cited by
Oxidative stress and some antioxidant systems in acid rain-treated bean plants
Velikova, V, Yordanov, I., & Edreva, A. (2000) · Plant Science · doi:10.1016/s0168-9452(99)00197-1 · Cited by 5,299
Oxygen free radicals and iron in relation to biology and medicine: Some problems and concepts
Halliwell, B., & Gutteridge, J. M. C. (1986) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(86)90305-x · Cited by 2,038
Valavanidis, A., Vlahogianni, T., Dassenakis, M., & Scoullos, M. (2006) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2005.03.013 · Cited by 1,795
Mao, Y.-B., Cai, W.-J., Wang, J.-W., Hong, G.-J., Tao, X.-Y., Wang, L.-J., Huang, Y.-P., & Chen, X.-Y. (2007) · Nature Biotechnology · doi:10.1038/nbt1352 · Cited by 1,358
Intracellular Antioxidants: from Chemical to Biochemical Mechanisms
Chaudière, J., & Ferrari-Iliou, R. (1999) · Food and Chemical Toxicology · doi:10.1016/s0278-6915(99)00090-3 · Cited by 671
Metadata
- Authors
- Kono, Y., & Fridovich, I.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1982-05
- Volume
- 257
- Issue
- 10
- Pages
- 5751-5754
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1481433938
- Cited by
- 1,251
- References
- 23
- FWCI
- 10.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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