Superoxide Dismutase AN ENZYMIC FUNCTION FOR ERYTHROCUPREIN (HEMOCUPREIN)
Joe M. McCord,Irwin Fridovich +1 more
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The demonstration that O2·- can reduce ferricytochrome c and tetranitromethane, and that superoxide dismutase, by competing for the superoxide radicals, can markedly inhibit these reactions, is demonstrated.About:
This article is published in Journal of Biological Chemistry.The article was published on 1969-11-25 and is currently open access. It has received 12468 citations till now. The article focuses on the topics: Copper chaperone for superoxide dismutase & Superoxide reductase.read more
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The role of superoxide and singlet oxygen in lipid peroxidation promoted by xanthine oxidase
Thoru Pederson,Steven D. Aust +1 more
TL;DR: It is suggested that the peroxidative oxidation of unsaturated lipid promoted by xanthine oxidase involves the formation of singinglet oxygen from superoxide, and the singlet oxygen reacts with the lipid to form fatty acid hydroperoxides.
Journal ArticleDOI
Are respiratory enzymes the primary sources of intracellular hydrogen peroxide
TL;DR: Mutants that lacked both NADH dehydrogenases respired very slowly, as expected; however, these mutants showed no diminution of H2O2 excretion, suggesting that H1O2 is primarily formed by a source outside the respiratory chain, which has not yet been identified.
Journal ArticleDOI
Single and combined effects of microplastics and cadmium on the cadmium accumulation, antioxidant defence and innate immunity of the discus fish (Symphysodon aequifasciatus)
TL;DR: It is suggested that exposure to Cd led to reduced Cd accumulation in the presence of MPs, which could induce severe oxidative stress and stimulate innate immunity in the juvenile S. aequifasciatus.
Journal ArticleDOI
The active site of galactose oxidase.
TL;DR: It is found that the form which has been extensively probed by EPR spectroscopy is devoid of catalytic activity and does not interact with substrate, indicating that the one-electron redox process which converts the inactive form to catalytically active enzyme is associated with oxidation of the protein rather than the metal center as has been proposed previously.
Book ChapterDOI
Reactions of nitric oxide, superoxide and peroxynitrite with superoxide dismutase in neurodegeneration.
TL;DR: This chapter describes how low concentrations of nitric oxide do not react rapidly with oxygen to form nitrogen dioxide and proposes that this mechanism may account for the pathological action of SOD mutations in amyotrophic lateral sclerosis.
References
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The Reduction of Cytochrome c by Milk Xanthine Oxidase
Joe M. McCord,Irwin Fridovich +1 more
TL;DR: The data are consistent with the conclusion that xanthine oxidase generates an unstable reduced form of oxygen, presumably the superoxide anion, and that this radical is the agent which directly reduces cytochrome c and initiates the sulfite-oxygen chain reaction.
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The microestimation of succinate and the extinction coefficient of cytochrome c.
Journal ArticleDOI
The Preparation and Properties of Deflavo Xanthine Oxidase
TL;DR: The deflavoenzyme is catalytically active in the oxidation of xanthine with acceptors such as ferricyanide and cytochrome c.
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The mechanism of aerobic oxidase reaction catalyzed by peroxidase.
TL;DR: It has been found that peroxidase catalyzes the formation of free radicals of hydrogen donors in the presence of H 2 O 2, and Compound III is not an active intermediate for dihydroxyfumarate oxidation.
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Electron-spin-resonance evidence for enzymic reduction of oxygen to a free radical, the superoxide ion.
TL;DR: It is concluded that the species observed is the superoxide ion, O(2) (-), and that the stability of this ion is greatly increased in alkaline solution.