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
Citations
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Superoxide Dismutases in Polymorphonuclear Leukocytes
Marvin L. Salin,Joe M. McCord +1 more
TL;DR: The superoxide dismutase-containing preparation of leukocytes released large amounts of superoxide into the medium when the cells were phagocytizing, suggesting that, if the cell population is homogeneous, superoxide production probably takes place on the outer surface of the cell membrane, in addition to inside the phagcytic vacuole.
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Exogenously applied polyamines increase drought tolerance of rice by improving leaf water status, photosynthesis and membrane properties.
TL;DR: It was revealed that drought stress severely reduced the rice fresh and dry weights, while PAs application improved net photosynthesis, water use efficiency, leaf water status, production of free proline, anthocyanins and soluble phenolics and improved membrane properties.
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Intracellular copper routing: the role of copper chaperones.
TL;DR: They are a family of conserved proteins present in prokaryotes and eukaryotes, which suggests that copper chaperones are used throughout nature for intracellular copper routing.
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The Tetrazolium Dyes MTS and XTT Provide New Quantitative Assays for Superoxide and Superoxide Dismutase
TL;DR: The stable MTS and XTT formazans have high extinction coefficients in the visible range which enable sensitive detection and quantification of superoxide radicals, avoiding some of the problems inherent in assays based on production of the insoluble NBT formazan.
Journal ArticleDOI
Relationship among Redox Potentials, Proton Dissociation Constants of Pyrrolic Nitrogens, and in Vivo and in Vitro Superoxide Dismutating Activities of Manganese(III) and Iron(III) Water-Soluble Porphyrins
Ines Batinic-Haberle,Ivan Spasojevic,Peter Hambright,Ludmil Benov,and Alvin L. Crumbliss,Irwin Fridovich +5 more
TL;DR: The log kcat values for the dismutation of O2•- by a series of monohydroxoiron and aquamanganese porphyrins, including ortho, meta, and para isomers of 5,10,15,20-tetrakis(N-alkylpyridiniumyl)porphyrins), were found to vary linearly with the metal-centered redox potentials (E1/2) for the M(III
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.
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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.