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Open AccessJournal ArticleDOI

Superoxide Dismutase AN ENZYMIC FUNCTION FOR ERYTHROCUPREIN (HEMOCUPREIN)

Joe M. McCord, +1 more
- 25 Nov 1969 - 
- Vol. 244, Iss: 22, pp 6049-6055
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TLDR
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.
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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.

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Citations
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The emerging role of reactive oxygen and nitrogen species in redox biology and some implications for plasma applications to medicine and biology

TL;DR: The importance of ROS and RNS to plant biology has been relatively little appreciated in the plasma biomedicine community, but it appears that there are opportunities for useful applications of plasmas in this area as well.
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Wilson's Disease

TL;DR: The discovery of the Wilson's disease gene has opened up a new molecular diagnostic approach, and could form the basis of future gene therapy.
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Review on in vivo and in vitro methods evaluation of antioxidant activity.

TL;DR: DPPH method was found to be used mostly for the in vitro antioxidant activity evaluation purpose while LPO was found as mostly used in vivo antioxidant assay.
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Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria.

TL;DR: Experiments with succinate as electron donor in the presence of antimycin A in intact rat heart mitochondria showed that myxothiazol, which inhibits reduction of the Rieske iron-sulfur center, prevented formation of hydrogen peroxide, determined spectrophotometrically as the H2O2-peroxidase complex.
References
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Journal ArticleDOI

The Reduction of Cytochrome c by Milk Xanthine Oxidase

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 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.
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