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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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Oxidative stress in health and disease: the therapeutic potential of Nrf2 activation.

TL;DR: The dysregulation of Nrf2-regulated genes provides a logical explanation for the connections between observable oxidative stress and perhaps 200 human diseases involving these various physiological processes, each reflecting a network involving many gene products.
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Parkinson's disease: a disorder due to nigral glutathione deficiency?

TL;DR: The hypothesis that loss of nigrostriatal dopaminergic neurons results from a regional GSH deficiency could have important therapeutic implications for the management and prevention of Parkinson's disease.
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.
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.
Journal ArticleDOI

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.
Journal ArticleDOI

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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