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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 regulation of mitochondrial oxygen uptake by redox reactions involving nitric oxide and ubiquinol.

TL;DR: Calculations indicate that mitochondrial ·NO decays primarily by pathways involving ONOO– formation and ubiquinol oxidation and, secondarily, by reversible binding to cytochrome oxidase.
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Endogenous peroxynitrite mediates mitochondrial dysfunction in rat diaphragm during endotoxemia

TL;DR: Results show that increased and sustained NO levels lead to a consecutive formation of O2−· that reacts with NO to form peroxynitrite, which in turn impairs mitochondrial function, which probably contributes to the impairment of muscle contractility.
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β-Amyloid (1–42)-induced learning and memory deficits in mice: involvement of oxidative burdens in the hippocampus and cerebral cortex

TL;DR: Whether oxidative stress contributes to the memory deficits induced by intracerebroventricular injection of Abeta (1-42) in mice is examined and the antioxidant alpha-tocopherol significantly prevented these oxidative stresses.
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Detection of reactive oxygen and reactive nitrogen species in skeletal muscle

TL;DR: A large body of evidence now indicates that ROS and RNS are continually produced by many different skeletal muscle types studied in vivo, in situ, and in vitro, and the molecular species that mediate specific biological effects remains largely undetermined.
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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