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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Clinical Pharmacokinetics of Antioxidants and Their Impact on Systemic Oxidative Stress
TL;DR: This article addresses data provided from clinical trials, highlighting the clinical pharmacokinetics of vitamin C, vitamin E, β-carotene, lycopene, lutein, quercetin, rutin, catechins and selenium.
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Superoxide Dismutase and Oxygen Toxicity in a Eukaryote
TL;DR: Data indicate that, in both prokaryotes and in eukaryotes, superoxide dismutase is an important component of the defenses against oxygen toxicity.
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Oxygen Free Radicals and Human Diseases
TL;DR: Free RADICALS and other reactive oxygen species are constantly formed in the human body, but they can be toxic when generated in excess and this toxicity is often aggravated by the presence of ions of such transition metals as iron or copper.
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Protection from Oxygen Toxicity with Endotoxin: ROLE OF THE ENDOGENOUS ANTIOXIDANT ENZYMES OF THE LUNG
TL;DR: It is concluded that, in the rat, a single dose of endotoxin given even 36 h after the onset of hyperoxic exposure results in marked protection against O(2)-induced lung damage; and the increased lung antioxidant enzyme activity in the endotoxin-treated rats appears to be an essential component of this protective action.
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Detection and Quantification of Superoxide Formed within the Periplasm of Escherichia coli
Sergei Korshunov,James A. Imlay +1 more
TL;DR: It is inferred that the adventitious autoxidation of dihydromenaquinone in the cytoplasmic membrane releases a steady flux of superoxide into the periplasm of E. coli, which may create oxidative stress in that compartment and be a primary substrate of CuZnSOD.
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.