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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Protective effect of vitamin E in dimethoate and malathion induced oxidative stress in rat erythrocytes
TL;DR: Vitamin E may amelierate OP-induced oxidative stress by decreasing LPO and altering antioxidant defense system in erthrocytes, which indicates that vitamin E provide protection against OP- induced oxidative stress.
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Hydrogen peroxide metabolism in human monocytes during differentiation in vitro.
TL;DR: The differentiation of human monocytes into macrophages in vitro is accompanied by an apparent reduction in the capacity to produce H2O2 and O2 - in this regard, the human monocyte-derived macrophage comes to resemble the resting tissuemacrophage previously characterized in the mouse peritoneal cavity.
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Intrinsic oxidative stress in cancer cells: a biochemical basis for therapeutic selectivity
TL;DR: The increased oxidative stress in cancer cells forces these cells to rely more on antioxidant enzymes such as SOD for O2− elimination, thus making the malignant cells more vulnerable to SOD inhibition than normal cells.
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The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells.
TL;DR: Data from oxidant-sensitive fluorescent probes can provide some information on cellular redox activity but is widely misinterpreted, and more information on specificity and cellular reactions is needed.
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Superoxide dismutase plus catalase enhances the efficacy of hypothermic cardioplegia to protect the globally ischemic, reperfused heart.
TL;DR: It is concluded that supplementing hypothermic cardioplegia solution with enzymes gave protection which was significantly better than that obtained with the other interventions, with values of these indicators not significantly different from those of nonischemic perfused controls.
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.