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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Metallochaperones, an intracellular shuttle service for metal ions.
TL;DR: The most recent advances in the understanding of copper metallochaperones are reviewed and mechanisms that may be relevant to other essential, yet potentially toxic, metal ions are discussed.
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Involvement of superoxide anion generation in the hypersensitive response of potato tuber tissues to infection with an incompatible race of Phytophthora infestans and to the hyphal wall components
TL;DR: Results indicate that an O 2 − -generating system may be activated in potato tissues during the incompatible interaction induced by invading fungi or fungal wall components, and also that the generation of O 1 − may be involved during hypersensitive cell death as a trigger of the sequence of resistance reactions.
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Superoxide dismutase delays neuronal apoptosis: A role for reactive oxygen species in programmed neuronal death
TL;DR: If NGF was added back to the culture medium after the period of peak ROS generation, apoptosis was completely prevented, suggesting that ROS production serves as an early signal, rather than a toxic agent, to mediate apoptosis.
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Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts
TL;DR: A role for peroxynitrite during development and progression of chronic rejection in human renal allografts is suggested, and inactivation of manganese superoxide dismutase by peroxlynitrite may represent a general mechanism that progressively increases the production of peroxysine nitration, leading to irreversible oxidative injury to mitochondria.
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The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme.
Ellen K. Hodgson,Irwin Fridovich +1 more
TL;DR: Bovine erythrocyte superoxide dismutase was slowly and irreversibly inactivated by hydrogen peroxide, and several compounds, including xanthine, urate, formate, and azide, protected the enzyme against inactivation by H2O2.
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.