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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Radical scavenging properties of polyamines
TL;DR: Di- and polyamines are effective scavengers of free radicals generated in a number of chemical and in vitro enzyme systems and some of the physiological effects of polyamines, in particular their propensity to inhibit lipid peroxidation and retard senescence, may be attributable to their radical-scavenging capability.
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The basic chemistry of nitrogen monoxide and peroxynitrite
TL;DR: After a discussion of the physical chemistry of nitrogen monoxide, several reactions that can acts as sinks are discussed, namely the reaction with dioxygen, with thiols and with superoxide, which leads to a powerful oxidant, peroxynitrite.
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SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model
Maged M. Harraz,Jennifer J. Marden,Weihong Zhou,Yulong Zhang,Aislinn J. Williams,Victor S. Sharov,Kathryn Nelson,Meihui Luo,Henry L. Paulson,Christian Schöneich,John F. Engelhardt +10 more
TL;DR: It is demonstrated that SOD1 is not just a catabolic enzyme, but can also directly regulate NADPH oxidase-dependent (Nox-dependent) O(2)(*-) production by binding Rac1 and inhibiting its GTPase activity.
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Copper, zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide
TL;DR: The capacity of Cu,Zn-SOD to generate "free" .OH radicals from H2O2 may in part explain the biological damage associated with elevated intracellular SOD activity.
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Reactive oxygen species and antioxidant mechanisms in human tissues and their relation to malignancies
Peeter Karihtala,Ylermi Soini +1 more
TL;DR: The present review aims to clarify the significance of oxidative stress and the role of cell redox state modulating systems in human malignancies in light of the current literature.
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.