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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Mitochondrial metabolism of reactive oxygen species
TL;DR: Experimental evidence indicates that the systems, evolved to protect mitochondria against endogenously produced ROS, can also scavenge ROS produced by other cellular sources, leading to the elimination of the old dysfunctional mitochondrial subpopulation.
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Solar disinfection is an augmentable, in situ-generated photo-Fenton reaction—Part 1: A review of the mechanisms and the fundamental aspects of the process
Stefanos Giannakis,María Inmaculada Polo López,Dorothee Spuhler,José Antonio Sánchez Pérez,Pilar Fernández Ibáñez,Cesar Pulgarin +5 more
TL;DR: In this article, a conceptual review concerning the photo-Fenton reaction at near-neutral pH, used for bacterial inactivation, is presented, where the effects of UVB and UVA on the bacterial cell are firstly discussed, followed by the presentation of the indirect oxidative stress-related inactivation mechanisms initiated into the microorganism, in presence of light.
Journal ArticleDOI
Kinetics and mechanism of the reduction of ferricytochrome c by the superoxide anion.
TL;DR: The mechanism of the reaction is discussed in terms of the approach of superoxide anion radicals to the heme edge and the available molecular orbitals of both heme and free radicals.
Journal ArticleDOI
Superoxide dismutase: A comparison of rate constants
Henry Jay Forman,Irwin Fridovich +1 more
TL;DR: The rate constant for the enzymatic dismutations catalyzed by the copper and zinc containing enzyme from bovine erythrocytes is independent of the concentration of O2− in the range 10−5 → 10−13m and is in full agreement with the results of pulse radiolytic investigations.
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Familial Amyotrophic Lateral Sclerosis-associated Mutations Decrease the Thermal Stability of Distinctly Metallated Species of Human Copper/Zinc Superoxide Dismutase
Jorge A. Rodriguez,Joan Selverstone Valentine,Daryl K. Eggers,James A. Roe,Ashutosh Tiwari,Robert H. Brown,Lawrence J. Hayward +6 more
TL;DR: It is concluded that decreased conformational stability shared by all of these mutant SOD1s may contribute to S OD1 toxicity in FALS.
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.