Superoxide Dismutase AN ENZYMIC FUNCTION FOR ERYTHROCUPREIN (HEMOCUPREIN)
Joe M. McCord,Irwin Fridovich +1 more
Reads0
Chats0
TLDR
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
Citations
More filters
Journal ArticleDOI
Quantitative aspects of the production of superoxide anion radical by milk xanthine oxidase
TL;DR: It was shown that at any given pH and oxygen tension, the amount of univalently reduced oxygen, which was detectable in terms of the reduction of cytochrome c, rose as the turnover rate of the enzyme was decreased by decreasing the concentration of xanthine.
Journal Article
Role of Superoxide dismutase in cancer: a review.
TL;DR: It is shown how diminished enzyme activities along with radical production may lead to many of the observed properties of cancer cells.
Journal ArticleDOI
Positive Control of a Regulon for Defenses against Oxidative Stress and Some Heat-Shock Proteins in Salmonella typhimurium
TL;DR: The oxyR regulatory network is a previously uncharacterized global regulatory system in enteric bacteria that is resistant to a variety of oxidizing agents and overexpresses at least five enzyme activities involved in defenses against oxidative damage.
Journal ArticleDOI
Free radicals and antioxidants in the year 2000. A historical look to the future.
TL;DR: If reactive oxygen species are intimately involved with the redox regulation of cell functions, as seems likely from current evidence, it may be easier to understand why attempts to change antioxidant balance in aging experiments have failed.
Journal ArticleDOI
Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria
TL;DR: Rat liver was homogenized in isotonic buffer, fractionated by differential centrifugation, and then subfractionated by equilibrium sedimentation in Nycodenz gradients to indicate that the cytosolic and the intermembrane space Cu,Zn-SODs are coded for by the same gene.
References
More filters
Journal ArticleDOI
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.
Journal ArticleDOI
The microestimation of succinate and the extinction coefficient of cytochrome c.
Journal ArticleDOI
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.
Journal ArticleDOI
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.
Journal ArticleDOI
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.