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Open AccessJournal ArticleDOI

Superoxide Dismutase AN ENZYMIC FUNCTION FOR ERYTHROCUPREIN (HEMOCUPREIN)

Joe M. McCord, +1 more
- 25 Nov 1969 - 
- Vol. 244, Iss: 22, pp 6049-6055
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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.
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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.

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Citations
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Evidence for increased lipid peroxidative damage and loss of superoxide dismutase activity as a mode of sublethal cryodamage to human sperm during cryopreservation.

TL;DR: It is concluded that cryopreservation does enhance lipid peroxidation in human sperm, as hypothesized, and that this enhancement is mediated at least in part by the loss of SOD activity occurring during the process.
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Periplasmic superoxide dismutase protects Salmonella from products of phagocyte NADPH-oxidase and nitric oxide synthase

TL;DR: Observations suggest that SOD protects periplasmic or inner membrane targets by diverting superoxide and limiting peroxynitrite formation, and they demonstrate the ability of the respiratory burst and nitric oxide synthase to synergistically kill microbial pathogens in vivo.
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Redox mechanisms in hepatic chronic wound healing and fibrogenesis

TL;DR: This information will serve as a basis of knowledge to introduce the role of ROS and other oxidative stress-related intermediates in contributing to essential events, such as the induction of cell death, the perpetuation of chronic inflammatory responses, fibrogenesis and much more, with a major focus on hepatic chronic wound healing and liver fibrogensesis.
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Synthetic fluorescent probes for studying copper in biological systems

TL;DR: The need for combined chemical and biological evaluation of these reagents, as well as the value of complementing probe data with other techniques for characterizing the different pools of metal ions in biological systems, are emphasized.
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ALS Genetics, Mechanisms, and Therapeutics: Where Are We Now?

TL;DR: The genetic basis of ALS is reviewed, highlighting factors that have contributed to the elusiveness of genetic heritability and future directions for research that may lead to effective treatment strategies outlined.
References
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Journal ArticleDOI

The Reduction of Cytochrome c by Milk Xanthine Oxidase

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 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.
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