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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An improved spectrophotometric assay for superoxide dismutase based on epinephrine autoxidation.
Ming Sun,Seymour Zigman +1 more
TL;DR: The enzyme assay based on adrenochrome absorption at480 nm has been improved by measuring the absorption change at 320 nm, which was found to be 6 to 10 times more sensitive and more consistent than that measured at 480 nm.
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A mutation in succinate dehydrogenase cytochrome b causes oxidative stress and ageing in nematodes
Naoaki Ishii,Michihiko Fujii,Philip S. Hartman,Michio Tsuda,Kayo Yasuda,Nanami Senoo-Matsuda,Sumino Yanase,Dai Ayusawa,Kenshi Suzuki +8 more
TL;DR: The results indicate that mev-1 governs the rate of ageing by modulating the cellular response to oxidative stress, which may cause an indirect increase in superoxide levels, which in turn leads to oxygen hypersensitivity and premature ageing.
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A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage.
TL;DR: It is demonstrated that Cu,Zn-SOD1 in the mitochondria appears important for reactive oxygen physiology and may have critical implications for SOD1 mutations linked to the fatal neurodegenerative disorder, amyotrophic lateral sclerosis.
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Biochemical reactivity of melatonin with reactive oxygen and nitrogen species: a review of the evidence
TL;DR: In vitro melatonin acts as a direct free radical scavenger with the ability to detoxify both reactive oxygen and reactive nitrogen species; in vivo, it is an effective pharmacological agent in reducing oxidative damage under conditions in which excessive free radical generation is believed to be involved.
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Evidence for enhanced vascular superoxide anion production in nitrate tolerance. A novel mechanism underlying tolerance and cross-tolerance.
TL;DR: It is shown that continuous NTG treatment is associated with increased vascular .-O2-production and consequent inhibition of NO and mediated vasorelaxation produced by both exogenous and endogenous nitrovasodilators.
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.