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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Oxidative stress and antioxidant defenses after prolonged starvation in Dentex dentex liver.
TL;DR: The results show that prolonged starvation leads to a pro-oxidant situation and oxidative stress despite activation of antioxidant defense mechanisms, and that inhibition of G6PDH activity might be responsible for this failure in cellular antioxidant defenses.
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Manganese, superoxide dismutase, and oxygen tolerance in some lactic acid bacteria.
F S Archibald,I Fridovich +1 more
TL;DR: The results support the conclusion that a high internal level of Mn(II) provides these organisms with an important defence against endogenous O2-.
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Intracellular proteolytic systems may function as secondary antioxidant defenses: An hypothesis
TL;DR: Evidence is presented to suggest that proteolytic systems (of proteinases, proteases, and peptidases) may function to prevent the formation or accumulation of oxidatively damaged protein aggregates and to prevent a wide variety of potentially toxic consequences.
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Adaptations against heme toxicity in blood-feeding arthropods
Aurélio V. Graça-Souza,Clarissa M. Maya-Monteiro,Gabriela O. Paiva-Silva,Glória R.C. Braz,Marcia Cristina Paes,Marcos Henrique Ferreira Sorgine,Marcus F. Oliveira,Pedro L. Oliveira +7 more
TL;DR: In this paper, the authors review mechanisms by which heme can exert biological damage, together with a wide spectrum of adaptations developed by blood-feeding insects and ticks to counteract its deleterious effects.
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Glutathione, stress responses, and redox signaling in lung inflammation.
TL;DR: The current knowledge on the role of GSH in redox signaling, particularly the regulation of transcription factors and downstream signaling in lung inflammation is featured.
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.