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Journal ArticleDOI

Superoxide radical from xanthine oxidase acting upon lumazine.

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TLDR
The results support the view that electron egress from heavily reduced xanthine oxidase occurs by divalent transfers, while that from the partially reduced enzyme is by univalent transfers.
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This article is published in Journal of Free Radicals in Biology & Medicine.The article was published on 1985-01-01. It has received 37 citations till now. The article focuses on the topics: Xanthine oxidation & Xanthine oxidase.

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Initiation of lipid peroxidation in biological systems

TL;DR: The data reviewed indicate that lipid peroxidation is initiated by nonenzymatic and enzymatic reactions, and the generation of a superoxide radical, or its protonated molecule, the perhydroxyl radical could directly initiate PUFA per oxidation.
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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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The role of iron in the initiation of lipid peroxidation.

TL;DR: Evidence is presented that lipid peroxidation requires both Fe3+ and Fe2+, perhaps with oxygen to form a Fe3-dioxygen-Fe2+ complex.
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Reaction of superoxide and nitric oxide with peroxynitrite. Implications for peroxynitrite-mediated oxidation reactions in vivo.

TL;DR: It is concluded that the oxidative processes initiated by the free radical intermediates formed from the decomposition of peroxynitrite are inhibited by excess production of ⋅NO or O⨪2, whereas oxidative pathways involving a direct reaction with each other are not altered.
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Redox cycling of iron and lipid peroxidation

TL;DR: Mechanisms of iron-catalyzed lipid peroxidation depend on the presence or absence of preformed lipid hydroperoxides (LOOH), with optimum activity occurring as the Fe2+/Fe3+ ratio approaches unity.
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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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.
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A new purification procedure for bovine milk xanthine oxidase: effect of proteolysis on the subunit structure.

TL;DR: Pancreatinized enzyme has a greater mobility than unproteolyzed enzyme on polyacrylamide gels and is in good agreement with the minimum molecular weight of 157,000 calculated from dry weight determination and flavin analysis.
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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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