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• W2053297714 startingPage "8310" @default.
• W2053297714 abstract "The reactions of the monodehydroascorbate radical (As.-) with various biological molecules were investigated by pulse radiolysis. As.- reacted with both fully reduced and semiquinone forms of hepatic NADH-cytochrome b5 reductase with second-order rate constants of 4.3 x 10(6) and 3.7 x 10(5) M-1 s-1, respectively, at pH 7.0. In contrast, no reaction of As.- with ferrous cytochrome b5 could be detected by pulse radiolysis, whereas the oxidation of cytochrome b5 by As.- was observed by ascorbate-ascorbate oxidase method. This suggests that the rate constant of As.- with the ferrous cytochrome b5 must be several orders in magnitude smaller than that of the disproportionation of As.-. On the other hand, As.- reduced Fe3+EDTA with a second-order rate constant of 4.0 x 10(6) M-1 s-1 but did not reduce ferric hemoproteins such as metmyoglobin, methemoglobin, and cytochrome b5 by either the pulse radiolysis or the ascorbate-ascorbate oxidase method." @default.
• W2053297714 created "2016-06-24" @default.
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• W2053297714 creator A5071361673 @default.
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• W2053297714 date "1991-08-27" @default.
• W2053297714 modified "2023-10-07" @default.
• W2053297714 title "Kinetic behavior of the monodehydroascorbate radical studied by pulse radiolysis" @default.
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• W2053297714 doi "https://doi.org/10.1021/bi00098a005" @default.
• W2053297714 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1883818" @default.
• W2053297714 hasPublicationYear "1991" @default.
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