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The mechanism of reduction of single-site redox proteins by ascorbic acid.


ABSTRACT: The reduction of single-site haem and copper redox proteins by ascorbic acid was studied as a function of pH. Evidence is presented that indicates that the double-deprotonated ascorbate anion, ascorbate2-, is the reducing agent, and the pH-independent second-order rate constants for reduction by this species are given. Investigation of the temperature dependences of these rate constants have yielded the values of the activation parameters (delta H++ and delta S++) for reduction. These values, together with ligand-replacement studies, suggest that ascorbate2- acts as an outer-sphere reductant for these proteins. Reasons to account for the apparent inability of ascorbic acid to reduce the alkaline conformer of mammalian ferricytochrome c are suggested.

SUBMITTER: Al-Ayash AI 

PROVIDER: S-EPMC1186415 | biostudies-other | 1979 Feb

REPOSITORIES: biostudies-other

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