A distal histidine mutant (H52Q) of yeast cytochrome c peroxidase catalyzes the oxidation of H(2)O(2) instead of its reduction.

Journal article

A H52Q variant of yeast cytochrome c peroxidase (CcP), in which the distal histidine is replaced by glutamine, catalyzes oxidation of H(2)O(2) instead of reduction. This redirection of catalytic action is detected by protein film voltammetry. In the presence of H(2)O(2), wild-type CcP, adsorbed on a graphite electrode, shows a strong catalytic reduction wave commencing at about 0.8V (pH 5.4); by contrast, H52Q does not exhibit this activity but instead shows a catalytic oxidation current at p...

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Authors: Bateman, L; Léger, C; Goodin, D; Armstrong, F

• Publication status: Published
• Journal: Journal of the American Chemical Society
• Volume: 123
• Issue: 38
• Pages: 9260-9263
• Publication date: 2001-09-01
• DOI: 10.1021/ja0158612
• EISSN: 1520-5126
• ISSN: 0002-7863
• Language: English
• Keywords: Binding Sites; Histidine; Saccharomyces cerevisiae; Oxidation-Reduction; Electrochemistry; Models, Molecular; Mutation; Cytochrome-c Peroxidase; Hydrogen Peroxide