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Simultaneous voltammetric comparisons of reduction potentials, reactivities, and stabilities of the high-potential catalytic states of wild-type and distal-pocket mutant (W51F) yeast cytochrome c peroxidase

Abstract:

Protein film voltammetry has been used to measure changes in the catalytic redox energetics of cytochrome c peroxidase produced by a single mutation in the distal pocket. Wild-type (WT) cytochrome c peroxidase adsorbs at a pyrolytic graphite edge electrode from ice-cold dilute succinate buffer, pH 5.4, to give an electroactive film showing a reversible and narrow (two- electron) signal, reduction potential 754 mV, which converts completely to a catalytic wave at a similar potential when low l...

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Publication status:
Published

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Publisher copy:
10.1021/ja980197j

Authors


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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
Journal:
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY More from this journal
Volume:
120
Issue:
25
Pages:
6270-6276
Publication date:
1998-07-01
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
Language:
English
Pubs id:
pubs:36558
UUID:
uuid:0a34edda-8b73-4315-9727-3347b3ac0c61
Local pid:
pubs:36558
Source identifiers:
36558
Deposit date:
2013-11-16

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