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Reversible electrochemistry of fumarate reductase immobilized on an electrode surface. Direct voltammetric observations of redox centers and their participation in rapid catalytic electron transport.

Abstract:

Fumarate reductase (Escherichia coli) can be immobilized in an extremely electroactive state at an electrode, with retention of native catalytic properties. The membrane-extrinsic FrdAB component adsorbs to monolayer coverage at edge-oriented pyrolytic graphite and catalyzes reduction of fumarate or oxidation of succinate, depending upon the electrode potential. In the absence of substrates, reversible redox transformations of centers in the enzyme are observed by cyclic voltammetry. The majo...

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Publication status:
Published

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Publisher copy:
10.1021/bi00071a023

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
Journal:
Biochemistry
Volume:
32
Issue:
20
Pages:
5455-5465
Publication date:
1993-05-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:2bb753d2-d235-412d-a700-5e6b7389705b
Source identifiers:
46006
Local pid:
pubs:46006

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