- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1021/bi00071a023
-
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- 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
- Copyright date:
- 1993
Journal article
Reversible electrochemistry of fumarate reductase immobilized on an electrode surface. Direct voltammetric observations of redox centers and their participation in rapid catalytic electron transport.
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