Published August 25, 2004
| Supplemental Material
Journal Article
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Reduction of Dioxygen Catalyzed by Pyrene-Wired Heme Domain Cytochrome P450 BM3 Electrodes
Abstract
We have electronically wired the cytochrome P450 BM3 heme domain to a graphite electrode with the use of a pyrene-terminated tether. AFM images clearly reveal that pyrene-wired enzyme molecules are adsorbed to the electrode surface. The enzyme-electrode system undergoes rapid and reversible electron transfer, displaying a standard rate constant higher than that of any other P450-electrode system. We also show that the graphite-pyrene-BM3 system catalyzes the four-electron reduction of dioxygen to water.
Additional Information
© 2004 American Chemical Society. Received June 7, 2004. Publication Date (Web): August 3, 2004. We thank J. S. Magyar and J. R. Winkler (Caltech), T. L. Poulos (U.C. Irvine), and E. M. Spain (Occidental College) for helpful discussions; C. P. Collier (Caltech) for assistance with the AFM; NSF (H.B.G.), NSERC (Canada) (A.K.U.), and David and Lucile Packard Foundation (M.G.H.) for research support.Attached Files
Supplemental Material - ja0466560si20040708_023328.pdf
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Additional details
- Eprint ID
- 76960
- Resolver ID
- CaltechAUTHORS:20170426-144912333
- NSF
- Natural Sciences and Engineering Research Council of Canada (NSERC)
- David and Lucile Packard Foundation
- Created
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2017-04-26Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field