Volume 116, 2000

A scanning tunnelling study of immobilised cytochrome P450cam

Abstract

A site-specifically engineered surface cysteine residue, located in a region where the haem moiety is closest to the surface, is used to anchor cytochrome P450cam enzyme molecules covalently to a gold electrode. More reproducibly ordered adsorption, at high coverage, occurs with this K344C mutant than with the wild-type enzyme. The subsequently formed close-packed monolayer arrays have been probed by scanning tunnelling microscopy under ambient conditions and under aqueous (buffered) solution at high resolution. Initial indications suggest that the immobilised enzyme is both electrochemically addressable and catalytically active.

Article information

Article type
Paper
Submitted
18 Feb 2000
First published
05 Jun 2000

Faraday Discuss., 2000,116, 15-22

A scanning tunnelling study of immobilised cytochrome P450cam

J. J. Davis, D. Djuricic, K. K. W. Lo, E. N. K. Wallace, L. Wong and H. A. O. Hill, Faraday Discuss., 2000, 116, 15 DOI: 10.1039/B001372M

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements