Jump to main content
Jump to site search

Volume 116, 2000
Previous Article Next Article

A scanning tunnelling study of immobilised cytochrome P450cam

Author affiliations

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.

Back to tab navigation

Publication details

The article was received on 18 Feb 2000 and first published on 05 Jun 2000


Article type: Paper
DOI: 10.1039/B001372M
Citation: Faraday Discuss., 2000,116, 15-22
  •   Request permissions

    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

Search articles by author

Spotlight

Advertisements