A scanning tunnelling study of immobilised cytochrome P450cam

Research output: Journal Publications and Reviews (RGC: 21, 22, 62)21_Publication in refereed journalpeer-review

42 Scopus Citations
View graph of relations

Author(s)

  • Jason J. Davis
  • Dejana Djuricic
  • Emma N. K. Wallace
  • Luet-Lok Wong
  • H. Allen O. Hill

Detail(s)

Original languageEnglish
Pages (from-to)15-22
Journal / PublicationFaraday Discussions
Volume116
Publication statusPublished - 2000
Externally publishedYes

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.

Citation Format(s)

A scanning tunnelling study of immobilised cytochrome P450cam. / Davis, Jason J.; Djuricic, Dejana; Lo, Kenneth K. W.; Wallace, Emma N. K.; Wong, Luet-Lok; Hill, H. Allen O.

In: Faraday Discussions, Vol. 116, 2000, p. 15-22.

Research output: Journal Publications and Reviews (RGC: 21, 22, 62)21_Publication in refereed journalpeer-review