Surface-modified mutants of cytochrome P450(cam) : Enzymatic properties and electrochemistry

Research output: Journal Publications and ReviewsRGC 21 - Publication in refereed journalpeer-review

71 Scopus Citations
View graph of relations

Author(s)

Detail(s)

Original languageEnglish
Pages (from-to)342-346
Journal / PublicationFEBS Letters
Volume451
Issue number3
Publication statusPublished - 28 May 1999
Externally publishedYes

Abstract

We report the electrochemistry of genetic variants of the haem monooxygenase cytochrome P450(cam). A surface cysteine-free mutant (abbreviated as SCF) was prepared in which the five surface cysteine residues Cys-58, Cys-85, Cys-136, Cys-148 and Cys-334 were changed to alanines. Four single surface cysteine mutants with an additional mutation, R72C, R112C, K344C or R364C, were also prepared. The haem spin-state equilibria, NADH turnover rates and camphor-hydroxylation properties, as well as the electrochemistry of these mutants are reported. The coupling of a redox-active label, N-ferrocenylmaleimide, to the single surface cysteine mutant SCF-K344C, and the electrochemistry of this modified mutant are also described. Copyright (C) 1999 Federation of European Biochemical Societies.

Research Area(s)

  • Electrochemistry, Mutagenesis, P450(cam), Redox-active label, Surface cysteine

Citation Format(s)

Surface-modified mutants of cytochrome P450(cam): Enzymatic properties and electrochemistry. / Lo, Kenneth Kam-Wing; Wong, Luet-Lok; Hill, H. Allen O.
In: FEBS Letters, Vol. 451, No. 3, 28.05.1999, p. 342-346.

Research output: Journal Publications and ReviewsRGC 21 - Publication in refereed journalpeer-review