P450BM3: the very model of a modern flavocytochrome

A W Munro, D G Leys, K J McLean, K R Marshall, T W B Ost, S Daff, C S Miles, S K Chapman, D A Lysek, C C Moser, C C Page, P L Dutton

Research output: Contribution to journalLiterature reviewpeer-review

Abstract

Flavocytochrome P450 BM3 is a bacterial P450 system in which a fatty acid hydroxylase P450 is fused to a mammalian-like diflavin NADPH-P450 reductase in a single polypeptide. The enzyme is soluble (unlike mammalian P450 redox systems) and its fusion arrangement affords it the highest catalytic activity of any P450 mono-oxygenase. This article discusses the fundamental properties of P450 BM3 and how progress with this model P450 has affected our comprehension of P450 systems in general.

Original languageEnglish
Pages (from-to)250-257
Number of pages8
JournalTrends in biochemical sciences
Volume27
Issue number5
Publication statusPublished - May 2002

Keywords

  • ELECTRON-TRANSFER
  • BACILLUS-MEGATERIUM
  • CYTOCHROME P450
  • CATALYTIC CYCLE
  • DOMAIN MOVEMENT
  • P-450 BM3
  • SUBSTRATE
  • BINDING
  • REDUCTASE
  • PROTEIN

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