Biodiversity of cytochrome P450 redox systems

Biochem Soc Trans. 2005 Aug;33(Pt 4):796-801. doi: 10.1042/BST0330796.

Abstract

P450s (cytochrome P450 mono-oxygenases) are a superfamily of haem-containing mono-oxygenase enzymes that participate in a wide range of biochemical pathways in different organisms from all of the domains of life. To facilitate their activity, P450s require sequential delivery of two electrons passed from one or more redox partner enzymes. Although the P450 enzymes themselves show remarkable similarity in overall structure, it is increasingly apparent that there is enormous diversity in the redox partner systems that drive the P450 enzymes. This paper examines some of the recent advances in our understanding of the biodiversity of the P450 redox apparatus, with a particular emphasis on the redox systems in the pathogen Mycobacterium tuberculosis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Biodiversity
  • Cytochrome P-450 Enzyme System / chemistry*
  • Cytochrome P-450 Enzyme System / genetics
  • Cytochrome P-450 Enzyme System / metabolism*
  • Electron Transport
  • Ferredoxins / chemistry
  • Ferredoxins / metabolism
  • Flavin-Adenine Dinucleotide / metabolism
  • Flavodoxin / chemistry
  • Flavodoxin / metabolism
  • Genome, Bacterial
  • Models, Molecular
  • Mycobacterium tuberculosis / enzymology
  • Mycobacterium tuberculosis / genetics
  • NADP / metabolism
  • Oxidation-Reduction
  • Protein Conformation

Substances

  • Bacterial Proteins
  • Ferredoxins
  • Flavodoxin
  • Flavin-Adenine Dinucleotide
  • NADP
  • Cytochrome P-450 Enzyme System