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Biological Diversity of Cytochrome P450 Redox Partner Systems

  • Kirsty J. McLean
  • Dominika Luciakova
  • James Belcher
  • Kang Lan Tee
  • Andrew W. MunroEmail author
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 851)

Abstract

Cytochrome P450 enzymes (P450s or CYPs) catalyze an enormous variety of oxidative reactions in organisms from all major domains of life. Their monooxygenase activity relies on the reductive scission of molecular oxygen (O2) bound to P450 heme iron, and thus on the delivery of two electrons to the heme iron at discrete points in the catalytic cycle. Early studies suggested that P450 redox partner machinery fell into only two major classes: either the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase, or bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. However, more recent studies, aided by genome sequence data, reveal a much more complex scenario. Several new types of P450 redox partner systems have now been characterized, including P450s naturally linked to their redox partners, or to a component protein of their P450 electron delivery system. Other P450s have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis. Further P450s are fused to non-redox partner enzymes and can catalyse consecutive reactions in a common pathway. This chapter describes the biochemistry and the enormous natural diversity of P450 redox systems, including descriptions of novel P450s fused to non-redox partner proteins.

Keywords

Cytochrome P450 Compound I P450 redox systems P450 oxidoreductase P450 BM3 P450-flavodoxin fusion protein P450-ferredoxin fusion protein 

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Copyright information

© Springer International Publishing Switzerland 2015

Authors and Affiliations

  • Kirsty J. McLean
    • 1
  • Dominika Luciakova
    • 1
  • James Belcher
    • 1
  • Kang Lan Tee
    • 1
  • Andrew W. Munro
    • 1
    Email author
  1. 1.Manchester Institute of BiotechnologyThe University of ManchesterManchesterUK

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