Cytochromes P450: History, Classes, Catalytic Mechanism, and Industrial Application

D. Cook, J. Finnigan, K. Cook, Gary Black, S. J. Charnock

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

19 Citations (Scopus)

Abstract

Cytochromes P450, a family of heme-containing monooxygenases that catalyze a diverse range of oxidative reactions, are so-called due to their maximum absorbance at 450 nm, ie, “Pigment–450 nm,” when bound to carbon monoxide. They have appeal both academically and commercially due to their high degree of regio- and stereoselectivity, for example, in the area of active pharmaceutical ingredient synthesis. Despite this potential, they often exhibit poor stability, low turnover numbers and typically require electron transport protein(s) for catalysis. P450 systems exist in a variety of functional domain architectures, organized into 10 classes. P450s are also divided into families, each of which is based solely on amino acid sequence homology. Their catalytic mechanism employs a very complex, multistep catalytic cycle involving a range of transient intermediates. Mutagenesis is a powerful tool for the development of improved biocatalysts and has been used extensively with the archetypal Class VIII P450, BM3, from Bacillus megaterium, but with the increasing scale of genomic sequencing, a huge resource is now available for the discovery of novel P450s.
Original languageEnglish
Title of host publicationInsights into Enzyme Mechanisms and Functions from Experimental and Computational Methods
EditorsChristo Christov
Place of PublicationLondon
PublisherElsevier
Pages105-126
Volume105
ISBN (Print)978-0-12-804825-2
DOIs
Publication statusE-pub ahead of print - 9 Aug 2016

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