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1576409 
Journal Article 
P450(BM3) (CYP102A1): connecting the dots 
Whitehouse, CJC; Bell, SG; Wong, L 
2012 
Yes 
Chemical Society Reviews
ISSN: 0306-0012
EISSN: 1460-4744 
41 
3 
1218-1260 
22008827 
WOS:000299176700015 
P450(BM3) (CYP102A1), a fatty acid hydroxylase from
Bacillus megaterium, has been extensively studied over a period of almost forty years. The enzyme
has been redesigned to catalyse the oxidation of non-natural substrates as diverse as
pharmaceuticals, terpenes and gaseous alkanes using a variety of engineering strategies. Crystal
structures have provided a basis for several of the catalytic effects brought about by
mutagenesis, while changes to reduction potentials, inter-domain electron transfer rates and
catalytic parameters have yielded functional insights. Areas of active research interest include
drug metabolite production, the development of process-scale techniques, unravelling general
mechanistic aspects of P450 chemistry, methane oxidation, and improving selectivity control to
allow the synthesis of fine chemicals. This review draws together the disparate research themes
and places them in a historical context with the aim of creating a resource that can be used as a
gateway to the field.