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Cited by 669

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

P450BM3(CYP102A1): connecting the dots

Whitehouse, Christopher J. C., Bell, Stephen G., Wong, Luet-Lok·2012·Chem. Soc. Rev.

Abstract

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.

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Crossref · 10.1039/c1cs15192d

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Metadata

Authors
Whitehouse, C. J. C., Bell, S. G., & Wong, L.-L.
Venue
Chem. Soc. Rev.
Published
2012
Volume
41
Issue
3
Pages
1218-1260
ISSN
  • 0306-0012 (ISSN-L)
  • 1460-4744
OpenAlex
W2108738397
Cited by
669
References
3
FWCI
0.45
Type
journal article
Language
en
Open access
closed

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.