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A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo

Coelho, Pedro S. and Wang, Z. Jane and Ener, Maraia E. and Baril, Stefanie A. and Kannan, Arvind and Arnold, Frances H. and Brustad, Eric M. (2013) A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo. Nature Chemical Biology, 9 (8). pp. 485-487. ISSN 1552-4450. PMCID PMC3720782. doi:10.1038/nchembio.1278. https://resolver.caltech.edu/CaltechAUTHORS:20130830-095755657

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Abstract

Whole-cell catalysts for non-natural chemical reactions will open new routes to sustainable production of chemicals. We designed a cytochrome 'P411' with unique serine-heme ligation that catalyzes efficient and selective olefin cyclopropanation in intact Escherichia coli cells. The mutation C400S in cytochrome P450_(BM3) gives a signature ferrous CO Soret peak at 411 nm, abolishes monooxygenation activity, raises the resting-state FeIII-to-FeII reduction potential and substantially improves NAD(P)H-driven activity.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1038/nchembio.1278 DOIArticle
http://dx.doi.org/10.1038/nchembio0214-164dErrataCorrigendum
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3720782/PubMed CentralArticle
http://rdcu.be/cm3OPublisherFree ReadCube access
http://rdcu.be/cm3PPublisherFree ReadCube access -- errata
ORCID:
AuthorORCID
Arnold, Frances H.0000-0002-4027-364X
Brustad, Eric M.0000-0002-7031-5433
Additional Information:© 2013 Nature Publishing Group. Received 4 April 2013; accepted 17 May 2013; published online 23 June 2013. Corrected after print 19 December 2013. Corrected version published online 17 January 2014. This research is supported by the Gordon and Betty Moore Foundation through the Caltech Programmable Molecular Technology Initiative. E.M.B. was supported by US National Institutes of Health (NIH) postdoctoral award F32GM087102 and a generous startup fund from University of North Carolina–Chapel Hill (UNC). Z.J.W. was supported by NIH 1F32EB015846-01. M.E.E. was supported by NIH grant RO1-DK019038. We thank N. Peck for help with preparative-scale experiments. We thank the Redinbo laboratory at UNC for assistance with X-ray data collection. M.E.E. thanks J.D. Blakemore and J.R. Winkler for electrodes and helpful discussions. Author contributions: P.S.C., F.H.A. and E.M.B. conceived the project and wrote the paper; P.S.C., E.M.B. and Z.J.W. designed the experiments; E.M.B. and S.A.B. performed the crystallography; M.E.E. performed the redox titrations; P.S.C., Z.J.W. and A.K. performed the catalysis experiments; all authors discussed the results.
Errata:In the version of this article initially published, the Protein Data Bank codes for the P450 and P411 constructs were inadvertently switched. Accession code 4H23 actually corresponds to the P411 structure, and 4H24 corresponds to the P450 structure. The error has been corrected in the HTML and PDF versions of the article.
Funders:
Funding AgencyGrant Number
Gordon and Betty Moore FoundationUNSPECIFIED
Caltech Programmable Molecular Technology InitiativeUNSPECIFIED
NIH Predocotral FellowshipF32GM087102
University of North Carolina Chapel HillUNSPECIFIED
NIH Postdoctoral Fellowship1F32EB015846-01
NIHRO1-DK019038
Issue or Number:8
PubMed Central ID:PMC3720782
DOI:10.1038/nchembio.1278
Record Number:CaltechAUTHORS:20130830-095755657
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20130830-095755657
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:41023
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:30 Aug 2013 17:54
Last Modified:10 Nov 2021 04:25

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