The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Olefin Cyclopropanation via Carbene Transfer Catalyzed by Engineered Cytochrome P450 Enzymes
Abstract
Putting a C in Cytochrome: Cytochrome P450 enzymes oxidize hydrocarbons using a highly reactive iron oxo intermediate. Much research has focused on tuning the protein structure to broaden the range of hydrocarbons that can be functionalized. Coelho et al. (p. 307 , published online 20 December; see the Perspective by Narayan and Sherman ) substituted a carbene source for the oxygen to make a P450 mutant a cyclopropanation catalyst whereby a carbon fragment is transferred in place of oxygen. Though carbene activation by iron is chemically analogous to the native oxygen activation pathway, the overall reaction is completely different from any known enzymatic transformation.
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Enzyme promiscuity: evolutionary and mechanistic aspects
Khersonsky, O., Roodveldt, C., & Tawfik, D. S. (2006) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2006.08.011 · Cited by 641
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Opportunities for merging chemical and biological synthesis
Wallace, S., & Balskus, E. P. (2014) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2014.03.006 · Cited by 86
“In their first report [39••], Arnold and co-workers hypothesized that cytochrome P450 enzymes, which catalyze a variety of reactions involving oxene transfer, might also be capable of generating and promoting transfer of carbene intermediates in the presence of suitable reagents (Figure 3A).”
Metadata
- Authors
- Coelho, P. S., Brustad, E. M., Kannan, A., & Arnold, F. H.
- Venue
- Science
- Published
- 2013-01-18
- Volume
- 339
- Issue
- 6117
- Pages
- 307-310
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2078531329
- Cited by
- 832
- References
- 1
- FWCI
- 20.27
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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