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
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Structure and function of cytochromes P450: a comparative analysis of three crystal structures
Hasemann, C. A., Kurumbail, R. G., Boddupalli, S. S., Peterson, J. A., & Deisenhofer, J. (1995) · Structure · doi:10.1016/s0969-2126(01)00134-4 · Cited by 692
Structure of a cytochrome P450-redox partner electron-transfer complex
Sevrioukova, I. F., Li, H., Zhang, H., Peterson, J. A., & Poulos, T. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.1863 · Cited by 501
Dietrich, J. A., Yoshikuni, Y., Fisher, K. J., Woolard, F. X., Ockey, D., McPhee, D. J., Renninger, N. S., Chang, M. C. Y., Baker, D., & Keasling, J. D. (2009) · ACS Chemical Biology · doi:10.1021/cb900006h · Cited by 186
Cited by
Heme Enzyme Structure and Function
Poulos, T. L. (2014) · Chemical Reviews · doi:10.1021/cr400415k · Cited by 1,443
Olefin Cyclopropanation via Carbene Transfer Catalyzed by Engineered Cytochrome P450 Enzymes
Coelho, P. S., Brustad, E. M., Kannan, A., & Arnold, F. H. (2013) · Science · doi:10.1126/science.1231434 · Cited by 832
Yang, Y., & Arnold, F. H. (2021) · Accounts of Chemical Research · doi:10.1021/acs.accounts.0c00591 · Cited by 357
Cytochrome P450 Monooxygenases in Biotechnology and Synthetic Biology
Urlacher, V. B., & Girhard, M. (2019) · Trends in Biotechnology · doi:10.1016/j.tibtech.2019.01.001 · Cited by 355
Metadata
- Authors
- Whitehouse, C. J. C., Bell, S. G., & Wong, L.-L.
- Venue
- Chem. Soc. Rev.
- Publisher
- Royal Society of Chemistry (RSC)
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
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.