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Unusual Cytochrome P450 Enzymes and Reactions
Open accessAbstract
Cytochrome P450 enzymes primarily catalyze mixed-function oxidation reactions, plus some reductions and rearrangements of oxygenated species, e.g. prostaglandins. Most of these reactions can be rationalized in a paradigm involving Compound I, a high-valent iron-oxygen complex (FeO(3+)), to explain seemingly unusual reactions, including ring couplings, ring expansion and contraction, and fusion of substrates. Most P450s interact with flavoenzymes or iron-sulfur proteins to receive electrons from NAD(P)H. In some cases, P450s are fused to protein partners. Other P450s catalyze non-redox isomerization reactions. A number of permutations on the P450 theme reveal the diversity of cytochrome P450 form and function.
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Structure and chemistry of cytochrome p450
Denisov, I. G., Makris, T. M., Sligar, S. G., & Schlichting, I. (2005) · Chemical Reviews · doi:10.1021/cr0307143 · Cited by 2,106
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Deshmukh, R., Khardenavis, A. A., & Purohit, H. J. (2016) · Indian Journal of Microbiology · doi:10.1007/s12088-016-0584-6 · Cited by 435
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
Machine learning for functional protein design
Notin, P., Rollins, N., Gal, Y., Sander, C., & Marks, D. (2024) · Nature Biotechnology · doi:10.1038/s41587-024-02127-0 · Cited by 270
Andrés, C. M. C., Pérez de la Lastra, J. M., Juan, C. A., Plou, F. J., & Pérez-Lebeña, E. (2022) · Stresses · doi:10.3390/stresses2030019 · Cited by 218
Metadata
- Authors
- Guengerich, F. P., & Munro, A. W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2013-06
- Volume
- 288
- Issue
- 24
- Pages
- 17065-17073
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2047259762
- Cited by
- 346
- References
- 1
- FWCI
- 14.30
- Type
- journal article
- Language
- en
- Open access
- hybrid
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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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