The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Common and Uncommon Cytochrome P450 Reactions Related to Metabolism and Chemical Toxicity
Abstract
Cytochrome P450 (P450) enzymes catalyze a variety of reactions and convert chemicals to potentially reactive products as well as make compounds less toxic. Most of the P450 reactions are oxidations. The majority of these can be rationalized in the context of an FeO(3+) intermediate and odd electron abstraction/rebound mechanisms; however, other iron-oxygen complexes are possible and alternate chemistries can be considered. Another issue regarding P450-catalyzed reactions is the delineation of rate-limiting steps in the catalytic cycle and the contribution to reaction selectivity. In addition to the rather classical oxidations, P450s also catalyze less generally discussed reactions including reduction, desaturation, ester cleavage, ring expansion, ring formation, aldehyde scission, dehydration, ipso attack, one-electron oxidation, coupling reactions, rearrangement of fatty acid and prostaglandin hydroperoxides, and phospholipase activity. Most of these reactions are rationalized in the context of high-valent iron-oxygen intermediates and Fe(2+) reductions, but others are not and may involve acid-base catalysis. Some of these transformations are involved in the bioactivation and detoxication of xenobiotic chemicals.
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Cites
The Carbon Monoxide-binding Pigment of Liver Microsomes
Omura, T., & Sato, R. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)82244-3 · Cited by 11,781
Oxygen Activation by Cytochrome P-4501
White, R. E., & Coon, M. J. (1980) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.49.070180.001531 · Cited by 1,023
Mammalian Microsomal Cytochrome P450 Monooxygenase
Williams, P. A., Cosme, J., Sridhar, V., Johnson, E. F., & McRee, D. E. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80408-6 · Cited by 696
Cited by
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
Prodrugs: design and clinical applications
Rautio, J., Kumpulainen, H., Heimbach, T., Oliyai, R., Oh, D., Järvinen, T., & Savolainen, J. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2468 · Cited by 1,630
Lee, W. M. (2003) · New England Journal of Medicine · doi:10.1056/nejmra021844 · Cited by 1,594
P450 Enzymes: Their Structure, Reactivity, and Selectivity—Modeled by QM/MM Calculations
Shaik, S., Cohen, S., Wang, Y., Chen, H., Kumar, D., & Thiel, W. (2010) · Chemical Reviews · doi:10.1021/cr900121s · Cited by 1,083
Ochratoxin A: An overview on toxicity and carcinogenicity in animals and humans
Pfohl‐Leszkowicz, A., & Manderville, R. A. (2007) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200600137 · Cited by 1,017
Bacterial resistance to antibiotics: Enzymatic degradation and modification
WRIGHT, G. (2005) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2005.04.002 · Cited by 897
Cytochrome P450 systems—biological variations of electron transport chains
Hannemann, F., Bichet, A., Ewen, K. M., & Bernhardt, R. (2007) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2006.07.017 · Cited by 759
Bioisosteres of the Phenyl Ring: Recent Strategic Applications in Lead Optimization and Drug Design
Subbaiah, M. A. M., & Meanwell, N. A. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01215 · Cited by 710
Targeted Covalent Inhibitors for Drug Design
Baillie, T. A. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201601091 · Cited by 578
Insect CYP Genes and P450 Enzymes
Feyereisen, R. (2012) · Insect Molecular Biology and Biochemistry · doi:10.1016/b978-0-12-384747-8.10008-x · Cited by 566
Complex reactions catalyzed by cytochrome P450 enzymes
Isin, E. M., & Guengerich, F. P. (2007) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2006.07.003 · Cited by 448
Self-citationSchiffer, L., Barnard, L., Baranowski, E. S., Gilligan, L. C., Taylor, A. E., Arlt, W., Shackleton, C. H. L., & Storbeck, K.-H. (2019) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2019.105439 · Cited by 450
“with hydroxylation and CeC bond cleavage being relevant reactions in steroidogenesis [9,10].”
Enzymatic functionalization of carbon–hydrogen bonds
Lewis, J. C., Coelho, P. S., & Arnold, F. H. (2011) · Chem. Soc. Rev. · doi:10.1039/c0cs00067a · Cited by 386
Role of cytochrome P450s in the generation and metabolism of reactive oxygen species
Veith, A., & Moorthy, B. (2018) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2017.10.003 · Cited by 363
Drug Bioactivation Covalent Binding to Target Proteins and Toxicity Relevance
Zhou, S., Chan, E., Duan, W., Huang, M., & Chen, Y.-Z. (2005) · Drug Metabolism Reviews · doi:10.1081/dmr-200028812 · Cited by 274
Kang, J.-Y., Kim, S.-Y., Kim, D., Kim, D.-H., Shin, S.-M., Park, S.-H., Kim, K.-H., Jung, H.-C., Pan, J.-G., Joung, Y. H., et al. (2011) · AMB Express · doi:10.1186/2191-0855-1-1 · Cited by 256
Cigarette smoking: cancer risks, carcinogens, and mechanisms
Hecht, S. S. (2006) · Langenbeck's Archives of Surgery · doi:10.1007/s00423-006-0111-z · Cited by 256
Application of In Vitro Metabolism Activation in High-Throughput Screening
Ooka, M., Lynch, C., & Xia, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218182 · Cited by 49
Chen, S., Wu, Q., Li, X., Li, D., Mei, N., Ning, B., Puig, M., Ren, Z., Tolleson, W. H., & Guo, L. (2021) · Journal of Environmental Science and Health, Part C · doi:10.1080/26896583.2021.1880242 · Cited by 44
Zhao, B., Moody, S. C., Hider, R. C., Lei, L., Kelly, S. L., Waterman, M. R., & Lamb, D. C. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13078500 · Cited by 42
Defining the Role of Gut Bacteria in the Metabolism of Deleobuvir: In Vitro and In Vivo Studies
McCabe, M., Sane, R. S., Keith-Luzzi, M., Xu, J., King, I., Whitcher-Johnstone, A., Johnstone, N., Tweedie, D. J., & Li, Y. (2015) · Drug Metabolism and Disposition · doi:10.1124/dmd.115.064477 · Cited by 37
Metadata
- Authors
- Guengerich, F. P.
- Venue
- Chemical Research in Toxicology
- Publisher
- American Chemical Society (ACS)
- Published
- 2001-05-05
- Volume
- 14
- Issue
- 6
- Pages
- 611-650
- ISSN
- 0893-228X (ISSN-L)
- 1520-5010
- OpenAlex
- W2106195907
- Cited by
- 1,655
- References
- 3
- FWCI
- 25.87
- Type
- journal article
- Language
- en
- Open access
- closed
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