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Cytochrome P450 cam : crystallography, oxygen activation, and electron transfer 1
Author(s) -
Poulos Thomas L.,
Raag Reetta
Publication year - 1992
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.6.2.1537455
Subject(s) - pseudomonas putida , cytochrome , chemistry , electron transfer , oxygen , cytochrome p450 , electron transport chain , crystallography , stereochemistry , biochemistry , photochemistry , enzyme , organic chemistry
Several crystal structures of various substrate and inhibited complexes of the camphor monoxygenase, cytochrome P450 cam from Pseudomonas putida , are now available. These structures, together with mutagenesis, biochemical, and biophysical studies, have allowed for a detailed penetration into the problem of how P450s activate molecular oxygen, control stereoselectivity, and transfer electrons. This review will provide a summary of the crystallographic work in light of what these structures have taught us about P450 function.—Poulos, T. L.; Raag, R. Cytochrome P450 cam : crystallography, oxygen activation, and electron transfer. FASEB J. 6: 674‐679; 1992.
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