Cytochrome P450cam: crystallography, oxygen activation, and electron transfer.
Several crystal structures of various substrate and inhibited complexes of the camphor monoxygenase, cytochrome P450cam 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
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Center for Advanced Research in Biotechnology, Maryland Biotechnology Institute, Rockville 20850.
Raag
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D000595:Amino Acid Sequence; D001665:Binding Sites; D019475:Camphor 5-Monooxygenase; D003461:Crystallography; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000378:metabolism; D004579:Electron Transport; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D016958:Pseudomonas putida / Q000201:enzymology*
D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D019475:Camphor 5-Monooxygenase