Ethylbenzene hydroxylation by cytochrome P450cam.
The metabolism of ethylbenzene by cytochrome P450cam was analyzed by experimental and theoretical methods. The present experiments indicate that ethylbenzene is hydroxylated almost exclusively at the secondary ethyl carbon with about a 2:1 ratio of R:S product. Several molecular dynamics trajectories were performed with different starting conformations of ethylbenzene in the active site of P450cam. The stereochemistry of hydroxylation predicted from the molecular dynamics simulations was found to be in good agreement with the observed products.
Filipovic
D
D
Department of Biochemistry, University of Illinois, Urbana 61801.
Paulsen
M D
MD
Loida
P J
PJ
Sligar
S G
SG
Ornstein
R L
RL
D001555:Benzene Derivatives / Q000378:metabolism*; D001665:Binding Sites; D019475:Camphor 5-Monooxygenase; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000378:metabolism*; D006418:Heme / Q000032:analysis; D006900:Hydroxylation; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D008968:Molecular Conformation; D011485:Protein Binding; D011487:Protein Conformation; D016958:Pseudomonas putida / Q000201:enzymology; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D014961:X-Ray Diffraction
D001555:Benzene Derivatives; D011994:Recombinant Proteins; D006418:Heme; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D019475:Camphor 5-Monooxygenase; C004912:ethylbenzene