A role for the strained phenylalanine ring rotation induced by substrate binding to cytochrome CYP102A1.
X-ray crystal structures of CYP102A1 (P450BM-3) have shown that PHE87 rotates upon substrate binding and is in contact with the heme cofactor. Analysis of substrate binding data combined with DFT calculations suggest that the ring is rotated into an unfavorable interaction with the heme and this could drive active site rearrangement.
Haines
Donovan C
DC
Department of Chemistry, University of Texas at Dallas, Box 830688, BE26, Richardson, TX 75083-0688, USA. haines@utdallas.edu
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites / Q000235:genetics; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D009251:NADPH-Ferrihemoprotein Reductase; D010649:Phenylalanine / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding / Q000235:genetics; D013379:Substrate Specificity / Q000235:genetics
D001426:Bacterial Proteins; D010649:Phenylalanine; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases