A role for the strained phenylalanine ring rotation induced by substrate binding to cytochrome CYP102A1.

Abstract excerpt

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.

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Bacterial Proteins
• Share to Binding Sites
• Share to Cytochrome P-450 Enzyme System