Substrate binding induces structural changes in cytochrome P450cam
The binding of (+)‐camphor to cytochrome P450cam (P450cam) expels a cluster of waters at the active site, raising the redox potential of the haem to an extent that allows reduction by the electron‐transfer system. This binding was reported to involve no significant structural changes in the protein. Here, two ferric P450cam structures partially complexed with (+)‐camphor were determined by X‐ray crystallography at 1.30–1.35 Å resolution, revealing the structures of the substrate‐free and substrate‐bound forms. (+)‐Camphor binding induces rotation of Thr101 to form a hydrogen bond that acts as a hydrogen donor to a peripheral haem propionate. This bonding contributes to the redox‐potential change.
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