Substrate binding induces structural changes in cytochrome P450cam

X-ray structures of ferric cytochrome P450cam partially complexed with the substrate (+)-camphor to two different extents were determined at 1.30–1.35 Å resolution, revealing the protein structures of the substrate-free and substrate-bound forms. 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