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Substrate binding induces structural changes in cytochrome P450cam.
- Source :
- Acta Crystallographica: Section F (Wiley-Blackwell); Feb2009, Vol. 65 Issue 2, p80-83, 4p
- Publication Year :
- 2009
-
Abstract
- 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 65
- Issue :
- 2
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section F (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 110812101
- Full Text :
- https://doi.org/10.1107/S1744309108044114