Ontology highlight
ABSTRACT:
SUBMITTER: Dey A
PROVIDER: S-EPMC2734335 | biostudies-literature | 2009 Jun
REPOSITORIES: biostudies-literature
Dey Abhishek A Jiang Yonging Y Ortiz de Montellano Paul P Hodgson Keith O KO Hedman Britt B Solomon Edward I EI
Journal of the American Chemical Society 20090601 22
Experimental covalencies of the Fe-S bond for the resting low-spin and substrate-bound high-spin active site of cytochrome P450 are reported. DFT calculations on the active site indicate that one H-bonding interaction from the protein backbone is needed to reproduce the experimental values. The H-bonding to the thiolate from the backbone decreases the anisotropic pi covalency of the Fe-S bond lowering the barrier of free rotation of the exchangeable axial ligand, which is important for reactivit ...[more]