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Experimental Documentation of the Structural Consequences of Hydrogen‐Bonding Interactions to the Proximal Cysteine of a Cytochrome P450
Author(s) -
Mak Piotr J.,
Yang Yuting,
Im Sangchoul,
Waskell Lucy A.,
Kincaid James R.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201205912
Subject(s) - chemistry , heme , hydroxylation , cysteine , ferric , ligand (biochemistry) , stereochemistry , photochemistry , cytochrome p450 , resonance raman spectroscopy , redox , cytochrome , substrate (aquarium) , active site , reactivity (psychology) , hemeprotein , oxidizing agent , enzyme , raman spectroscopy , biochemistry , organic chemistry , receptor , medicine , physics , oceanography , alternative medicine , pathology , optics , geology
Reactivity control : Resonance Raman spectroscopy is used to document, for the first time, a 6 cm −1 decrease of the FeS stretch by introducing an H‐bond donor into the proximal pocket of a cytochrome P450, which interacts with the cysteine thiolate axial ligand (see picture). The anticipated trans ‐effect on bound exogenous ligands is also confirmed.