Experimental documentation of the structural consequences of hydrogen-bonding interactions to the proximal cysteine of a cytochrome P450. Angew Chem Int Ed Engl 2012 Oct 08;51(41):10403-7
Date
09/13/2012Pubmed ID
22968976Pubmed Central ID
PMC3517159DOI
10.1002/anie.201205912Scopus ID
2-s2.0-84867071362 (requires institutional sign-in at Scopus site) 29 CitationsAbstract
Resonance Raman spectroscopy is used to document, for the first time, a 6 cm−1 decrease of the Fe-S stretch by introducing an H-bond donor into the proximal pocket of a cytochrome P450, which interacts with the key cysteine thiolate axial ligand. The anticipated trans-effect on bound exogenous ligands is also confirmed and evidence is obtained supporting intimate interaction of the new histidyl-imidazole fragment with the heme periphery.
Author List
Mak PJ, Yang Y, Im S, Waskell LA, Kincaid JRAuthor
James Kincaid PhD Department Chair and Professor, Biophysical Chemistry in the Chemistry department at Marquette UniversityMESH terms used to index this publication - Major topics in bold
CysteineCytochrome P-450 Enzyme System
Hydrogen Bonding
Iron
Oxidation-Reduction
Spectrum Analysis, Raman
Sulfur
