Experimental Documentation of the Structural Consequences of Hydrogen-Bonding Interactions to the Proximal Cysteine of a Cytochrome P450
Angewandte Chemie International Edition
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.
Mak, Piotr J.; Yang, Yuting; Im, Sangchoul; Waskell, Lucy A.; and Kincaid, James R., "Experimental Documentation of the Structural Consequences of Hydrogen-Bonding Interactions to the Proximal Cysteine of a Cytochrome P450" (2012). Chemistry Faculty Research and Publications. 402.
Accepted version. Angewandte Chemie International Edition, Vol. 51, No. 41 (October 2012): 10403–10407. DOI. © 2012 Wiley-VCH Verlag. Used with permission.