Experimental Documentation of the Structural Consequences of Hydrogen-Bonding Interactions to the Proximal Cysteine of a Cytochrome P450

Authors

Piotr J. Mak, Marquette UniversityFollow
Yuting Yang, University of Michigan and VA Medical Center
Sangchoul Im, University of Michigan and VA Medical CenterFollow
Lucy A. Waskell, University of Michigan and VA Medical CenterFollow
James R. Kincaid, Marquette UniversityFollow

Document Type

Article

Publication Date

10-2012

Source Publication

Angewandte Chemie International Edition

Source ISSN

1433-7851

Abstract

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.

Comments

Accepted version. Angewandte Chemie International Edition, Vol. 51, No. 41 (October 2012): 10403–10407. DOI. © 2012 Wiley-VCH Verlag. Used with permission.

Recommended Citation

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.
https://epublications.marquette.edu/chem_fac/402