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 8;51(41):10403-7. doi: 10.1002/anie.201205912. Epub 2012 Sep 11.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Cysteine / chemistry*
  • Cysteine / metabolism
  • Cytochrome P-450 Enzyme System / chemistry*
  • Cytochrome P-450 Enzyme System / metabolism
  • Hydrogen Bonding
  • Iron / chemistry
  • Oxidation-Reduction
  • Spectrum Analysis, Raman
  • Sulfur / chemistry

Substances

  • Sulfur
  • Cytochrome P-450 Enzyme System
  • Iron
  • Cysteine