Profiling the active site of a copper enzyme through its far-infrared fingerprint

Angew Chem Int Ed Engl. 2011 Aug 22;50(35):8062-6. doi: 10.1002/anie.201102014. Epub 2011 Jul 12.

Abstract

Vibrations of the metal active site of the Cu,Zn-superoxide dismutase enzyme were analyzed by far-infrared difference spectroscopy and theoretical normal mode calculation. Both electrochemically triggered Cu(I) and Cu(II) redox states show well-defined infrared vibrational modes, notably modes of the histidine ligands, the Cu(II)-His(61)-Zn(II) bridge and of the water pseudo-ligand.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalytic Domain
  • Copper / chemistry
  • Histidine / chemistry
  • Ligands
  • Oxidation-Reduction
  • Spectroscopy, Fourier Transform Infrared
  • Superoxide Dismutase / chemistry*
  • Superoxide Dismutase / metabolism
  • Water / chemistry

Substances

  • Ligands
  • Water
  • Histidine
  • Copper
  • Superoxide Dismutase