Crystallographic studies of heme oxygenase complexed with an unstable reaction intermediate, verdoheme

J Inorg Biochem. 2012 Aug;113:102-9. doi: 10.1016/j.jinorgbio.2012.04.012. Epub 2012 Apr 27.

Abstract

This article discusses the accuracy of X-ray structural studies of heme oxygenase (HO) in complex with an unstable intermediate, verdoheme. Heme degradation by HO proceeds through three successive steps of O(2) activation. The mechanism of the third step, the ring opening of verdoheme, has been the least understood. Recent structural studies of the verdoheme-HO complex provide detailed information concerning this mechanism. Due to X-ray-induced photoreduction and the instability of verdoheme, it has been difficult to obtain an accurate structure for the ferrous verdoheme-HO complex. Therefore, accurate structural studies, including analysis of the electronic state of the verdoheme-HO complex, are needed to elucidate the proper reaction mechanism.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Biliverdine / chemistry
  • Catalysis
  • Crystallography, X-Ray
  • Heme / analogs & derivatives*
  • Heme / chemistry
  • Heme Oxygenase (Decyclizing) / chemistry*
  • Humans
  • Models, Molecular
  • Oxidation-Reduction
  • Oxygen / chemistry*
  • Photochemical Processes
  • Quantum Theory
  • Water / chemistry

Substances

  • verdoheme
  • Water
  • Heme
  • Heme Oxygenase (Decyclizing)
  • Biliverdine
  • Oxygen