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

Masaki Unno, Toshitaka Matsui, Masao Ikeda-Saito

Research output: Contribution to journalShort surveypeer-review

16 Citations (Scopus)

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 O2 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.

Original languageEnglish
Pages (from-to)102-109
Number of pages8
JournalJournal of Inorganic Biochemistry
Volume113
DOIs
Publication statusPublished - 2012 Aug

Keywords

  • Heme oxygenase
  • Microspectrophotometer
  • Photoreduction
  • Reaction mechanism
  • Verdoheme
  • X-ray crystallography

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

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