Journal
JOURNAL OF INORGANIC BIOCHEMISTRY
Volume 113, Issue -, Pages 102-109Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2012.04.012
Keywords
Verdoheme; Microspectrophotometer; Heme oxygenase; X-ray crystallography; Photoreduction; Reaction mechanism
Funding
- Japan Society for the Promotion of Science (JSPS) [24570122, 23550186, 24350081]
- Grants-in-Aid for Scientific Research [24570122, 23370052, 23550186] Funding Source: KAKEN
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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. (C) 2012 Elsevier Inc. All rights reserved.
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