TY - JOUR
T1 - Crystallographic studies of heme oxygenase complexed with an unstable reaction intermediate, verdoheme
AU - Unno, Masaki
AU - Matsui, Toshitaka
AU - Ikeda-Saito, Masao
N1 - Funding Information:
We thank Prof. S. Shaik and Dr. W. Lai of Hebrew University for their help with the QM/MM calculation. We thank Mr. K. Omori, a former graduate student of Tohoku University, for preparing and characterizing the verdoheme–HmuO crystals. This work was supported in parts by Grants-in-Aid for Scientific Research , 24570122 (M. U.), 23550186 (T. M.), and 24350081 (M.I.-S.) from Japan Society for the Promotion of Science (JSPS) .
PY - 2012/8
Y1 - 2012/8
N2 - 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.
AB - 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.
KW - Heme oxygenase
KW - Microspectrophotometer
KW - Photoreduction
KW - Reaction mechanism
KW - Verdoheme
KW - X-ray crystallography
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U2 - 10.1016/j.jinorgbio.2012.04.012
DO - 10.1016/j.jinorgbio.2012.04.012
M3 - Short survey
C2 - 22673156
AN - SCOPUS:84863725870
SN - 0162-0134
VL - 113
SP - 102
EP - 109
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
ER -