著者

海野 昌喜 松井 敏高 齋藤 正男

出版者

日本結晶学会

雑誌

日本結晶学会誌 (ISSN:03694585)

巻号頁・発行日

vol.53, no.3, pp.213-218, 2011-06-30 (Released:2011-07-13)

参考文献数

19

被引用文献数

2

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X-ray crystallographic analysis of a metalloprotein requires knowing the electronic state of the metal center, if one wants to elucidate the exact function and/or reaction mechanism. As an example, we show our recent structural analysis of the heme oxygenase reaction intermediate which is involved in the third step of the heme degradation reaction. The reaction intermediate was crystallized under anaerobic condition, and the obtained crystals were frozen into liquid nitrogen. The absorption spectra of the single crystal before and after X-ray irradiation were compared with that of the frozen solution in 100 K cold nitrogen stream. The determined structure offers the first solid evidence for the presence of a water cluster in the distal pocket of this catalytically critical intermediate. This structure combined with the QM/MM calculation supports our proposal that the biliverdin is produced via Fe-OOH verdoheme intermediate.