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血红素加氧酶与不稳定反应中间产物胆绿素复合物的晶体学研究。

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

机构信息

Frontier Research Center for Applied Atomic Sciences, Ibaraki University, Tokai, Naka, Ibaraki 319-1106, Japan.

出版信息

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

DOI:10.1016/j.jinorgbio.2012.04.012
PMID:22673156
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.

摘要

本文讨论了血红素加氧酶（HO）与不稳定中间产物胆绿素复合物的 X 射线结构研究的准确性。HO 通过三个连续的 O(2)激活步骤进行血红素降解。第三步，即胆绿素的开环反应，是理解最少的步骤。最近胆绿素-HO 复合物的结构研究提供了有关该机制的详细信息。由于 X 射线诱导的光还原和胆绿素的不稳定性，很难获得亚铁胆绿素-HO 复合物的准确结构。因此，需要进行准确的结构研究，包括胆绿素-HO 复合物电子态的分析，以阐明正确的反应机制。

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