同步加速器 X 射线诱导的高铁肌红蛋白亚硝酸盐晶体光还原反应，生成保留 O 键合亚硝酸盐配体的亚铁衍生物。
Synchrotron X-ray-induced photoreduction of ferric myoglobin nitrite crystals gives the ferrous derivative with retention of the O-bonded nitrite ligand.
机构信息
Department of Chemistry and Biochemistry, University of Oklahoma, 620 Parrington Oval, Norman, Oklahoma 73019, USA.
出版信息
Biochemistry. 2010 Jul 27;49(29):5969-71. doi: 10.1021/bi100801g.
Abstract
Exposure of a single crystal of the nitrite adduct of ferric myoglobin (Mb) at 100 K to high-intensity synchrotron X-ray radiation resulted in changes in the UV-vis spectrum that can be attributed to reduction of the ferric compound to the ferrous derivative. We employed correlated single-crystal spectroscopy with crystallography to further characterize this photoproduct. The 1.55 A resolution crystal structure of the photoproduct reveals retention of the O-binding mode for binding of nitrite to the iron center. The data are consistent with cryogenic generation and trapping, at 100 K, of a ferrous d(6) Mb(II)(ONO)* complex by photoreduction of the ferric precursor crystals using high-intensity X-ray radiation.
摘要
将铁肌红蛋白（Mb）亚硝酸盐加合物的单晶在 100 K 下暴露于高强度同步加速器 X 射线辐射下，导致紫外可见光谱发生变化，这可以归因于将三价铁化合物还原为二价衍生物。我们采用相关单晶光谱学与晶体学进一步表征这种光产物。该光产物的 1.55Å 分辨率晶体结构表明，亚硝酸盐与铁中心的结合保持了 O 结合模式。这些数据与在 100 K 下使用高强度 X 射线辐射通过光还原铁前体晶体低温生成和捕获亚铁 d(6)Mb(II)(ONO)*配合物是一致的。
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