Co(II)/Co(I) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model
Co(II)/Co(I) reduction-induced axial histidine-flipping in myoglobin reconstituted with a cobalt tetradehydrocorrin as a methionine synthase model
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DOI：
10.1039/c4cc05448b
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发表时间：
2014-01-01
影响因子：
4.9
通讯作者：
Hisaeda, Yoshio
中科院分区：
文献类型：
--
作者：
Hayashi, Takashi;Morita, Yoshitsugu;Hisaeda, Yoshio
制备了一种脱辅基肌红蛋白与四氢咕啉钴的结合物，以复制辅酶（I）丙氨酸在甲硫氨酸合酶中的配位行为。X射线晶体学分析表明，四配位Co（I）物种是通过血红素口袋中五配位Co（II）辅因子还原后轴向Co-His 93连接的裂解而形成的。
A conjugate between apomyoglobin and cobalt tetradehydrocorrin was prepared to replicate the coordination behavior of cob(I) alamin in methionine synthase. X-ray crystallography reveals that the tetra-coordinated Co(I) species is formed through the cleavage of the axial Co-His93 ligation after the reduction of the penta-coordinated Co(II) cofactor in the heme pocket.