Active site structures of deoxyhemerythrin and oxyhemerythrin.
Active site structures of deoxyhemerythrin and oxyhemerythrin.
复制标题
脱氧血红蛋白和氧血红蛋白的活性位点结构。
DOI：
10.1073/pnas.82.3.713
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发表时间：
1985
影响因子：
11.1
通讯作者：
Sanders-Loehr,J
中科院分区：
文献类型：
--
作者：
Stenkamp,RE;Sieker,LC;Jensen,LH;McCallum,JD;Sanders-Loehr,J
用X射线晶体学技术研究了非血红素铁、氧转运蛋白血红蛋白的生理活性形式。在3.9-A分辨率，脱氧形式和甲氰菊酯形式（methemerythrin）的蛋白质之间的差异电子密度图表明，只有小的差异，双核铁络合物。铁原子的配位在脱氧和甲硫氨酸形式中似乎是相同的，络合物中的一个铁是五配位的，另一个铁是六配位的。脱氧态的铁原子似乎相距较远。一项2.2-A的氧代血红蛋白分离度研究表明，双氧与一个铁原子结合--在蛋白质的met形式中的五配位铁原子，与叠氮基血红蛋白中叠氮化物的结合位点相同。
The physiologically active forms of the nonheme-iron, oxygen-transport protein hemerythrin have been studied by x-ray crystallographic techniques. At 3.9-A resolution, a difference electron-density map between the deoxy form and met form (methemerythrin) of the protein suggests only small differences in the binuclear iron complexes. The coordination of the iron atoms appears to be the same in both the deoxy and met forms, one iron of the complexes being pentacoordinate, the other iron being hexacoordinate. The iron atoms appear to be somewhat farther apart in the deoxy form. A 2.2-A resolution study of oxyhemerythrin shows that dioxygen binds to one iron atom--the pentacoordinate one in the met form of the protein, the same binding site found for azide in azidomethemerythrin.