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Orientation of the g-Tensor Axes of the Rieske Subunit in the Cytochrome bCl Complext

机译:细胞色素bC复合物中Rieske亚基的g轴张力的方向。

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The orientation of the g-tensors of the Rieske iron-sulfur protein subunit was determined in a single crystal of the bovine mitochondrial cytochrome bCl complex with stigmatellin in the Qo quinol binding site.The g-tensor principal axes are skewed with respect to the Fe-Fe and S-S atom direction in the 2Fe2S cluster,which is allowed by the lack of rigorous symmetry of the cluster.The asymmetric unit in the crystal is the active dimmer,and the g-tensor axes have slightly different orientations relative to the iron-sulfur cluster in the two halves of the dimmer.The g approx= 1.79 axis makes an average angle of 30 deg with respect to the Fe-Fe direction and the g approx= 2.024 axis an average angle of 26 deg with respect to the S-S direction.This assignment of the g-tensoraxis directions indicates that conformations of the Rieske protein are likely the same in the cytochrome bCl and br/complexes and that the extent of motion of the Rieske head domain during the catalytic cycle has been highly conserved during evolution of these distantly related complexes.
机译:Rieske铁-硫蛋白亚基的g张量的取向是在Qo quinol结合位点上带有柱头蛋白的牛线粒体细胞色素bCl络合物的单晶中确定的.g张量主轴相对于Fe偏斜。 -Fe和SS原子在2Fe2S团簇中的方向,这是由于该团簇缺乏严格的对称性所允许的。晶体中的不对称单元是主动调光器,并且g张量轴相对于铁原子取向略有不同。调光器的两半中的硫簇.g大约= 1.79轴相对于Fe-Fe方向的平均角度为30度,g大约= 2.024轴相对于SS方向的平均角度为26度g轴方向的这种分配表明Rieske蛋白的构象在细胞色素bCl和br /复合物中可能是相同的,并且Rieske头域在催化循环中的运动程度已经很高。在这些遥远相关的复合体的进化过程中,ghly是保守的。

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