Structural Model of the Fe-Hydrogenase/Cytochromec 553 Complex Combining Transverse Relaxation-optimized Spectroscopy Experiments and Soft Docking Calculations*
Structural Model of the Fe-Hydrogenase/Cytochromec 553 Complex Combining Transverse Relaxation-optimized Spectroscopy Experiments and Soft Docking Calculations*
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结合横向弛豫优化光谱实验和软对接计算的 Fe-氢化酶/细胞色素 553 复合物的结构模型*
DOI：
10.1074/jbc.m909835199
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发表时间：
2000
期刊：
影响因子：
--
通讯作者：
F. Guerlesquin
中科院分区：
文献类型：
--
作者：
X. Morelli;M. Czjzek;C. Hatchikian;O. Bornet;J. Fontecilla;N. Palma;J. Moura;F. Guerlesquin
铁氢化酶是一种54 kda的铁硫酶，对硫酸盐还原细菌的氢循环至关重要。脱硫弧菌（Desulfovibrio desulicans）铁氢化酶（Fe-hydrogenase）的x射线结构最近已经被解决，但识别其氧化还原伙伴的结构信息对于理解酶的结构-功能关系至关重要。在本工作中，我们结合对接计算和核磁共振实验，得到了铁氢化酶与其氧化还原伙伴细胞色素c553配合物的结构模型。该络合物的假设模型表明，氢化酶的小亚基在与氧化还原伙伴形成络合物中起重要作用；氢化酶上50%的相互作用位点涉及到这个小亚基。在氢化酶远端簇的配体Cys-38和细胞色素中血红素的配体Cys-10之间观察到最密切的氧化还原中心接触。利用Greenpath软件研究了从铁氢化酶远端簇到细胞色素553血红素的电子途径，并表明观察到的半胱氨酸/半胱氨酸接触起重要作用。配合物界面上残基的空间排列与铁氧还蛋白-细胞色素c 553配合物非常相似，因此，这是铁氢化酶-细胞色素c 553相互作用域的一个很好的模型。
Fe-hydrogenase is a 54-kDa iron–sulfur enzyme essential for hydrogen cycling in sulfate-reducing bacteria. The x-ray structure of Desulfovibrio desulfuricans Fe-hydrogenase has recently been solved, but structural information on the recognition of its redox partners is essential to understand the structure-function relationships of the enzyme. In the present work, we have obtained a structural model of the complex of Fe-hydrogenase with its redox partner, the cytochrome c 553, combining docking calculations and NMR experiments. The putative models of the complex demonstrate that the small subunit of the hydrogenase has an important role in the complex formation with the redox partner; 50% of the interacting site on the hydrogenase involves the small subunit. The closest contact between the redox centers is observed between Cys-38, a ligand of the distal cluster of the hydrogenase and Cys-10, a ligand of the heme in the cytochrome. The electron pathway from the distal cluster of the Fe-hydrogenase to the heme of cytochromec 553 was investigated using the software Greenpath and indicates that the observed cysteine/cysteine contact has an essential role. The spatial arrangement of the residues on the interface of the complex is very similar to that already described in the ferredoxin-cytochrome c 553 complex, which therefore, is a very good model for the interacting domain of the Fe-hydrogenase-cytochrome c 553.
影响因子：
2.9
作者：
Davidson, VL;Jones, LH
通讯作者：
Jones, LH