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首页> 外文期刊>Biochemistry >Redox Linked Conformational Changes in Cytochrome c(3) from Desulfovibrio desulfuricans ATCC 27774
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Redox Linked Conformational Changes in Cytochrome c(3) from Desulfovibrio desulfuricans ATCC 27774

机译：氧化还原联系细胞色素C（3）的构象变化来自脱硫脱硫症ATCC 27774

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摘要

Cytochrome c(3) from Desulfovibrio desulfuricans. ATCC 27774 appears to be capable of receiving two protons and two electrons from hydrogenase for transport to the membrane, and converting electronic energy into proton motive force. Detailed studies of the mechanism require control both of the redox state and of the protonation state of the protein; hence, structure determination of the protein in solution by NMR is the preferred method. This work compares the structures of the protonated protein in the fully oxidized and fully reduced states as a First step toward elucidating the pH-dependent and redox-state-dependent conformational changes that drive the energy transduction. These high-resolution structures revealed significant localized differences upon change of redox state, even though the global folds of the two families of structures are similar. There are concerted redox-linked motions within the protein that bring E61 and K75 closer to heme II in the oxidized form. This is consistent with an electrostatically driven movement that may provide an important contribution to the previously measured positive cooperativity between hemes I and II. No significant conformational changes were observed that might be related to redox-Bohr effects; the families of structures represent mainly protonated forms, and therefore, pH dependence should not play a major role in the observed structural rearrangements.
机译：细胞色素C（3）来自脱硫脱硫血症。 ATCC 27774似乎能够从氢酶接收两种质子和两个电子以用于运输到膜，并将电子能量转化为质子动力。对机制的详细研究需要控制氧化还原状态和蛋白质的质子化状态;因此，通过NMR溶液中蛋白质的结构测定是优选的方法。这项工作将质子化蛋白质的结构与完全氧化和完全降低状态的结构进行比较，作为阐明驱动能量转导的pH依赖性和氧化还原状态相关的构象变化的第一步。这些高分辨率结构在氧化还原状态的变化时揭示了显着的局部差异，即使两个结构的全球褶皱是相似的。在蛋白质中有齐心的氧化氧连接动作，使E61和K75更接近氧化形式的血红素II。这与静电驱动的运动一致，可以为先前测量的血液I和II之间的阳性合作性提供重要贡献。没有观察到与氧化还原-BoHR效应有关的显着构象变化;结构家庭主要代表质子化形式，因此，pH依赖性不应在观察到的结构重排中发挥重要作用。

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