Complex I: A chimaera of a redox and conformation-driven proton pump?
Complex I: A chimaera of a redox and conformation-driven proton pump?
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DOI：
10.1023/a:1010722717257
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发表时间：
2001-06-01
影响因子：
3
通讯作者：
Friedrich, T
中科院分区：
文献类型：
--
作者：
Friedrich, T
从系统发育序列分析可以得出结论，质子泵NADH：泛醌氧化还原酶(复合体I)是从先前存在的电子转移和质子转移模块进化而来的。它由外周NADH脱氢酶模块、两亲性氢酶模块和膜结合转运蛋白模块组成。这些模块，或至少其中的一部分，也存在于各种其他细菌酶中。据推测，它们在复合体I和相关酶中具有类似的功能。根据各个模块的功能，可以推测络合物I的作用机制。氢酶模块可能是氧化还原驱动的质子泵，而转运蛋白模块可能是构象驱动的质子泵。这意味着络合物I包含两个能量耦合位置。NADH脱氢酶模块似乎参与了质子转运中的电子转移和骚乱。
From phylogenetic sequence analysis, it can be concluded that the proton-pumping NADH:ubiquinone oxidoreductase (complex I) has evolved from preexisting modules for electron transfer and proton translocation. It is built up by a peripheral NADH dehydrogenase module, an amphipatic hydrogenase module, and a membrane-bound transporter module. These modules, or at least part of them, are also present in various other bacterial enzymes. It is assumed that they fulfill a similar function in complex I and related enzymes. Based on the function of the individual modules, it is possible to speculate about the mechanism of complex I. The hydrogenase module might work as a redox-driven proton pump, while the transporter module might act as a conformation-driven proton pump. This implies that complex I contains two energy-coupling sites. The NADH dehydrogenase module seems to be involved in electron transfer and riot in proton translocation.