Chapter 4:Multi-scale Molecular Simulations on Respiratory Complex I
Chapter 4:Multi-scale Molecular Simulations on Respiratory Complex I
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第 4 章：呼吸复合物 I 的多尺度分子模拟
DOI：
10.1039/9781788010405-00081
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发表时间：
2018
期刊：
影响因子：
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通讯作者：
Kaila VRI
中科院分区：
文献类型：
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作者：
Kaila VRI
复合物I是最大（0.5-1 MDa）和最复杂的呼吸酶之一。它催化电子从烟碱酰胺二核苷酸（NADH）转移到其亲水结构域中的醌（Q），沿着沿着一个约10 - 20个碳原子。100纳米线由黄素单核苷酸（FMN）和8-9个FeS中心组成。1-5这在一个过程中将Q还原为对苯二酚（QH 2），该过程与四个质子穿过复合物I、6、7的膜结构域的泵送相耦合，直到约1000。距离Q降低点200 m处（图4.1）。尽管最近从几个物种中解析了X射线8 -12和冷冻EM 13 -15结构，但来自标记16-18交联19和定点诱变研究20-26以及生物物理实验27，28的数据，复合物I催化这种显著的长距离质子偶联电子转移（PCET）过程的机制仍然不清楚。阐明复合物I的分子机制并不是
Complex I is one of the largest (0.5–1 MDa) and most intricate respiratory enzymes. It catalyzes electron transfer (eT) from nicotine amide dinucleotide (NADH) to quinone (Q) in its hydrophilic domain along a ca. 100 Å wire composed of flavin mononucleotide (FMN) and 8–9 FeS centers. 1–5 This reduces Q to quinol (QH2) in a process that is coupled to pumping of four protons across the membrane domain of complex I, 6, 7 up to ca. 200 Å away from the site of Q reduction (Figure 4.1). Despite recently resolved X-ray8–12 and cryo-EM13–15 structures from several species, data from labeling-, 16–18 crosslinking-, 19 and site-directed mutagenesis studies, 20–26 as well as biophysical experiments, 27, 28 the mechanism by which complex I catalyzes this remarkable long-range proton-coupled electron transfer (PCET) process still remains unclear. Elucidating the molecular mechanism of complex I is not
DOI：
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发表时间：
2006
期刊：
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影响因子：
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作者：
Iroon Polytechniou-
通讯作者：
Iroon Polytechniou-