Structure and Mechanism of Respiratory III-IV Supercomplexes in Bioenergetic Membranes.
Structure and Mechanism of Respiratory III-IV Supercomplexes in Bioenergetic Membranes.
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DOI：
10.1021/acs.chemrev.1c00140
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发表时间：
2021-08-11
期刊：
影响因子：
62.1
通讯作者：
Ädelroth P
中科院分区：
文献类型：
--
作者：
Brzezinski P;Moe A;Ädelroth P
在有氧生物能量守恒的最后步骤中，电子通过呼吸链传递的自由能被转化为跨膜的质子电化学梯度。在线粒体和许多细菌中，二氧电子受体的还原是由细胞色素c氧化酶（复合体IV）催化的，细胞色素c氧化酶通过膜结合或水溶性细胞色素c接收来自细胞色素bc1（复合体III）的电子。这些复合体独立起作用，但在许多生物体中它们结合形成超复合体。本文综述了非专性III2IV1/2Saccharomyces cerevisiae线粒体超复合体和放线菌中专性III2IV2线粒体超复合体的结构特征和功能意义。分析的重点是配合物III的Q-cycle， CytcO的质子摄取，以及配合物III和IV之间电子连接的机制和结构解决方案。
In the final steps of energy conservation in aerobic organisms, free energy from electron transfer through the respiratory chain is transduced into a proton electrochemical gradient across a membrane. In mitochondria and many bacteria, reduction of the dioxygen electron acceptor is catalyzed by cytochrome c oxidase (complex IV), which receives electrons from cytochrome bc1 (complex III), via membrane-bound or water-soluble cytochrome c. These complexes function independently, but in many organisms they associate to form supercomplexes. Here, we review the structural features and the functional significance of the nonobligate III2IV1/2Saccharomyces cerevisiae mitochondrial supercomplex as well as the obligate III2IV2 supercomplex from actinobacteria. The analysis is centered around the Q-cycle of complex III, proton uptake by CytcO, as well as mechanistic and structural solutions to the electronic link between complexes III and IV.
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影响因子：
2.9
作者：
Adelroth, P;Gennis, RB;Brzezinski, P
通讯作者：
Brzezinski, P
影响因子：
4.3
作者：
Aagaard, A;Namslauer, A;Brzezinski, P
通讯作者：
Brzezinski, P
影响因子：
4.8
作者：
ALLEN, LA;ZHAO, XJ;POYTON, RO
通讯作者：
POYTON, RO
DOI：
10.1073/pnas.1413855111
发表时间：
2014-11-04
影响因子：
11.1
作者：
Blaza, James N.;Serreli, Riccardo;Hirst, Judy
通讯作者：
Hirst, Judy
影响因子：
4.6
作者：
Schäfer J;Dawitz H;Ott M;Ädelroth P;Brzezinski P
通讯作者：
Brzezinski P