Making the leap from structure to mechanism: are the open states of mammalian complex I identified by cryoEM resting states or catalytic intermediates?
Making the leap from structure to mechanism: are the open states of mammalian complex I identified by cryoEM resting states or catalytic intermediates?
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DOI：
10.1016/j.sbi.2022.102447
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发表时间：
2022-12
影响因子：
6.8
通讯作者：
Hirst J
中科院分区：
文献类型：
--
作者：
Chung I;Grba DN;Wright JJ;Hirst J
呼吸复合物I（NADH：泛醌氧化还原酶）是一种多亚基、能量转导线粒体酶，对氧化磷酸化和调节NAD+/NADH库至关重要。尽管最近的进展，结构知识和悠久的历史，生化分析，氧化还原耦合质子易位的机制复杂的I仍然是未知的。由于其能够将混合群体中的分子分离成不同的类别，单粒子电子低温显微镜已经能够识别和表征不同的复合物I构象。然而，决定它们的催化和/或调节特性以支持机制假设，特别是在没有结构样品的详细生化表征的情况下，已被证明具有挑战性。在这篇综述中，我们探讨了不同的机制解释的封闭和开放状态确定在cryoEM分析哺乳动物复合物I。
Respiratory complex I (NADH:ubiquinone oxidoreductase) is a multi-subunit, energy-transducing mitochondrial enzyme that is essential for oxidative phosphorylation and regulating NAD+/NADH pools. Despite recent advances in structural knowledge and a long history of biochemical analyses, the mechanism of redox-coupled proton translocation by complex I remains unknown. Due to its ability to separate molecules in a mixed population into distinct classes, single-particle electron cryomicroscopy has enabled identification and characterisation of different complex I conformations. However, deciding on their catalytic and/or regulatory properties to underpin mechanistic hypotheses, especially without detailed biochemical characterisation of the structural samples, has proven challenging. In this review we explore different mechanistic interpretations of the closed and open states identified in cryoEM analyses of mammalian complex I.
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DOI：
10.1093/plcell/koab092
发表时间：
2021-07-19
期刊：
The Plant cell
影响因子：
--
作者：
Klusch N;Senkler J;Yildiz Ö;Kühlbrandt W;Braun HP
通讯作者：
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影响因子：
8.6
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影响因子：
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影响因子：
16.6
作者：
Bridges HR;Fedor JG;Blaza JN;Di Luca A;Jussupow A;Jarman OD;Wright JJ;Agip AA;Gamiz-Hernandez AP;Roessler MM;Kaila VRI;Hirst J
通讯作者：
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影响因子：
56.9
作者：
Kampjut, Domen;Sazanov, Leonid A.
通讯作者：
Sazanov, Leonid A.