A two-state stabilization-change mechanism for proton-pumping complex I.
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TLDR
The proposed two-state stabilization-change mechanism is fully reversible and thus inherently explains the operation of complex I in forward and reverse mode.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 2011-10-01 and is currently open access. It has received 107 citations till now. The article focuses on the topics: Membrane protein complex & Electron transport chain.read more
Citations
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Journal ArticleDOI
Mitochondrial complex I.
TL;DR: Evaluated data on the mechanisms of energy transduction and superoxide production by complex I is evaluated, contemporary mechanistic models are discussed, and how mechanistic studies may contribute to understanding the roles of complex I dysfunctions in human diseases are explored.
Book ChapterDOI
Molecular Mechanisms of Superoxide Production by the Mitochondrial Respiratory Chain
Stefan Dröse,Ulrich Brandt +1 more
TL;DR: A detailed understanding of the molecular mechanisms driving these enzymes is required to understand mitochondrial ROS production during oxidative stress and redox signalling.
Journal ArticleDOI
A giant molecular proton pump: structure and mechanism of respiratory complex I
TL;DR: The crystal structure of the entire complex I was solved using a bacterial enzyme provided novel insights into the core architecture of the complex, the electron transfer and proton translocation pathways, as well as the mechanism that couples these two processes.
Journal ArticleDOI
Mechanistic insight from the crystal structure of mitochondrial complex I
Volker Zickermann,Christophe Wirth,Hamid R. Nasiri,Hamid R. Nasiri,Karin Siegmund,Harald Schwalbe,Carola Hunte,Ulrich Brandt,Ulrich Brandt +8 more
TL;DR: The proposed transition into the active form is based on a concerted structural rearrangement at the ubiquinone reduction site, providing support for a two-state stabilization-change mechanism of proton pumping.
Journal ArticleDOI
Architecture of Human Mitochondrial Respiratory Megacomplex I2III2IV2.
TL;DR: The structure of the human respiratory chain megacomplex with 140 subunits and a subset of associated cofactors is examined using cryo-electron microscopy to reveal the precise assignment of individual subunits of human CI and CIII and enables future in-depth analysis of the electron transport chain as a whole.
References
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Journal ArticleDOI
Energy Converting NADH: Quinone Oxidoreductase (Complex I)
TL;DR: The coupling mechanism of complex I most likely involves semiquinone intermediates that drive proton pumping through redox-linked conformational changes.
Journal ArticleDOI
The architecture of respiratory complex I
TL;DR: The architecture of the complex provides strong clues about the coupling mechanism: the conformational changes at the interface of the two main domains may drive the long amphipathic α-helix of NuoL in a piston-like motion, tilting nearby discontinuous TM helices, resulting in proton translocation.
Journal ArticleDOI
Inhibitors of NADH-ubiquinone reductase: an overview.
TL;DR: The compounds that inhibit the NADH–ubiquinone reductase activity of complex I are classified according to three fundamental types of action on the basis of available evidence and recent insights.
Journal ArticleDOI
Bovine complex I is a complex of 45 different subunits.
TL;DR: The subunit composition of bovine complex I is established, a complex of 45 different proteins plus non-covalently bound FMN and eight iron-sulfur clusters and shown to be a C-terminal fragment of subunit SGDH arising from a specific peptide bond cleavage between Ile-55 and Pro-56 during the electrospray ionization process.
Journal ArticleDOI
Iron-sulfur clusters/semiquinones in complex I.
TL;DR: This mini-review describes three aspects of the recent progress in the study of the redox components of Complex I and suggests that the cluster N2 may have a unique ligand structure with an atypical cluster-ligation sequence motif located in the NuoB (NQO6/PSST) subunit rather than in the long advocated NuoI (NZO9/TYKY) subunits.