TY  - JOUR
A1  - Parey, Kristian Kurt
A1  - Brandt, Ulrich
A1  - Xie, Hao
A1  - Mills, Deryck J.
A1  - Siegmund, Karin
A1  - Vonck, Janet
A1  - Kühlbrandt, Werner
A1  - Zickermann, Volker
T1  - Cryo-EM structure of respiratory complex I at work
T2  - eLife
N2  - Mitochondrial complex I has a key role in cellular energy metabolism, generating a major portion of the proton motive force that drives aerobic ATP synthesis. The hydrophilic arm of the L-shaped ~1 MDa membrane protein complex transfers electrons from NADH to ubiquinone, providing the energy to drive proton pumping at distant sites in the membrane arm. The critical steps of energy conversion are associated with the redox chemistry of ubiquinone. We report the cryo-EM structure of complete mitochondrial complex I from the aerobic yeast Yarrowia lipolytica both in the deactive form and after capturing the enzyme during steady-state activity. The site of ubiquinone binding observed during turnover supports a two-state stabilization change mechanism for complex I.
KW  - Research article
KW  - structural biology and molecular biophysics
KW  - respiratory complex I
KW  - redox-linked proton translocation
KW  - active/deactive transition
KW  - Yarrowia lipolytica
Y1  - 2018
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/48359
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-483593
SN  - 2050-084X
N1  - Copyright Parey et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.
VL  - 7
IS  - e39213
SP  - 1
EP  - 28
PB  - eLife Sciences Publications
CY  - Cambridge
ER  -