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Elife. 2018 Oct 2;7. pii: e39213. doi: 10.7554/eLife.39213.

Cryo-EM structure of respiratory complex I at work.

Author information

1
Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, Germany.
2
Radboud Institute for Molecular Life Sciences, Department of Pediatrics, Radboud University Medical Centre, Nijmegen, The Netherlands.
3
Cluster of Excellence Macromolecular Complexes, Goethe University Frankfurt, Frankfurt, Germany.
4
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Frankfurt, Germany.
5
Medical School, Institute of Biochemistry II, Goethe University Frankfurt, Frankfurt, Germany.
6
Centre for Biomolecular Magnetic Resonance, Institute for Biophysical Chemistry, Goethe University Frankfurt, Frankfurt, Germany.

Abstract

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.

KEYWORDS:

Yarrowia lipolytica; active/deactive transition; molecular biophysics; redox-linked proton translocation; respiratory complex I; structural biology

PMID:
30277212
PMCID:
PMC6168287
DOI:
10.7554/eLife.39213
[Indexed for MEDLINE]
Free PMC Article

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