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Cryo-EM structure of respiratory complex I at work
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Journal Article
Cryo-EM structure of respiratory complex I at work
2018
Overview
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.
Publisher
eLife Science Publications, Ltd,eLife Sciences Publications Ltd,eLife Sciences Publications, Ltd
Subject
/ Biology
/ Cryoelectron Microscopy - methods
/ Electron Transport Complex I - chemistry
/ Electron Transport Complex I - metabolism
/ Electron Transport Complex I - ultrastructure
/ Enzymes
/ Fungal Proteins - metabolism
/ Fungal Proteins - ultrastructure
/ Mammals
/ Mitochondria - ultrastructure
/ NADH
/ NADH-ubiquinone oxidoreductase
/ Proteins
/ redox-linked proton translocation
/ Sequence Homology, Amino Acid
