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Journal Article

Respiratory complex I - structure, mechanism and evolution

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Parey,  Kristian Kurt
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Biochemistry II, University Hospital, Goethe University, Frankfurt am Main, Germany;
Centre for Biomolecular Magnetic Resonance, Institute for Biophysical Chemistry, Goethe University, Frankfurt am Main, Germany;

/persons/resource/persons137933

Vonck,  Janet       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Parey, K. K., Wirth, C., Vonck, J., & Zickermann, V. (2020). Respiratory complex I - structure, mechanism and evolution. Current Opinion in Structural Biology, 63. doi:10.1016/j.sbi.2020.01.004.


Cite as: https://hdl.handle.net/21.11116/0000-0005-A969-7
Abstract
Respiratory complex I is an intricate multi-subunit membrane protein with a central function in aerobic energy metabolism. During the last years, structures of mitochondrial complex I and respiratory supercomplexes were determined by cryo-EM at increasing resolution. Structural and computational studies have shed light on the dynamics of proton translocation pathways, the interaction of complex I with lipids and the unusual access pathway of ubiquinone to the active site. Recent advances in understanding complex I function include characterization of specific conformational changes that are critical for proton pumping. Cryo-EM structures of the NADH dehydrogenase-like (NDH) complex of photosynthesis and a bacterial membrane bound hydrogenase (MBH) have provided a broader perspective on the complex I superfamily.