Mammalian Respiratory Complex I Through the Lens of Cryo-EM.
Blaza, James N
Annual Review of Biophysics
Annual Reviews Inc.
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Agip, N., Blaza, J. N., Fedor, J., & Hirst, J. (2019). Mammalian Respiratory Complex I Through the Lens of Cryo-EM.. Annual Review of Biophysics, 48 165-184. https://doi.org/10.1146/annurev-biophys-052118-115704
Single-particle electron cryomicroscopy (cryo-EM) has led to a revolution in structural work on mammalian respiratory complex I. Complex I (mitochondrial NADH:ubiquinone oxidoreductase), a membrane-bound redox-driven proton pump, is one of the largest and most complicated enzymes in the mammalian cell. Rapid progress, following the first 5-Å resolution data on bovine complex I in 2014, has led to a model for mouse complex I at 3.3-Å resolution that contains 96% of the 8,518 residues and to the identification of different particle classes, some of which are assigned to biochemically defined states. Factors that helped improve resolution, including improvements to biochemistry, cryo-EM grid preparation, data collection strategy, and image processing, are discussed. Together with recent structural data from an ancient relative, membrane-bound hydrogenase, cryo-EM on mammalian complex I has provided new insights into the proton-pumping machinery and a foundation for understanding the enzyme's catalytic mechanism.
NADH:ubiquinone oxidoreductase, electron cryomicroscopy, membrane-bound hydrogenase, mitochondria, oxidative phosphorylation, single-particle reconstruction
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External DOI: https://doi.org/10.1146/annurev-biophys-052118-115704
This record's URL: https://www.repository.cam.ac.uk/handle/1810/296787
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