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- W2916585268 abstract "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." @default.
- W2916585268 created "2019-03-02" @default.
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- W2916585268 creator A5056046836 @default.
- W2916585268 creator A5056621986 @default.
- W2916585268 creator A5090746349 @default.
- W2916585268 date "2019-05-06" @default.
- W2916585268 modified "2023-10-18" @default.
- W2916585268 title "Mammalian Respiratory Complex I Through the Lens of Cryo-EM" @default.
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- W2916585268 doi "https://doi.org/10.1146/annurev-biophys-052118-115704" @default.
- W2916585268 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30786232" @default.
- W2916585268 hasPublicationYear "2019" @default.
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