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Mammalian Respiratory Complex I Through the Lens of Cryo-EM. | LitMetric

Mammalian Respiratory Complex I Through the Lens of Cryo-EM.

Annu Rev Biophys

Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom; email: , , ,

Published: May 2019

AI Article Synopsis

  • - Single-particle electron cryomicroscopy (cryo-EM) has significantly advanced our understanding of mammalian respiratory complex I, a complex enzyme crucial for energy production in cells.
  • - Since achieving 5-Å resolution data on bovine complex I in 2014, researchers have developed a detailed model for mouse complex I at 3.3-Å resolution, capturing nearly all of its 8,518 residues and revealing different functional states.
  • - Key improvements in resolution have been made through advancements in biochemistry, cryo-EM techniques, and data analysis, leading to new insights into the enzyme's function and its proton-pumping mechanism.

Article 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.

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Source
http://dx.doi.org/10.1146/annurev-biophys-052118-115704DOI Listing

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