By the same authors

Mammalian Respiratory Complex I Through the Lens of Cryo-EM

Research output: Contribution to journalReview articlepeer-review



Publication details

JournalAnnual review of biophysics
DateAccepted/In press - 19 Oct 2018
DateE-pub ahead of print - 20 Feb 2019
DatePublished (current) - 6 May 2019
Number of pages20
Pages (from-to)165-184
Early online date20/02/19
Original languageEnglish


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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