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From the same journal

Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states

Research output: Contribution to journalArticlepeer-review


  • Ahmed-Noor A Agip
  • James N Blaza
  • Hannah R Bridges
  • Carlo Viscomi
  • Shaun Rawson
  • Stephen P Muench
  • Judy Hirst


Publication details

JournalNature Structural & Molecular Biology
DateAccepted/In press - 26 Apr 2018
DateE-pub ahead of print - 18 Jun 2018
DatePublished (current) - 1 Jul 2018
Issue number7
Number of pages9
Pages (from-to)548-556
Early online date18/06/18
Original languageEnglish


Complex I (NADH:ubiquinone oxidoreductase) uses the reducing potential of NADH to drive protons across the energy-transducing inner membrane and power oxidative phosphorylation in mammalian mitochondria. Recent cryo-EM analyses have produced near-complete models of all 45 subunits in the bovine, ovine and porcine complexes and have identified two states relevant to complex I in ischemia-reperfusion injury. Here, we describe the 3.3-Å structure of complex I from mouse heart mitochondria, a biomedically relevant model system, in the 'active' state. We reveal a nucleotide bound in subunit NDUFA10, a nucleoside kinase homolog, and define mechanistically critical elements in the mammalian enzyme. By comparisons with a 3.9-Å structure of the 'deactive' state and with known bacterial structures, we identify differences in helical geometry in the membrane domain that occur upon activation or that alter the positions of catalytically important charged residues. Our results demonstrate the capability of cryo-EM analyses to challenge and develop mechanistic models for mammalian complex I.

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