---
res:
  bibo_abstract:
  - Mitochondrial complex I couples NADH:ubiquinone oxidoreduction to proton pumping
    by an unknown mechanism. Here, we present cryo-electron microscopy structures
    of ovine complex I in five different conditions, including turnover, at resolutions
    up to 2.3 to 2.5 angstroms. Resolved water molecules allowed us to experimentally
    define the proton translocation pathways. Quinone binds at three positions along
    the quinone cavity, as does the inhibitor rotenone that also binds within subunit
    ND4. Dramatic conformational changes around the quinone cavity couple the redox
    reaction to proton translocation during open-to-closed state transitions of the
    enzyme. In the induced deactive state, the open conformation is arrested by the
    ND6 subunit. We propose a detailed molecular coupling mechanism of complex I,
    which is an unexpected combination of conformational changes and electrostatic
    interactions.@eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Domen
      foaf_name: Kampjut, Domen
      foaf_surname: Kampjut
      foaf_workInfoHomepage: http://www.librecat.org/personId=37233050-F248-11E8-B48F-1D18A9856A87
  - foaf_Person:
      foaf_givenName: Leonid A
      foaf_name: Sazanov, Leonid A
      foaf_surname: Sazanov
      foaf_workInfoHomepage: http://www.librecat.org/personId=338D39FE-F248-11E8-B48F-1D18A9856A87
    orcid: 0000-0002-0977-7989
  bibo_doi: 10.1126/science.abc4209
  bibo_issue: '6516'
  bibo_volume: 370
  dct_date: 2020^xs_gYear
  dct_identifier:
  - UT:000583031800004
  dct_isPartOf:
  - http://id.crossref.org/issn/10959203
  dct_language: eng
  dct_publisher: American Association for the Advancement of Science@
  dct_title: The coupling mechanism of mammalian respiratory complex I@
  fabio_hasPubmedId: '32972993'
...