---
res:
  bibo_abstract:
  - The 1 MDa, 45-subunit proton-pumping NADH-ubiquinone oxidoreductase (complex I)
    is the largest complex of the mitochondrial electron transport chain. The molecular
    mechanism of complex I is central to the metabolism of cells, but has yet to be
    fully characterized. The last two years have seen steady progress towards this
    goal with the first atomic-resolution structure of the entire bacterial complex
    I, a 5 Å cryo-electron microscopy map of bovine mitochondrial complex I and a
    ∼3.8 Å resolution X-ray crystallographic study of mitochondrial complex I from
    yeast Yarrowia lipotytica. In this review we will discuss what we have learned
    from these studies and what remains to be elucidated.@eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Jame A
      foaf_name: Letts, Jame A
      foaf_surname: Letts
      foaf_workInfoHomepage: http://www.librecat.org/personId=322DA418-F248-11E8-B48F-1D18A9856A87
    orcid: 0000-0002-9864-3586
  - 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: 10.1016/j.sbi.2015.08.008
  bibo_issue: '8'
  bibo_volume: 33
  dct_date: 2015^xs_gYear
  dct_identifier:
  - UT:000365362400016
  dct_language: eng
  dct_publisher: Elsevier@
  dct_title: 'Gaining mass: The structure of respiratory complex I-from bacterial
    towards mitochondrial versions@'
...