---
res:
  bibo_abstract:
  - NADH-ubiquinone oxidoreductase (complex I) is the largest (∼1 MDa) and the least
    characterized complex of the mitochondrial electron transport chain. Because of
    the ease of sample availability, previous work has focused almost exclusively
    on bovine complex I. However, only medium resolution structural analyses of this
    complex have been reported. Working with other mammalian complex I homologues
    is a potential approach for overcoming these limitations. Due to the inherent
    difficulty of expressing large membrane protein complexes, screening of complex
    I homologues is limited to large mammals reared for human consumption. The high
    sequence identity among these available sources may preclude the benefits of screening.
    Here, we report the characterization of complex I purified from Ovis aries (ovine)
    heart mitochondria. All 44 unique subunits of the intact complex were identified
    by mass spectrometry. We identified differences in the subunit composition of
    subcomplexes of ovine complex I as compared with bovine, suggesting differential
    stability of inter-subunit interactions within the complex. Furthermore, the 42-kDa
    subunit, which is easily lost from the bovine enzyme, remains tightly bound to
    ovine complex I. Additionally, we developed a novel purification protocol for
    highly active and stable mitochondrial complex I using the branched-chain detergent
    lauryl maltose neopentyl glycol. Our data demonstrate that, although closely related,
    significant differences exist between the biochemical properties of complex I
    prepared from ovine and bovine mitochondria and that ovine complex I represents
    a suitable alternative target for further structural studies. @eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: James A
      foaf_name: Letts, James 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: Gianluca
      foaf_name: Degliesposti, Gianluca
      foaf_surname: Degliesposti
  - foaf_Person:
      foaf_givenName: Karol
      foaf_name: Fiedorczuk, Karol
      foaf_surname: Fiedorczuk
      foaf_workInfoHomepage: http://www.librecat.org/personId=5BFF67CE-02D1-11E9-B11A-A5A4D7DFFFD0
  - foaf_Person:
      foaf_givenName: Mark
      foaf_name: Skehel, Mark
      foaf_surname: Skehel
  - 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: 10.1074/jbc.M116.735142
  bibo_issue: '47'
  bibo_volume: 291
  dct_date: 2016^xs_gYear
  dct_identifier:
  - UT:000388875500026
  dct_language: eng
  dct_publisher: American Society for Biochemistry and Molecular Biology@
  dct_title: Purification of ovine respiratory complex i results in a highly active
    and stable preparation@
...