---
res:
  bibo_abstract:
  - The mechanism coupling electron transfer and proton pumping in respiratory complex
    I (NADH-ubiquinone oxidoreductase) has not been established, but it has been suggested
    that it involves conformational changes. Here, the influence of substrates on
    the conformation of purified complex I from Escherichia coli was studied by cross-linking
    and electron microscopy. When a zero-length cross-linking reagent was used, the
    presence of NAD(P)H, in contrast to that of NAD+, prevented the formation of cross-links
    between the hydrophilic subunits of the complex, including NuoB, NuoI, and NuoCD.
    Comparisons using different cross-linkers suggested that NuoB, which is likely
    to coordinate the key iron-sulfur cluster N2, is the most mobile subunit. The
    presence of NAD(P)H led also to enhanced proteolysis of subunit NuoG. These data
    indicate that upon NAD(P)H binding, the peripheral arm of the complex adopts a
    more open conformation, with increased distances between subunits. Single particle
    analysis showed the nature of this conformational change. The enzyme retains its
    L-shape in the presence of NADH, but exhibits a significantly more open or expanded
    structure both in the peripheral arm and, unexpectedly, in the membrane domain
    also.@eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Aygun
      foaf_name: Mamedova, Aygun A
      foaf_surname: Mamedova
  - foaf_Person:
      foaf_givenName: Peter
      foaf_name: Holt, Peter J
      foaf_surname: Holt
  - foaf_Person:
      foaf_givenName: Joe
      foaf_name: Carroll, Joe D
      foaf_surname: Carroll
  - foaf_Person:
      foaf_givenName: Leonid A
      foaf_name: Leonid Sazanov
      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.M401539200
  bibo_issue: '22'
  bibo_volume: 279
  dct_date: 2004^xs_gYear
  dct_publisher: American Society for Biochemistry and Molecular Biology@
  dct_title: Substrate-induced conformational change in bacterial complex I@
...