---
_id: '444'
abstract:
- lang: eng
  text: Complex I (NADH:ubiquinone oxidoreductase) plays a central role in cellular
    energy generation, contributing to the proton motive force used to produce ATP.
    It couples the transfer of two electrons between NADH and quinone to translocation
    of four protons across the membrane. It is the largest protein assembly of bacterial
    and mitochondrial respiratory chains, composed, in mammals, of up to 45 subunits
    with a total molecular weight of ∼1 MDa. Bacterial enzyme is about half the size,
    providing the important “minimal” model of complex I. The l-shaped complex consists
    of a hydrophilic arm, where electron transfer occurs, and a membrane arm, where
    proton translocation takes place. Previously, we have solved the crystal structures
    of the hydrophilic domain of complex I from Thermus thermophilus and of the membrane
    domain from Escherichia coli, followed by the atomic structure of intact, entire
    complex I from T. thermophilus. Recently, we have solved by cryo-EM a first complete
    atomic structure of mammalian (ovine) mitochondrial complex I. Core subunits are
    well conserved from the bacterial version, whilst supernumerary subunits form
    an interlinked, stabilizing shell around the core. Subunits containing additional
    cofactors, including Zn ion, NADPH and phosphopantetheine, probably have regulatory
    roles. Dysfunction of mitochondrial complex I is implicated in many human neurodegenerative
    diseases. The structure of mammalian enzyme provides many insights into complex
    I mechanism, assembly, maturation and dysfunction, allowing detailed molecular
    analysis of disease-causing mutations.
author:
- first_name: Leonid A
  full_name: Sazanov, Leonid A
  id: 338D39FE-F248-11E8-B48F-1D18A9856A87
  last_name: Sazanov
  orcid: 0000-0002-0977-7989
citation:
  ama: 'Sazanov LA. Structure of respiratory complex I: “Minimal” bacterial and “de
    luxe” mammalian versions. In: Wikström M, ed. <i>Mechanisms of Primary Energy
    Transduction in Biology </i>. Mechanisms of Primary Energy Transduction in Biology
    . Royal Society of Chemistry; 2017:25-59. doi:<a href="https://doi.org/10.1039/9781788010405-00025">10.1039/9781788010405-00025</a>'
  apa: 'Sazanov, L. A. (2017). Structure of respiratory complex I: “Minimal” bacterial
    and “de luxe” mammalian versions. In M. Wikström (Ed.), <i>Mechanisms of primary
    energy transduction in biology </i> (pp. 25–59). Royal Society of Chemistry. <a
    href="https://doi.org/10.1039/9781788010405-00025">https://doi.org/10.1039/9781788010405-00025</a>'
  chicago: 'Sazanov, Leonid A. “Structure of Respiratory Complex I: ‘Minimal’ Bacterial
    and ‘de Luxe’ Mammalian Versions.” In <i>Mechanisms of Primary Energy Transduction
    in Biology </i>, edited by Mårten Wikström, 25–59. Mechanisms of Primary Energy
    Transduction in Biology . Royal Society of Chemistry, 2017. <a href="https://doi.org/10.1039/9781788010405-00025">https://doi.org/10.1039/9781788010405-00025</a>.'
  ieee: 'L. A. Sazanov, “Structure of respiratory complex I: ‘Minimal’ bacterial and
    ‘de luxe’ mammalian versions,” in <i>Mechanisms of primary energy transduction
    in biology </i>, M. Wikström, Ed. Royal Society of Chemistry, 2017, pp. 25–59.'
  ista: 'Sazanov LA. 2017.Structure of respiratory complex I: “Minimal” bacterial
    and “de luxe” mammalian versions. In: Mechanisms of primary energy transduction
    in biology . , 25–59.'
  mla: 'Sazanov, Leonid A. “Structure of Respiratory Complex I: ‘Minimal’ Bacterial
    and ‘de Luxe’ Mammalian Versions.” <i>Mechanisms of Primary Energy Transduction
    in Biology </i>, edited by Mårten Wikström, Royal Society of Chemistry, 2017,
    pp. 25–59, doi:<a href="https://doi.org/10.1039/9781788010405-00025">10.1039/9781788010405-00025</a>.'
  short: L.A. Sazanov, in:, M. Wikström (Ed.), Mechanisms of Primary Energy Transduction
    in Biology , Royal Society of Chemistry, 2017, pp. 25–59.
date_created: 2018-12-11T11:46:30Z
date_published: 2017-11-29T00:00:00Z
date_updated: 2021-01-12T07:56:59Z
day: '29'
department:
- _id: LeSa
doi: 10.1039/9781788010405-00025
editor:
- first_name: Mårten
  full_name: Wikström, Mårten
  last_name: Wikström
language:
- iso: eng
month: '11'
oa_version: None
page: 25 - 59
publication: 'Mechanisms of primary energy transduction in biology '
publication_identifier:
  isbn:
  - 978-1-78262-865-1
publication_status: published
publisher: Royal Society of Chemistry
publist_id: '7379'
quality_controlled: '1'
series_title: 'Mechanisms of Primary Energy Transduction in Biology '
status: public
title: 'Structure of respiratory complex I: “Minimal” bacterial and “de luxe” mammalian
  versions'
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2017'
...