---
_id: '1226'
abstract:
- lang: eng
  text: Mitochondrial complex I (also known as NADH:ubiquinone oxidoreductase) contributes
    to cellular energy production by transferring electrons from NADH to ubiquinone
    coupled to proton translocation across the membrane. It is the largest protein
    assembly of the respiratory chain with a total mass of 970 kilodaltons. Here we
    present a nearly complete atomic structure of ovine (Ovis aries) mitochondrial
    complex I at 3.9 Å resolution, solved by cryo-electron microscopy with cross-linking
    and mass-spectrometry mapping experiments. All 14 conserved core subunits and
    31 mitochondria-specific supernumerary subunits are resolved within the L-shaped
    molecule. The hydrophilic matrix arm comprises flavin mononucleotide and 8 iron-sulfur
    clusters involved in electron transfer, and the membrane arm contains 78 transmembrane
    helices, mostly contributed by antiporter-like subunits involved in proton translocation.
    Supernumerary subunits form an interlinked, stabilizing shell around the conserved
    core. Tightly bound lipids (including cardiolipins) further stabilize interactions
    between the hydrophobic subunits. Subunits with possible regulatory roles contain
    additional cofactors, NADPH and two phosphopantetheine molecules, which are shown
    to be involved in inter-subunit interactions. We observe two different conformations
    of the complex, which may be related to the conformationally driven coupling mechanism
    and to the active-deactive transition of the enzyme. Our structure provides insight
    into the mechanism, assembly, maturation and dysfunction of mitochondrial complex
    I, and allows detailed molecular analysis of disease-causing mutations.
article_processing_charge: No
article_type: original
author:
- first_name: Karol
  full_name: Fiedorczuk, Karol
  id: 5BFF67CE-02D1-11E9-B11A-A5A4D7DFFFD0
  last_name: Fiedorczuk
- first_name: James A
  full_name: Letts, James A
  id: 322DA418-F248-11E8-B48F-1D18A9856A87
  last_name: Letts
  orcid: 0000-0002-9864-3586
- first_name: Gianluca
  full_name: Degliesposti, Gianluca
  last_name: Degliesposti
- first_name: Karol
  full_name: Kaszuba, Karol
  id: 3FDF9472-F248-11E8-B48F-1D18A9856A87
  last_name: Kaszuba
- first_name: Mark
  full_name: Skehel, Mark
  last_name: Skehel
- 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: Fiedorczuk K, Letts JA, Degliesposti G, Kaszuba K, Skehel M, Sazanov LA. Atomic
    structure of the entire mammalian mitochondrial complex i. <i>Nature</i>. 2016;538(7625):406-410.
    doi:<a href="https://doi.org/10.1038/nature19794">10.1038/nature19794</a>
  apa: Fiedorczuk, K., Letts, J. A., Degliesposti, G., Kaszuba, K., Skehel, M., &#38;
    Sazanov, L. A. (2016). Atomic structure of the entire mammalian mitochondrial
    complex i. <i>Nature</i>. Nature Publishing Group. <a href="https://doi.org/10.1038/nature19794">https://doi.org/10.1038/nature19794</a>
  chicago: Fiedorczuk, Karol, James A Letts, Gianluca Degliesposti, Karol Kaszuba,
    Mark Skehel, and Leonid A Sazanov. “Atomic Structure of the Entire Mammalian Mitochondrial
    Complex I.” <i>Nature</i>. Nature Publishing Group, 2016. <a href="https://doi.org/10.1038/nature19794">https://doi.org/10.1038/nature19794</a>.
  ieee: K. Fiedorczuk, J. A. Letts, G. Degliesposti, K. Kaszuba, M. Skehel, and L.
    A. Sazanov, “Atomic structure of the entire mammalian mitochondrial complex i,”
    <i>Nature</i>, vol. 538, no. 7625. Nature Publishing Group, pp. 406–410, 2016.
  ista: Fiedorczuk K, Letts JA, Degliesposti G, Kaszuba K, Skehel M, Sazanov LA. 2016.
    Atomic structure of the entire mammalian mitochondrial complex i. Nature. 538(7625),
    406–410.
  mla: Fiedorczuk, Karol, et al. “Atomic Structure of the Entire Mammalian Mitochondrial
    Complex I.” <i>Nature</i>, vol. 538, no. 7625, Nature Publishing Group, 2016,
    pp. 406–10, doi:<a href="https://doi.org/10.1038/nature19794">10.1038/nature19794</a>.
  short: K. Fiedorczuk, J.A. Letts, G. Degliesposti, K. Kaszuba, M. Skehel, L.A. Sazanov,
    Nature 538 (2016) 406–410.
date_created: 2018-12-11T11:50:49Z
date_published: 2016-10-20T00:00:00Z
date_updated: 2021-01-12T06:49:13Z
day: '20'
department:
- _id: LeSa
doi: 10.1038/nature19794
ec_funded: 1
external_id:
  pmid:
  - '27595392'
intvolume: '       538'
issue: '7625'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5164932/
month: '10'
oa: 1
oa_version: Submitted Version
page: 406 - 410
pmid: 1
project:
- _id: 2593EBD6-B435-11E9-9278-68D0E5697425
  name: Atomic-Resolution Structures of Mitochondrial Respiratory Chain Supercomplexes
    (FEBS)
- _id: 2590DB08-B435-11E9-9278-68D0E5697425
  call_identifier: H2020
  grant_number: '701309'
  name: Atomic-Resolution Structures of Mitochondrial Respiratory Chain Supercomplexes
    (H2020)
publication: Nature
publication_status: published
publisher: Nature Publishing Group
publist_id: '6108'
quality_controlled: '1'
scopus_import: 1
status: public
title: Atomic structure of the entire mammalian mitochondrial complex i
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 538
year: '2016'
...
---
_id: '1232'
abstract:
- lang: eng
  text: Mitochondrial electron transport chain complexes are organized into supercomplexes
    responsible for carrying out cellular respiration. Here we present three architectures
    of mammalian (ovine) supercomplexes determined by cryo-electron microscopy. We
    identify two distinct arrangements of supercomplex CICIII 2 CIV (the respirasome)
    - a major 'tight' form and a minor 'loose' form (resolved at the resolution of
    5.8 Å and 6.7 Å, respectively), which may represent different stages in supercomplex
    assembly or disassembly. We have also determined an architecture of supercomplex
    CICIII 2 at 7.8 Å resolution. All observed density can be attributed to the known
    80 subunits of the individual complexes, including 132 transmembrane helices.
    The individual complexes form tight interactions that vary between the architectures,
    with complex IV subunit COX7a switching contact from complex III to complex I.
    The arrangement of active sites within the supercomplex may help control reactive
    oxygen species production. To our knowledge, these are the first complete architectures
    of the dominant, physiologically relevant state of the electron transport chain.
acknowledgement: We thank the MRC LMB Cambridge for the use of the Titan Krios microscope.
  Data processing was performed using the IST high-performance computer cluster. J.A.L.
  holds a long-term fellowship from FEBS. K.F. is partially funded by a MRC UK PhD
  fellowship.
author:
- first_name: James A
  full_name: Letts, James A
  id: 322DA418-F248-11E8-B48F-1D18A9856A87
  last_name: Letts
  orcid: 0000-0002-9864-3586
- first_name: Karol
  full_name: Fiedorczuk, Karol
  id: 5BFF67CE-02D1-11E9-B11A-A5A4D7DFFFD0
  last_name: Fiedorczuk
- 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: Letts JA, Fiedorczuk K, Sazanov LA. The architecture of respiratory supercomplexes.
    <i>Nature</i>. 2016;537(7622):644-648. doi:<a href="https://doi.org/10.1038/nature19774">10.1038/nature19774</a>
  apa: Letts, J. A., Fiedorczuk, K., &#38; Sazanov, L. A. (2016). The architecture
    of respiratory supercomplexes. <i>Nature</i>. Nature Publishing Group. <a href="https://doi.org/10.1038/nature19774">https://doi.org/10.1038/nature19774</a>
  chicago: Letts, James A, Karol Fiedorczuk, and Leonid A Sazanov. “The Architecture
    of Respiratory Supercomplexes.” <i>Nature</i>. Nature Publishing Group, 2016.
    <a href="https://doi.org/10.1038/nature19774">https://doi.org/10.1038/nature19774</a>.
  ieee: J. A. Letts, K. Fiedorczuk, and L. A. Sazanov, “The architecture of respiratory
    supercomplexes,” <i>Nature</i>, vol. 537, no. 7622. Nature Publishing Group, pp.
    644–648, 2016.
  ista: Letts JA, Fiedorczuk K, Sazanov LA. 2016. The architecture of respiratory
    supercomplexes. Nature. 537(7622), 644–648.
  mla: Letts, James A., et al. “The Architecture of Respiratory Supercomplexes.” <i>Nature</i>,
    vol. 537, no. 7622, Nature Publishing Group, 2016, pp. 644–48, doi:<a href="https://doi.org/10.1038/nature19774">10.1038/nature19774</a>.
  short: J.A. Letts, K. Fiedorczuk, L.A. Sazanov, Nature 537 (2016) 644–648.
date_created: 2018-12-11T11:50:51Z
date_published: 2016-09-29T00:00:00Z
date_updated: 2021-01-12T06:49:16Z
day: '29'
department:
- _id: LeSa
doi: 10.1038/nature19774
intvolume: '       537'
issue: '7622'
language:
- iso: eng
month: '09'
oa_version: None
page: 644 - 648
project:
- _id: 2593EBD6-B435-11E9-9278-68D0E5697425
  name: Atomic-Resolution Structures of Mitochondrial Respiratory Chain Supercomplexes
    (FEBS)
publication: Nature
publication_status: published
publisher: Nature Publishing Group
publist_id: '6102'
quality_controlled: '1'
scopus_import: 1
status: public
title: The architecture of respiratory supercomplexes
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 537
year: '2016'
...
---
_id: '1276'
abstract:
- lang: eng
  text: The cytochrome (cyt) bc 1 complex is an integral component of the respiratory
    electron transfer chain sustaining the energy needs of organisms ranging from
    humans to bacteria. Due to its ubiquitous role in the energy metabolism, both
    the oxidation and reduction of the enzyme's substrate co-enzyme Q has been studied
    vigorously. Here, this vast amount of data is reassessed after probing the substrate
    reduction steps at the Q i-site of the cyt bc 1 complex of Rhodobacter capsulatus
    using atomistic molecular dynamics simulations. The simulations suggest that the
    Lys251 side chain could rotate into the Q i-site to facilitate binding of half-protonated
    semiquinone-a reaction intermediate that is potentially formed during substrate
    reduction. At this bent pose, the Lys251 forms a salt bridge with the Asp252,
    thus making direct proton transfer possible. In the neutral state, the lysine
    side chain stays close to the conserved binding location of cardiolipin (CL).
    This back-and-forth motion between the CL and Asp252 indicates that Lys251 functions
    as a proton shuttle controlled by pH-dependent negative feedback. The CL/K/D switching,
    which represents a refinement to the previously described CL/K pathway, fine-tunes
    the proton transfer process. Lastly, the simulation data was used to formulate
    a mechanism for reducing the substrate at the Q i-site.
acknowledgement: We wish to thank CSC – IT Centre for Science (Espoo, Finland) for
  computational resources. For financial support, we wish to thank the Academy of
  Finland (TR, IV and PAP; Center of Excellence in Biomembrane Research (IV, TR)),
  the Finnish Doctoral Programme in Computational Sciences (KK), the Sigrid Juselius
  Foundation (IV), the Paulo Foundation (PAP), and the European Research Council (IV,
  TR; Advanced Grant project CROWDED-PRO-LIPIDS). AO acknowledges The Wellcome Trust
  International Senior Research Fellowship.
article_number: '33607'
author:
- first_name: Pekka
  full_name: Postila, Pekka
  last_name: Postila
- first_name: Karol
  full_name: Kaszuba, Karol
  id: 3FDF9472-F248-11E8-B48F-1D18A9856A87
  last_name: Kaszuba
- first_name: Patryk
  full_name: Kuleta, Patryk
  last_name: Kuleta
- first_name: Ilpo
  full_name: Vattulainen, Ilpo
  last_name: Vattulainen
- first_name: Marcin
  full_name: Sarewicz, Marcin
  last_name: Sarewicz
- first_name: Artur
  full_name: Osyczka, Artur
  last_name: Osyczka
- first_name: Tomasz
  full_name: Róg, Tomasz
  last_name: Róg
citation:
  ama: Postila P, Kaszuba K, Kuleta P, et al. Atomistic determinants of co-enzyme
    Q reduction at the Qi-site of the cytochrome bc1 complex. <i>Scientific Reports</i>.
    2016;6. doi:<a href="https://doi.org/10.1038/srep33607">10.1038/srep33607</a>
  apa: Postila, P., Kaszuba, K., Kuleta, P., Vattulainen, I., Sarewicz, M., Osyczka,
    A., &#38; Róg, T. (2016). Atomistic determinants of co-enzyme Q reduction at the
    Qi-site of the cytochrome bc1 complex. <i>Scientific Reports</i>. Nature Publishing
    Group. <a href="https://doi.org/10.1038/srep33607">https://doi.org/10.1038/srep33607</a>
  chicago: Postila, Pekka, Karol Kaszuba, Patryk Kuleta, Ilpo Vattulainen, Marcin
    Sarewicz, Artur Osyczka, and Tomasz Róg. “Atomistic Determinants of Co-Enzyme
    Q Reduction at the Qi-Site of the Cytochrome Bc1 Complex.” <i>Scientific Reports</i>.
    Nature Publishing Group, 2016. <a href="https://doi.org/10.1038/srep33607">https://doi.org/10.1038/srep33607</a>.
  ieee: P. Postila <i>et al.</i>, “Atomistic determinants of co-enzyme Q reduction
    at the Qi-site of the cytochrome bc1 complex,” <i>Scientific Reports</i>, vol.
    6. Nature Publishing Group, 2016.
  ista: Postila P, Kaszuba K, Kuleta P, Vattulainen I, Sarewicz M, Osyczka A, Róg
    T. 2016. Atomistic determinants of co-enzyme Q reduction at the Qi-site of the
    cytochrome bc1 complex. Scientific Reports. 6, 33607.
  mla: Postila, Pekka, et al. “Atomistic Determinants of Co-Enzyme Q Reduction at
    the Qi-Site of the Cytochrome Bc1 Complex.” <i>Scientific Reports</i>, vol. 6,
    33607, Nature Publishing Group, 2016, doi:<a href="https://doi.org/10.1038/srep33607">10.1038/srep33607</a>.
  short: P. Postila, K. Kaszuba, P. Kuleta, I. Vattulainen, M. Sarewicz, A. Osyczka,
    T. Róg, Scientific Reports 6 (2016).
date_created: 2018-12-11T11:51:05Z
date_published: 2016-09-26T00:00:00Z
date_updated: 2021-01-12T06:49:34Z
day: '26'
ddc:
- '576'
department:
- _id: LeSa
doi: 10.1038/srep33607
file:
- access_level: open_access
  checksum: 07c591c1250ebef266333cbc3228b4dd
  content_type: application/pdf
  creator: system
  date_created: 2018-12-12T10:17:09Z
  date_updated: 2020-07-14T12:44:42Z
  file_id: '5261'
  file_name: IST-2016-691-v1+1_srep33607.pdf
  file_size: 1960563
  relation: main_file
file_date_updated: 2020-07-14T12:44:42Z
has_accepted_license: '1'
intvolume: '         6'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
publication: Scientific Reports
publication_status: published
publisher: Nature Publishing Group
publist_id: '6040'
pubrep_id: '691'
quality_controlled: '1'
scopus_import: 1
status: public
title: Atomistic determinants of co-enzyme Q reduction at the Qi-site of the cytochrome
  bc1 complex
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 6
year: '2016'
...
---
_id: '1288'
abstract:
- lang: eng
  text: Respiratory complex I transfers electrons from NADH to quinone, utilizing
    the reaction energy to translocate protons across the membrane. It is a key enzyme
    of the respiratory chain of many prokaryotic and most eukaryotic organisms. The
    reversible NADH oxidation reaction is facilitated in complex I by non-covalently
    bound flavin mononucleotide (FMN). Here we report that the catalytic activity
    of E. coli complex I with artificial electron acceptors potassium ferricyanide
    (FeCy) and hexaamineruthenium (HAR) is significantly inhibited in the enzyme pre-reduced
    by NADH. Further, we demonstrate that the inhibition is caused by reversible dissociation
    of FMN. The binding constant (Kd) for FMN increases from the femto- or picomolar
    range in oxidized complex I to the nanomolar range in the NADH reduced enzyme,
    with an FMN dissociation time constant of ~ 5 s. The oxidation state of complex
    I, rather than that of FMN, proved critical to the dissociation. Such dissociation
    is not observed with the T. thermophilus enzyme and our analysis suggests that
    the difference may be due to the unusually high redox potential of Fe-S cluster
    N1a in E. coli. It is possible that the enzyme attenuates ROS production in vivo
    by releasing FMN under highly reducing conditions.
acknowledgement: This work was funded by the UK Medical Research Council.
author:
- first_name: Peter
  full_name: Holt, Peter
  last_name: Holt
- first_name: Rouslan
  full_name: Efremov, Rouslan
  last_name: Efremov
- first_name: Eiko
  full_name: Nakamaru Ogiso, Eiko
  last_name: Nakamaru Ogiso
- 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: Holt P, Efremov R, Nakamaru Ogiso E, Sazanov LA. Reversible FMN dissociation
    from Escherichia coli respiratory complex I. <i>Biochimica et Biophysica Acta
    - Bioenergetics</i>. 2016;1857(11):1777-1785. doi:<a href="https://doi.org/10.1016/j.bbabio.2016.08.008">10.1016/j.bbabio.2016.08.008</a>
  apa: Holt, P., Efremov, R., Nakamaru Ogiso, E., &#38; Sazanov, L. A. (2016). Reversible
    FMN dissociation from Escherichia coli respiratory complex I. <i>Biochimica et
    Biophysica Acta - Bioenergetics</i>. Elsevier. <a href="https://doi.org/10.1016/j.bbabio.2016.08.008">https://doi.org/10.1016/j.bbabio.2016.08.008</a>
  chicago: Holt, Peter, Rouslan Efremov, Eiko Nakamaru Ogiso, and Leonid A Sazanov.
    “Reversible FMN Dissociation from Escherichia Coli Respiratory Complex I.” <i>Biochimica
    et Biophysica Acta - Bioenergetics</i>. Elsevier, 2016. <a href="https://doi.org/10.1016/j.bbabio.2016.08.008">https://doi.org/10.1016/j.bbabio.2016.08.008</a>.
  ieee: P. Holt, R. Efremov, E. Nakamaru Ogiso, and L. A. Sazanov, “Reversible FMN
    dissociation from Escherichia coli respiratory complex I,” <i>Biochimica et Biophysica
    Acta - Bioenergetics</i>, vol. 1857, no. 11. Elsevier, pp. 1777–1785, 2016.
  ista: Holt P, Efremov R, Nakamaru Ogiso E, Sazanov LA. 2016. Reversible FMN dissociation
    from Escherichia coli respiratory complex I. Biochimica et Biophysica Acta - Bioenergetics.
    1857(11), 1777–1785.
  mla: Holt, Peter, et al. “Reversible FMN Dissociation from Escherichia Coli Respiratory
    Complex I.” <i>Biochimica et Biophysica Acta - Bioenergetics</i>, vol. 1857, no.
    11, Elsevier, 2016, pp. 1777–85, doi:<a href="https://doi.org/10.1016/j.bbabio.2016.08.008">10.1016/j.bbabio.2016.08.008</a>.
  short: P. Holt, R. Efremov, E. Nakamaru Ogiso, L.A. Sazanov, Biochimica et Biophysica
    Acta - Bioenergetics 1857 (2016) 1777–1785.
date_created: 2018-12-11T11:51:09Z
date_published: 2016-11-01T00:00:00Z
date_updated: 2021-01-12T06:49:38Z
day: '01'
department:
- _id: LeSa
doi: 10.1016/j.bbabio.2016.08.008
intvolume: '      1857'
issue: '11'
language:
- iso: eng
month: '11'
oa_version: None
page: 1777 - 1785
publication: Biochimica et Biophysica Acta - Bioenergetics
publication_status: published
publisher: Elsevier
publist_id: '6028'
quality_controlled: '1'
scopus_import: 1
status: public
title: Reversible FMN dissociation from Escherichia coli respiratory complex I
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 1857
year: '2016'
...
---
_id: '1638'
abstract:
- lang: eng
  text: The mitochondrial respiratory chain, also known as the electron transport
    chain (ETC), is crucial to life, and energy production in the form of ATP is the
    main mitochondrial function. Three proton-translocating enzymes of the ETC, namely
    complexes I, III and IV, generate proton motive force, which in turn drives ATP
    synthase (complex V). The atomic structures and basic mechanisms of most respiratory
    complexes have previously been established, with the exception of complex I, the
    largest complex in the ETC. Recently, the crystal structure of the entire complex
    I was solved using a bacterial enzyme. The structure provided novel insights into
    the core architecture of the complex, the electron transfer and proton translocation
    pathways, as well as the mechanism that couples these two processes.
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. A giant molecular proton pump: structure and mechanism of respiratory
    complex I. <i>Nature Reviews Molecular Cell Biology</i>. 2015;16(6):375-388. doi:<a
    href="https://doi.org/10.1038/nrm3997">10.1038/nrm3997</a>'
  apa: 'Sazanov, L. A. (2015). A giant molecular proton pump: structure and mechanism
    of respiratory complex I. <i>Nature Reviews Molecular Cell Biology</i>. Nature
    Publishing Group. <a href="https://doi.org/10.1038/nrm3997">https://doi.org/10.1038/nrm3997</a>'
  chicago: 'Sazanov, Leonid A. “A Giant Molecular Proton Pump: Structure and Mechanism
    of Respiratory Complex I.” <i>Nature Reviews Molecular Cell Biology</i>. Nature
    Publishing Group, 2015. <a href="https://doi.org/10.1038/nrm3997">https://doi.org/10.1038/nrm3997</a>.'
  ieee: 'L. A. Sazanov, “A giant molecular proton pump: structure and mechanism of
    respiratory complex I,” <i>Nature Reviews Molecular Cell Biology</i>, vol. 16,
    no. 6. Nature Publishing Group, pp. 375–388, 2015.'
  ista: 'Sazanov LA. 2015. A giant molecular proton pump: structure and mechanism
    of respiratory complex I. Nature Reviews Molecular Cell Biology. 16(6), 375–388.'
  mla: 'Sazanov, Leonid A. “A Giant Molecular Proton Pump: Structure and Mechanism
    of Respiratory Complex I.” <i>Nature Reviews Molecular Cell Biology</i>, vol.
    16, no. 6, Nature Publishing Group, 2015, pp. 375–88, doi:<a href="https://doi.org/10.1038/nrm3997">10.1038/nrm3997</a>.'
  short: L.A. Sazanov, Nature Reviews Molecular Cell Biology 16 (2015) 375–388.
date_created: 2018-12-11T11:53:11Z
date_published: 2015-05-22T00:00:00Z
date_updated: 2021-01-12T06:52:10Z
day: '22'
department:
- _id: LeSa
doi: 10.1038/nrm3997
intvolume: '        16'
issue: '6'
language:
- iso: eng
month: '05'
oa_version: None
page: 375 - 388
publication: Nature Reviews Molecular Cell Biology
publication_status: published
publisher: Nature Publishing Group
publist_id: '5517'
quality_controlled: '1'
scopus_import: 1
status: public
title: 'A giant molecular proton pump: structure and mechanism of respiratory complex
  I'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 16
year: '2015'
...
---
_id: '1683'
abstract:
- lang: eng
  text: 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.
author:
- first_name: Jame A
  full_name: Letts, Jame A
  id: 322DA418-F248-11E8-B48F-1D18A9856A87
  last_name: Letts
  orcid: 0000-0002-9864-3586
- 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: 'Letts JA, Sazanov LA. Gaining mass: The structure of respiratory complex I-from
    bacterial towards mitochondrial versions. <i>Current Opinion in Structural Biology</i>.
    2015;33(8):135-145. doi:<a href="https://doi.org/10.1016/j.sbi.2015.08.008">10.1016/j.sbi.2015.08.008</a>'
  apa: 'Letts, J. A., &#38; Sazanov, L. A. (2015). Gaining mass: The structure of
    respiratory complex I-from bacterial towards mitochondrial versions. <i>Current
    Opinion in Structural Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.sbi.2015.08.008">https://doi.org/10.1016/j.sbi.2015.08.008</a>'
  chicago: 'Letts, James A, and Leonid A Sazanov. “Gaining Mass: The Structure of
    Respiratory Complex I-from Bacterial towards Mitochondrial Versions.” <i>Current
    Opinion in Structural Biology</i>. Elsevier, 2015. <a href="https://doi.org/10.1016/j.sbi.2015.08.008">https://doi.org/10.1016/j.sbi.2015.08.008</a>.'
  ieee: 'J. A. Letts and L. A. Sazanov, “Gaining mass: The structure of respiratory
    complex I-from bacterial towards mitochondrial versions,” <i>Current Opinion in
    Structural Biology</i>, vol. 33, no. 8. Elsevier, pp. 135–145, 2015.'
  ista: 'Letts JA, Sazanov LA. 2015. Gaining mass: The structure of respiratory complex
    I-from bacterial towards mitochondrial versions. Current Opinion in Structural
    Biology. 33(8), 135–145.'
  mla: 'Letts, James A., and Leonid A. Sazanov. “Gaining Mass: The Structure of Respiratory
    Complex I-from Bacterial towards Mitochondrial Versions.” <i>Current Opinion in
    Structural Biology</i>, vol. 33, no. 8, Elsevier, 2015, pp. 135–45, doi:<a href="https://doi.org/10.1016/j.sbi.2015.08.008">10.1016/j.sbi.2015.08.008</a>.'
  short: J.A. Letts, L.A. Sazanov, Current Opinion in Structural Biology 33 (2015)
    135–145.
date_created: 2018-12-11T11:53:27Z
date_published: 2015-08-01T00:00:00Z
date_updated: 2021-01-12T06:52:30Z
day: '01'
department:
- _id: LeSa
doi: 10.1016/j.sbi.2015.08.008
intvolume: '        33'
issue: '8'
language:
- iso: eng
month: '08'
oa_version: None
page: 135 - 145
publication: Current Opinion in Structural Biology
publication_status: published
publisher: Elsevier
publist_id: '5465'
quality_controlled: '1'
scopus_import: 1
status: public
title: 'Gaining mass: The structure of respiratory complex I-from bacterial towards
  mitochondrial versions'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 33
year: '2015'
...