---
_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: '1521'
abstract:
- lang: eng
  text: Complex I (NADH:ubiquinone oxidoreductase) plays a central role in cellular
    energy production, coupling electron transfer between NADH and quinone to proton
    translocation. It is the largest protein assembly of respiratory chains and one
    of the most elaborate redox membrane proteins known. Bacterial enzyme is about
    half the size of mitochondrial and thus provides its important &quot;minimal&quot;
    model. Dysfunction of mitochondrial complex I is implicated in many human neurodegenerative
    diseases. The L-shaped complex consists of a hydrophilic arm, where electron transfer
    occurs, and a membrane arm, where proton translocation takes place. We have solved
    the crystal structures of the hydrophilic domain of complex I from Thermus thermophilus,
    the membrane domain from Escherichia coli and recently of the intact, entire complex
    I from T. thermophilus (536. kDa, 16 subunits, 9 iron-sulphur clusters, 64 transmembrane
    helices). The 95. Å long electron transfer pathway through the enzyme proceeds
    from the primary electron acceptor flavin mononucleotide through seven conserved
    Fe-S clusters to the unusual elongated quinone-binding site at the interface with
    the membrane domain. Four putative proton translocation channels are found in
    the membrane domain, all linked by the central flexible axis containing charged
    residues. The redox energy of electron transfer is coupled to proton translocation
    by the as yet undefined mechanism proposed to involve long-range conformational
    changes. This article is part of a Special Issue entitled Respiratory complex
    I, edited by Volker Zickermann and Ulrich Brandt.
acknowledgement: funded by the Medical Research Council (Grant number MC_U105674180)
author:
- first_name: John
  full_name: Berrisford, John
  last_name: Berrisford
- first_name: Rozbeh
  full_name: Baradaran, Rozbeh
  last_name: Baradaran
- 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: Berrisford J, Baradaran R, Sazanov LA. Structure of bacterial respiratory complex
    I. <i>Biochimica et Biophysica Acta - Bioenergetics</i>. 2016;1857(7):892-901.
    doi:<a href="https://doi.org/10.1016/j.bbabio.2016.01.012">10.1016/j.bbabio.2016.01.012</a>
  apa: Berrisford, J., Baradaran, R., &#38; Sazanov, L. A. (2016). Structure of bacterial
    respiratory complex I. <i>Biochimica et Biophysica Acta - Bioenergetics</i>. Elsevier.
    <a href="https://doi.org/10.1016/j.bbabio.2016.01.012">https://doi.org/10.1016/j.bbabio.2016.01.012</a>
  chicago: Berrisford, John, Rozbeh Baradaran, and Leonid A Sazanov. “Structure of
    Bacterial Respiratory Complex I.” <i>Biochimica et Biophysica Acta - Bioenergetics</i>.
    Elsevier, 2016. <a href="https://doi.org/10.1016/j.bbabio.2016.01.012">https://doi.org/10.1016/j.bbabio.2016.01.012</a>.
  ieee: J. Berrisford, R. Baradaran, and L. A. Sazanov, “Structure of bacterial respiratory
    complex I,” <i>Biochimica et Biophysica Acta - Bioenergetics</i>, vol. 1857, no.
    7. Elsevier, pp. 892–901, 2016.
  ista: Berrisford J, Baradaran R, Sazanov LA. 2016. Structure of bacterial respiratory
    complex I. Biochimica et Biophysica Acta - Bioenergetics. 1857(7), 892–901.
  mla: Berrisford, John, et al. “Structure of Bacterial Respiratory Complex I.” <i>Biochimica
    et Biophysica Acta - Bioenergetics</i>, vol. 1857, no. 7, Elsevier, 2016, pp.
    892–901, doi:<a href="https://doi.org/10.1016/j.bbabio.2016.01.012">10.1016/j.bbabio.2016.01.012</a>.
  short: J. Berrisford, R. Baradaran, L.A. Sazanov, Biochimica et Biophysica Acta
    - Bioenergetics 1857 (2016) 892–901.
date_created: 2018-12-11T11:52:30Z
date_published: 2016-07-01T00:00:00Z
date_updated: 2021-01-12T06:51:21Z
day: '01'
department:
- _id: LeSa
doi: 10.1016/j.bbabio.2016.01.012
intvolume: '      1857'
issue: '7'
language:
- iso: eng
month: '07'
oa_version: None
page: 892 - 901
publication: Biochimica et Biophysica Acta - Bioenergetics
publication_status: published
publisher: Elsevier
publist_id: '5654'
quality_controlled: '1'
scopus_import: 1
status: public
title: Structure of bacterial respiratory complex I
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 1857
year: '2016'
...
---
_id: '1186'
abstract:
- lang: eng
  text: The human pathogen Streptococcus pneumoniae is decorated with a special class
    of surface-proteins known as choline-binding proteins (CBPs) attached to phosphorylcholine
    (PCho) moieties from cell-wall teichoic acids. By a combination of X-ray crystallography,
    NMR, molecular dynamics techniques and in vivo virulence and phagocytosis studies,
    we provide structural information of choline-binding protein L (CbpL) and demonstrate
    its impact on pneumococcal pathogenesis and immune evasion. CbpL is a very elongated
    three-module protein composed of (i) an Excalibur Ca 2+ -binding domain -reported
    in this work for the very first time-, (ii) an unprecedented anchorage module
    showing alternate disposition of canonical and non-canonical choline-binding sites
    that allows vine-like binding of fully-PCho-substituted teichoic acids (with two
    choline moieties per unit), and (iii) a Ltp-Lipoprotein domain. Our structural
    and infection assays indicate an important role of the whole multimodular protein
    allowing both to locate CbpL at specific places on the cell wall and to interact
    with host components in order to facilitate pneumococcal lung infection and transmigration
    from nasopharynx to the lungs and blood. CbpL implication in both resistance against
    killing by phagocytes and pneumococcal pathogenesis further postulate this surface-protein
    as relevant among the pathogenic arsenal of the pneumococcus.
acknowledgement: We gratefully acknowledge Karsta Barnekow and Kristine Sievert-Giermann,
  for technical assistance and Lothar Petruschka for in silico analysis (all Dept.
  of Genetics, University of Greifswald). We are further grateful to the staff from
  SLS synchrotron beamline for help in data collection. This work was supported by
  grants from the Deutsche Forschungsgemeinschaft DFG GRK 1870 (to SH) and the Spanish
  Ministry of Economy and Competitiveness (BFU2014-59389-P to JAH, CTQ2014-52633-P
  to MB and SAF2012-39760-C02-02 to FG) and S2010/BMD-2457 (Community of Madrid to
  JAH and FG).
article_number: '38094'
author:
- first_name: Javier
  full_name: Gutierrez-Fernandez, Javier
  id: 3D9511BA-F248-11E8-B48F-1D18A9856A87
  last_name: Gutierrez-Fernandez
- first_name: Malek
  full_name: Saleh, Malek
  last_name: Saleh
- first_name: Martín
  full_name: Alcorlo, Martín
  last_name: Alcorlo
- first_name: Alejandro
  full_name: Gómez Mejóa, Alejandro
  last_name: Gómez Mejóa
- first_name: David
  full_name: Pantoja Uceda, David
  last_name: Pantoja Uceda
- first_name: Miguel
  full_name: Treviño, Miguel
  last_name: Treviño
- first_name: Franziska
  full_name: Vob, Franziska
  last_name: Vob
- first_name: Mohammed
  full_name: Abdullah, Mohammed
  last_name: Abdullah
- first_name: Sergio
  full_name: Galán Bartual, Sergio
  last_name: Galán Bartual
- first_name: Jolien
  full_name: Seinen, Jolien
  last_name: Seinen
- first_name: Pedro
  full_name: Sánchez Murcia, Pedro
  last_name: Sánchez Murcia
- first_name: Federico
  full_name: Gago, Federico
  last_name: Gago
- first_name: Marta
  full_name: Bruix, Marta
  last_name: Bruix
- first_name: Sven
  full_name: Hammerschmidt, Sven
  last_name: Hammerschmidt
- first_name: Juan
  full_name: Hermoso, Juan
  last_name: Hermoso
citation:
  ama: Gutierrez-Fernandez J, Saleh M, Alcorlo M, et al. Modular architecture and
    unique teichoic acid recognition features of choline-binding protein L CbpL contributing
    to pneumococcal pathogenesis. <i>Scientific Reports</i>. 2016;6. doi:<a href="https://doi.org/10.1038/srep38094">10.1038/srep38094</a>
  apa: Gutierrez-Fernandez, J., Saleh, M., Alcorlo, M., Gómez Mejóa, A., Pantoja Uceda,
    D., Treviño, M., … Hermoso, J. (2016). Modular architecture and unique teichoic
    acid recognition features of choline-binding protein L CbpL contributing to pneumococcal
    pathogenesis. <i>Scientific Reports</i>. Nature Publishing Group. <a href="https://doi.org/10.1038/srep38094">https://doi.org/10.1038/srep38094</a>
  chicago: Gutierrez-Fernandez, Javier, Malek Saleh, Martín Alcorlo, Alejandro Gómez
    Mejóa, David Pantoja Uceda, Miguel Treviño, Franziska Vob, et al. “Modular Architecture
    and Unique Teichoic Acid Recognition Features of Choline-Binding Protein L CbpL
    Contributing to Pneumococcal Pathogenesis.” <i>Scientific Reports</i>. Nature
    Publishing Group, 2016. <a href="https://doi.org/10.1038/srep38094">https://doi.org/10.1038/srep38094</a>.
  ieee: J. Gutierrez-Fernandez <i>et al.</i>, “Modular architecture and unique teichoic
    acid recognition features of choline-binding protein L CbpL contributing to pneumococcal
    pathogenesis,” <i>Scientific Reports</i>, vol. 6. Nature Publishing Group, 2016.
  ista: Gutierrez-Fernandez J, Saleh M, Alcorlo M, Gómez Mejóa A, Pantoja Uceda D,
    Treviño M, Vob F, Abdullah M, Galán Bartual S, Seinen J, Sánchez Murcia P, Gago
    F, Bruix M, Hammerschmidt S, Hermoso J. 2016. Modular architecture and unique
    teichoic acid recognition features of choline-binding protein L CbpL contributing
    to pneumococcal pathogenesis. Scientific Reports. 6, 38094.
  mla: Gutierrez-Fernandez, Javier, et al. “Modular Architecture and Unique Teichoic
    Acid Recognition Features of Choline-Binding Protein L CbpL Contributing to Pneumococcal
    Pathogenesis.” <i>Scientific Reports</i>, vol. 6, 38094, Nature Publishing Group,
    2016, doi:<a href="https://doi.org/10.1038/srep38094">10.1038/srep38094</a>.
  short: J. Gutierrez-Fernandez, M. Saleh, M. Alcorlo, A. Gómez Mejóa, D. Pantoja
    Uceda, M. Treviño, F. Vob, M. Abdullah, S. Galán Bartual, J. Seinen, P. Sánchez
    Murcia, F. Gago, M. Bruix, S. Hammerschmidt, J. Hermoso, Scientific Reports 6
    (2016).
date_created: 2018-12-11T11:50:36Z
date_published: 2016-12-05T00:00:00Z
date_updated: 2021-01-12T06:48:56Z
day: '05'
ddc:
- '576'
- '610'
department:
- _id: LeSa
doi: 10.1038/srep38094
file:
- access_level: open_access
  checksum: e007d78b483bc59bf5ab98e9d42a6ec1
  content_type: application/pdf
  creator: system
  date_created: 2018-12-12T10:10:18Z
  date_updated: 2020-07-14T12:44:37Z
  file_id: '4804'
  file_name: IST-2017-735-v1+1_srep38094.pdf
  file_size: 2716045
  relation: main_file
file_date_updated: 2020-07-14T12:44:37Z
has_accepted_license: '1'
intvolume: '         6'
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '12'
oa: 1
oa_version: Published Version
publication: Scientific Reports
publication_status: published
publisher: Nature Publishing Group
publist_id: '6167'
pubrep_id: '735'
quality_controlled: '1'
scopus_import: 1
status: public
title: Modular architecture and unique teichoic acid recognition features of choline-binding
  protein L CbpL contributing to pneumococcal pathogenesis
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: '1209'
abstract:
- lang: eng
  text: '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. '
acknowledgement: "J.A.S supported in part by a Medical Research D.G.Council UK Ph.D.
  fellowship.\r\nThis work was supported in part by European Union's 2020 Research
  and Innovation Program under Grant 701309. \r\n"
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: Gianluca
  full_name: Degliesposti, Gianluca
  last_name: Degliesposti
- first_name: Karol
  full_name: Fiedorczuk, Karol
  id: 5BFF67CE-02D1-11E9-B11A-A5A4D7DFFFD0
  last_name: Fiedorczuk
- 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: Letts JA, Degliesposti G, Fiedorczuk K, Skehel M, Sazanov LA. Purification
    of ovine respiratory complex i results in a highly active and stable preparation.
    <i>Journal of Biological Chemistry</i>. 2016;291(47):24657-24675. doi:<a href="https://doi.org/10.1074/jbc.M116.735142">10.1074/jbc.M116.735142</a>
  apa: Letts, J. A., Degliesposti, G., Fiedorczuk, K., Skehel, M., &#38; Sazanov,
    L. A. (2016). Purification of ovine respiratory complex i results in a highly
    active and stable preparation. <i>Journal of Biological Chemistry</i>. American
    Society for Biochemistry and Molecular Biology. <a href="https://doi.org/10.1074/jbc.M116.735142">https://doi.org/10.1074/jbc.M116.735142</a>
  chicago: Letts, James A, Gianluca Degliesposti, Karol Fiedorczuk, Mark Skehel, and
    Leonid A Sazanov. “Purification of Ovine Respiratory Complex i Results in a Highly
    Active and Stable Preparation.” <i>Journal of Biological Chemistry</i>. American
    Society for Biochemistry and Molecular Biology, 2016. <a href="https://doi.org/10.1074/jbc.M116.735142">https://doi.org/10.1074/jbc.M116.735142</a>.
  ieee: J. A. Letts, G. Degliesposti, K. Fiedorczuk, M. Skehel, and L. A. Sazanov,
    “Purification of ovine respiratory complex i results in a highly active and stable
    preparation,” <i>Journal of Biological Chemistry</i>, vol. 291, no. 47. American
    Society for Biochemistry and Molecular Biology, pp. 24657–24675, 2016.
  ista: Letts JA, Degliesposti G, Fiedorczuk K, Skehel M, Sazanov LA. 2016. Purification
    of ovine respiratory complex i results in a highly active and stable preparation.
    Journal of Biological Chemistry. 291(47), 24657–24675.
  mla: Letts, James A., et al. “Purification of Ovine Respiratory Complex i Results
    in a Highly Active and Stable Preparation.” <i>Journal of Biological Chemistry</i>,
    vol. 291, no. 47, American Society for Biochemistry and Molecular Biology, 2016,
    pp. 24657–75, doi:<a href="https://doi.org/10.1074/jbc.M116.735142">10.1074/jbc.M116.735142</a>.
  short: J.A. Letts, G. Degliesposti, K. Fiedorczuk, M. Skehel, L.A. Sazanov, Journal
    of Biological Chemistry 291 (2016) 24657–24675.
date_created: 2018-12-11T11:50:44Z
date_published: 2016-11-18T00:00:00Z
date_updated: 2021-01-12T06:49:06Z
day: '18'
department:
- _id: LeSa
doi: 10.1074/jbc.M116.735142
ec_funded: 1
intvolume: '       291'
issue: '47'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5114416/
month: '11'
oa: 1
oa_version: Submitted Version
page: 24657 - 24675
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: Journal of Biological Chemistry
publication_status: published
publisher: American Society for Biochemistry and Molecular Biology
publist_id: '6139'
quality_controlled: '1'
scopus_import: 1
status: public
title: Purification of ovine respiratory complex i results in a highly active and
  stable preparation
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 291
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'
...