---
_id: '7395'
abstract:
- lang: eng
text: The mitochondrial electron transport chain complexes are organized into supercomplexes
(SCs) of defined stoichiometry, which have been proposed to regulate electron
flux via substrate channeling. We demonstrate that CoQ trapping in the isolated
SC I+III2 limits complex (C)I turnover, arguing against channeling. The SC structure,
resolved at up to 3.8 Å in four distinct states, suggests that CoQ oxidation may
be rate limiting because of unequal access of CoQ to the active sites of CIII2.
CI shows a transition between “closed” and “open” conformations, accompanied by
the striking rotation of a key transmembrane helix. Furthermore, the state of
CI affects the conformational flexibility within CIII2, demonstrating crosstalk
between the enzymes. CoQ was identified at only three of the four binding sites
in CIII2, suggesting that interaction with CI disrupts CIII2 symmetry in a functionally
relevant manner. Together, these observations indicate a more nuanced functional
role for the SCs.
article_processing_charge: No
article_type: original
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: Gianluca
full_name: Degliesposti, Gianluca
last_name: Degliesposti
- 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, Fiedorczuk K, Degliesposti G, Skehel M, Sazanov LA. Structures of
respiratory supercomplex I+III2 reveal functional and conformational crosstalk.
Molecular Cell. 2019;75(6):1131-1146.e6. doi:10.1016/j.molcel.2019.07.022
apa: Letts, J. A., Fiedorczuk, K., Degliesposti, G., Skehel, M., & Sazanov,
L. A. (2019). Structures of respiratory supercomplex I+III2 reveal functional
and conformational crosstalk. Molecular Cell. Cell Press. https://doi.org/10.1016/j.molcel.2019.07.022
chicago: Letts, James A, Karol Fiedorczuk, Gianluca Degliesposti, Mark Skehel, and
Leonid A Sazanov. “Structures of Respiratory Supercomplex I+III2 Reveal Functional
and Conformational Crosstalk.” Molecular Cell. Cell Press, 2019. https://doi.org/10.1016/j.molcel.2019.07.022.
ieee: J. A. Letts, K. Fiedorczuk, G. Degliesposti, M. Skehel, and L. A. Sazanov,
“Structures of respiratory supercomplex I+III2 reveal functional and conformational
crosstalk,” Molecular Cell, vol. 75, no. 6. Cell Press, p. 1131–1146.e6,
2019.
ista: Letts JA, Fiedorczuk K, Degliesposti G, Skehel M, Sazanov LA. 2019. Structures
of respiratory supercomplex I+III2 reveal functional and conformational crosstalk.
Molecular Cell. 75(6), 1131–1146.e6.
mla: Letts, James A., et al. “Structures of Respiratory Supercomplex I+III2 Reveal
Functional and Conformational Crosstalk.” Molecular Cell, vol. 75, no.
6, Cell Press, 2019, p. 1131–1146.e6, doi:10.1016/j.molcel.2019.07.022.
short: J.A. Letts, K. Fiedorczuk, G. Degliesposti, M. Skehel, L.A. Sazanov, Molecular
Cell 75 (2019) 1131–1146.e6.
date_created: 2020-01-29T16:02:33Z
date_published: 2019-09-19T00:00:00Z
date_updated: 2023-09-07T14:53:06Z
day: '19'
ddc:
- '570'
department:
- _id: LeSa
doi: 10.1016/j.molcel.2019.07.022
ec_funded: 1
external_id:
isi:
- '000486614200006'
pmid:
- '31492636'
file:
- access_level: open_access
checksum: 5202f53a237d6650ece038fbf13bdcea
content_type: application/pdf
creator: dernst
date_created: 2020-02-04T10:37:28Z
date_updated: 2020-07-14T12:47:57Z
file_id: '7447'
file_name: 2019_MolecularCell_Letts.pdf
file_size: 9654895
relation: main_file
file_date_updated: 2020-07-14T12:47:57Z
has_accepted_license: '1'
intvolume: ' 75'
isi: 1
issue: '6'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
page: 1131-1146.e6
pmid: 1
project:
- _id: 2590DB08-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '701309'
name: Atomic-Resolution Structures of Mitochondrial Respiratory Chain Supercomplexes
publication: Molecular Cell
publication_identifier:
issn:
- 1097-2765
publication_status: published
publisher: Cell Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structures of respiratory supercomplex I+III2 reveal functional and conformational
crosstalk
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: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 75
year: '2019'
...
---
_id: '515'
abstract:
- lang: eng
text: 'The oxidative phosphorylation electron transport chain (OXPHOS-ETC) of the
inner mitochondrial membrane is composed of five large protein complexes, named
CI-CV. These complexes convert energy from the food we eat into ATP, a small molecule
used to power a multitude of essential reactions throughout the cell. OXPHOS-ETC
complexes are organized into supercomplexes (SCs) of defined stoichiometry: CI
forms a supercomplex with CIII2 and CIV (SC I+III2+IV, known as the respirasome),
as well as with CIII2 alone (SC I+III2). CIII2 forms a supercomplex with CIV (SC
III2+IV) and CV forms dimers (CV2). Recent cryo-EM studies have revealed the structures
of SC I+III2+IV and SC I+III2. Furthermore, recent work has shed light on the
assembly and function of the SCs. Here we review and compare these recent studies
and discuss how they have advanced our understanding of mitochondrial electron
transport.'
article_type: original
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: 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. Clarifying the supercomplex: The higher-order organization
of the mitochondrial electron transport chain. Nature Structural and Molecular
Biology. 2017;24(10):800-808. doi:10.1038/nsmb.3460'
apa: 'Letts, J. A., & Sazanov, L. A. (2017). Clarifying the supercomplex: The
higher-order organization of the mitochondrial electron transport chain. Nature
Structural and Molecular Biology. Nature Publishing Group. https://doi.org/10.1038/nsmb.3460'
chicago: 'Letts, James A, and Leonid A Sazanov. “Clarifying the Supercomplex: The
Higher-Order Organization of the Mitochondrial Electron Transport Chain.” Nature
Structural and Molecular Biology. Nature Publishing Group, 2017. https://doi.org/10.1038/nsmb.3460.'
ieee: 'J. A. Letts and L. A. Sazanov, “Clarifying the supercomplex: The higher-order
organization of the mitochondrial electron transport chain,” Nature Structural
and Molecular Biology, vol. 24, no. 10. Nature Publishing Group, pp. 800–808,
2017.'
ista: 'Letts JA, Sazanov LA. 2017. Clarifying the supercomplex: The higher-order
organization of the mitochondrial electron transport chain. Nature Structural
and Molecular Biology. 24(10), 800–808.'
mla: 'Letts, James A., and Leonid A. Sazanov. “Clarifying the Supercomplex: The
Higher-Order Organization of the Mitochondrial Electron Transport Chain.” Nature
Structural and Molecular Biology, vol. 24, no. 10, Nature Publishing Group,
2017, pp. 800–08, doi:10.1038/nsmb.3460.'
short: J.A. Letts, L.A. Sazanov, Nature Structural and Molecular Biology 24 (2017)
800–808.
date_created: 2018-12-11T11:46:54Z
date_published: 2017-10-05T00:00:00Z
date_updated: 2021-01-12T08:01:17Z
day: '05'
ddc:
- '572'
department:
- _id: LeSa
doi: 10.1038/nsmb.3460
ec_funded: 1
file:
- access_level: open_access
checksum: 9bc7e8c41b43636dd7566289e511f096
content_type: application/pdf
creator: lsazanov
date_created: 2019-11-07T12:51:07Z
date_updated: 2020-07-14T12:46:36Z
file_id: '6993'
file_name: 29893_2_merged_1501257589_red.pdf
file_size: 4118385
relation: main_file
file_date_updated: 2020-07-14T12:46:36Z
has_accepted_license: '1'
intvolume: ' 24'
issue: '10'
language:
- iso: eng
month: '10'
oa: 1
oa_version: Submitted Version
page: 800 - 808
project:
- _id: 2590DB08-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '701309'
name: Atomic-Resolution Structures of Mitochondrial Respiratory Chain Supercomplexes
(H2020)
publication: Nature Structural and Molecular Biology
publication_identifier:
issn:
- '15459993'
publication_status: published
publisher: Nature Publishing Group
publist_id: '7304'
quality_controlled: '1'
scopus_import: 1
status: public
title: 'Clarifying the supercomplex: The higher-order organization of the mitochondrial
electron transport chain'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 24
year: '2017'
...
---
_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.
Journal of Biological Chemistry. 2016;291(47):24657-24675. doi:10.1074/jbc.M116.735142
apa: Letts, J. A., Degliesposti, G., Fiedorczuk, K., Skehel, M., & Sazanov,
L. A. (2016). Purification of ovine respiratory complex i results in a highly
active and stable preparation. Journal of Biological Chemistry. American
Society for Biochemistry and Molecular Biology. https://doi.org/10.1074/jbc.M116.735142
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.” Journal of Biological Chemistry. American
Society for Biochemistry and Molecular Biology, 2016. https://doi.org/10.1074/jbc.M116.735142.
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,” Journal of Biological Chemistry, 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.” Journal of Biological Chemistry,
vol. 291, no. 47, American Society for Biochemistry and Molecular Biology, 2016,
pp. 24657–75, doi:10.1074/jbc.M116.735142.
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: '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. Nature. 2016;538(7625):406-410.
doi:10.1038/nature19794
apa: Fiedorczuk, K., Letts, J. A., Degliesposti, G., Kaszuba, K., Skehel, M., &
Sazanov, L. A. (2016). Atomic structure of the entire mammalian mitochondrial
complex i. Nature. Nature Publishing Group. https://doi.org/10.1038/nature19794
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.” Nature. Nature Publishing Group, 2016. https://doi.org/10.1038/nature19794.
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,”
Nature, 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.” Nature, vol. 538, no. 7625, Nature Publishing Group, 2016,
pp. 406–10, doi:10.1038/nature19794.
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.
Nature. 2016;537(7622):644-648. doi:10.1038/nature19774
apa: Letts, J. A., Fiedorczuk, K., & Sazanov, L. A. (2016). The architecture
of respiratory supercomplexes. Nature. Nature Publishing Group. https://doi.org/10.1038/nature19774
chicago: Letts, James A, Karol Fiedorczuk, and Leonid A Sazanov. “The Architecture
of Respiratory Supercomplexes.” Nature. Nature Publishing Group, 2016.
https://doi.org/10.1038/nature19774.
ieee: J. A. Letts, K. Fiedorczuk, and L. A. Sazanov, “The architecture of respiratory
supercomplexes,” Nature, 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.” Nature,
vol. 537, no. 7622, Nature Publishing Group, 2016, pp. 644–48, doi:10.1038/nature19774.
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: '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. Current Opinion in Structural Biology.
2015;33(8):135-145. doi:10.1016/j.sbi.2015.08.008'
apa: 'Letts, J. A., & Sazanov, L. A. (2015). Gaining mass: The structure of
respiratory complex I-from bacterial towards mitochondrial versions. Current
Opinion in Structural Biology. Elsevier. https://doi.org/10.1016/j.sbi.2015.08.008'
chicago: 'Letts, James A, and Leonid A Sazanov. “Gaining Mass: The Structure of
Respiratory Complex I-from Bacterial towards Mitochondrial Versions.” Current
Opinion in Structural Biology. Elsevier, 2015. https://doi.org/10.1016/j.sbi.2015.08.008.'
ieee: 'J. A. Letts and L. A. Sazanov, “Gaining mass: The structure of respiratory
complex I-from bacterial towards mitochondrial versions,” Current Opinion in
Structural Biology, 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.” Current Opinion in
Structural Biology, vol. 33, no. 8, Elsevier, 2015, pp. 135–45, doi:10.1016/j.sbi.2015.08.008.'
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'
...