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@article{1753762,
author = {Kampjut, D. and Sazanov, L.A.},
article_location = {WASHINGTON},
article_number = {6516},
doi = {http://dx.doi.org/10.1126/science.abc4209},
keywords = {CRYSTAL-STRUCTURE; PROTON PUMP; VALIDATION},
language = {eng},
issn = {0036-8075},
journal = {Science},
title = {The coupling mechanism of mammalian respiratory complex I},
url = {https://science.sciencemag.org/content/370/6516/eabc4209},
volume = {370},
year = {2020}
}
TY - JOUR
ID - 1753762
AU - Kampjut, D. - Sazanov, L.A.
PY - 2020
TI - The coupling mechanism of mammalian respiratory complex I
JF - Science
VL - 370
IS - 6516
SP - "547"-"+"
EP - "547"-"+"
PB - AMER ASSOC ADVANCEMENT SCIENCE
SN - 00368075
KW - CRYSTAL-STRUCTURE
KW - PROTON PUMP
KW - VALIDATION
UR - https://science.sciencemag.org/content/370/6516/eabc4209
N2 - Mitochondrial complex I couples NADH:ubiquinone oxidoreduction to proton pumping by an unknown mechanism. Here, we present cryo-electron microscopy structures of ovine complex I in five different conditions, including turnover, at resolutions up to 2.3 to 2.5 angstroms. Resolved water molecules allowed us to experimentally define the proton translocation pathways. Quinone binds at three positions along the quinone cavity, as does the inhibitor rotenone that also binds within subunit ND4. Dramatic conformational changes around the quinone cavity couple the redox reaction to proton translocation during open-to-closed state transitions of the enzyme. In the induced deactive state, the open conformation is arrested by the ND6 subunit. We propose a detailed molecular coupling mechanism of complex I, which is an unexpected combination of conformational changes and electrostatic interactions.
ER -
KAMPJUT, D. and L.A. SAZANOV. The coupling mechanism of mammalian respiratory complex I. \textit{Science}. WASHINGTON: AMER ASSOC ADVANCEMENT SCIENCE, 2020, vol.~370, No~6516, p.~''547''-''+'', 12 pp. ISSN~0036-8075. Available from: https://dx.doi.org/10.1126/science.abc4209.
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