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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. a L.A. SAZANOV. The coupling mechanism of mammalian respiratory complex I. \textit{Science}. WASHINGTON: AMER ASSOC ADVANCEMENT SCIENCE, 2020, roč.~370, č.~6516, s.~''547''-''+'', 12 s. ISSN~0036-8075. Dostupné z: https://dx.doi.org/10.1126/science.abc4209.
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