Detailed Information on Publication Record
2020
The coupling mechanism of mammalian respiratory complex I
KAMPJUT, D. and L.A. SAZANOVBasic information
Original name
The coupling mechanism of mammalian respiratory complex I
Authors
KAMPJUT, D. and L.A. SAZANOV
Edition
Science, WASHINGTON, AMER ASSOC ADVANCEMENT SCIENCE, 2020, 0036-8075
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10608 Biochemistry and molecular biology
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 47.728
RIV identification code
RIV/00216224:14740/20:00121273
Organization unit
Central European Institute of Technology
UT WoS
000583031800004
Keywords in English
CRYSTAL-STRUCTURE; PROTON PUMP; VALIDATION
Tags
International impact, Reviewed
Změněno: 26/4/2021 08:38, Mgr. Pavla Foltynová, Ph.D.
Abstract
V originále
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.
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