The coupling mechanism of mammalian respiratory complex I

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F20%3A00121273" target="_blank" >RIV/00216224:14740/20:00121273 - isvavai.cz</a>

Výsledek na webu

<a href="https://science.sciencemag.org/content/370/6516/eabc4209" target="_blank" >https://science.sciencemag.org/content/370/6516/eabc4209</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1126/science.abc4209" target="_blank" >10.1126/science.abc4209</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The coupling mechanism of mammalian respiratory complex I

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

The coupling mechanism of mammalian respiratory complex I

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

—

Návaznosti

—

Rok uplatnění

2020

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Science

ISSN

0036-8075

e-ISSN

—

Svazek periodika

370

Číslo periodika v rámci svazku

6516

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

„547“-„+“

Kód UT WoS článku

000583031800004

EID výsledku v databázi Scopus

2-s2.0-85094982581