TY  - JOUR
A1  - Galemou Yoga, Etienne
A1  - Schiller, Jonathan
A1  - Zickermann, Volker
T1  - Ubiquinone binding and reduction by complex I : open questions and mechanistic implications
T2  - Frontiers in Chemistry
N2  - NADH: ubiquinone oxidoreductase (complex I) is the first enzyme complex of the respiratory chain. Complex I is a redox-driven proton pump that contributes to the proton motive force that drives ATP synthase. The structure of complex I has been analyzed by x-ray crystallography and electron cryo-microscopy and is now well-described. The ubiquinone (Q) reduction site of complex I is buried in the peripheral arm and a tunnel-like structure is thought to provide access for the hydrophobic substrate from the membrane. Several intermediate binding positions for Q in the tunnel were identified in molecular simulations. Structural data showed the binding of native Q molecules and short chain analogs and inhibitors in the access pathway and in the Q reduction site, respectively. We here review the current knowledge on the interaction of complex I with Q and discuss recent hypothetical models for the coupling mechanism.
KW  - respiratory chain
KW  - NADH dehydrogenase
KW  - oxidative phosphorylation
KW  - proton pumping
KW  - electron transfer
KW  - semiquinone
KW  - inhibitor
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/61248
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-612487
SN  - 2296-2646
VL  - 9
IS  - art. 672851
SP  - 1
EP  - 9
PB  - Frontiers Media
CY  - Lausanne
ER  -