Galemou Yoga 2021 Front Chem: Difference between revisions
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|abstract=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. | |abstract=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. | ||
|keywords=NADH dehydrogenase, Electron transfer, Inhibitor, Oxidative phosphorylation, Proton pumping, Respiratory chain, Semiquinone | |||
|editor=[[Plangger M]] | |editor=[[Plangger M]] | ||
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{{Labeling}} | {{Labeling | ||
|area=mt-Structure;fission;fusion | |||
|enzymes=Complex I | |||
}} | |||
Latest revision as of 16:15, 22 March 2023
| Galemou Yoga E, Schiller J, Zickermann V (2021) Ubiquinone binding and reduction by complex I-open questions and mechanistic implications. https://doi.org/10.3389/fchem.2021.672851 |
» Front Chem 9:672851. PMID: 33996767 Open Access
Galemou Yoga Etienne, Schiller Jonathan, Zickermann Volker (2021) Front Chem
Abstract: 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. • Keywords: NADH dehydrogenase, Electron transfer, Inhibitor, Oxidative phosphorylation, Proton pumping, Respiratory chain, Semiquinone • Bioblast editor: Plangger M
Labels: MiParea: mt-Structure;fission;fusion
Enzyme: Complex I
