Difference between revisions of "Schiller 2022 Pharmaceuticals (Basel)"
Tag: Manual revert |
|||
| (2 intermediate revisions by the same user not shown) | |||
| Line 8: | Line 8: | ||
|editor=[[Plangger M]] | |editor=[[Plangger M]] | ||
}} | }} | ||
{{Labeling}} | {{Labeling | ||
|enzymes=Complex I | |||
}} | |||
Latest revision as of 15:58, 22 March 2023
| Schiller J, Zickermann V (2022) Binding of natural inhibitors to respiratory complex I. https://doi.org/10.3390/ph15091088 |
» Pharmaceuticals (Basel) 15:1088. PMID: 36145309 Open Access
Schiller Jonathan, Zickermann Volker (2022) Pharmaceuticals (Basel)
Abstract: NADH:ubiquinone oxidoreductase (respiratory complex I) is a redox-driven proton pump with a central role in mitochondrial oxidative phosphorylation. The ubiquinone reduction site of complex I is located in the matrix arm of this large protein complex and connected to the membrane via a tunnel. A variety of chemically diverse compounds are known to inhibit ubiquinone reduction by complex I. Rotenone, piericidin A, and annonaceous acetogenins are representatives of complex I inhibitors from biological sources. The structure of complex I is determined at high resolution, and inhibitor binding sites are described in detail. In this review, we summarize the state of knowledge of how natural inhibitors bind in the Q reduction site and the Q access pathway and how their inhibitory mechanisms compare with that of a synthetic anti-cancer agent.
• Bioblast editor: Plangger M
Labels:
Enzyme: Complex I
