2026-04-18T07:50:22Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/164392024-09-27T09:21:44Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19605

00925njm 22002777a 4500 dc Arroum, Tasnim author Borowski, Marie-Theres author Marx, Nico author Schmelter, Frank author Scholz, Martin author Psathaki, Olympia Ekaterini author Hippler, Michael author Enriquez, Jose Antonio author Busch, Karin B author 2023-04-25 The orchestrated activity of the mitochondrial respiratory or electron transport chain (ETC) and ATP synthase convert reduction power (NADH, FADH2) into ATP, the cell's energy currency in a process named oxidative phosphorylation (OXPHOS). Three out of the four ETC complexes are found in supramolecular assemblies: complex I, III, and IV form the respiratory supercomplexes (SC). The plasticity model suggests that SC formation is a form of adaptation to changing conditions such as energy supply, redox state, and stress. Complex I, the NADH-dehydrogenase, is part of the largest supercomplex (CI + CIII2 + CIVn). Here, we demonstrate the role of NDUFB10, a subunit of the membrane arm of complex I, in complex I and supercomplex assembly on the one hand and bioenergetics function on the other. NDUFB10 knockout was correlated with a decrease of SCAF1, a supercomplex assembly factor, and a reduction of respiration and mitochondrial membrane potential. This likely is due to loss of proton pumping since the CI P P -module is downregulated and the P D -module is completely abolished in NDUFB10 knock outs. Biol Chem. 2023 Mar 24;404(5):399-415. http://hdl.handle.net/20.500.12105/16439 36952351 10.1515/hsz-2022-0309 1437-4315 Biological chemistry Loss of respiratory complex I subunit NDUFB10 affects complex I assembly and supercomplex formation.