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               <mods:identifier type="citation">Biol Chem. 2023 Mar 24;404(5):399-415.</mods:identifier>
               <mods:identifier type="uri">http://hdl.handle.net/20.500.12105/16439</mods:identifier>
               <mods:identifier type="pubmedID">36952351</mods:identifier>
               <mods:identifier type="doi">10.1515/hsz-2022-0309</mods:identifier>
               <mods:identifier type="e-issn">1437-4315</mods:identifier>
               <mods:identifier type="journal">Biological chemistry</mods:identifier>
               <mods:abstract>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.</mods:abstract>
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                  <mods:title>Loss of respiratory complex I subunit NDUFB10 affects complex I assembly and supercomplex formation.</mods:title>
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