Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10801665 | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | 2016 | 9 Pages |
Abstract
The cytochrome c oxidase (COX) is the terminal enzyme of the respiratory chain. The complex accepts electrons from cytochrome c and passes them onto molecular oxygen. This process contributes to energy capture in the form of a membrane potential across the inner membrane. The enzyme complex assembles in a stepwise process from the three mitochondria-encoded core subunits Cox1, Cox2 and Cox3, which associate with nuclear-encoded subunits and cofactors. In the yeast Saccharomyces cerevisiae, the cytochrome c oxidase associates with the bc1-complex into supercomplexes, allowing efficient energy transduction. Here we report on Cox26 as a protein found in respiratory chain supercomplexes containing cytochrome c oxidase. Our analyses reveal Cox26 as a novel stoichiometric structural subunit of the cytochrome c oxidase. A loss of Cox26 affects cytochrome c oxidase activity and respirasome organization.
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Authors
Maria Levchenko, Jan-Moritz Wuttke, Katharina Römpler, Bernhard Schmidt, Klaus Neifer, Lisa Juris, Mirjam Wissel, Peter Rehling, Markus Deckers,