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  Cox26 is a novel stoichiometric subunit of the yeast cytochrome c oxidase.

Levchenko, M., Wuttke, J. M., Römpler, K., Schmidt, B., Neifer, K., Juris, L., et al. (2016). Cox26 is a novel stoichiometric subunit of the yeast cytochrome c oxidase. Biochimica et Biophysica Acta - Molecular Cell Research, 1863(7), 1624-1632. doi:10.1016/j.bbamcr.2016.04.007.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-FF95-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-07FF-6
Genre: Journal Article

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 Creators:
Levchenko, M., Author
Wuttke, J. M., Author
Römpler, K., Author
Schmidt, B., Author
Neifer, K., Author
Juris, L., Author
Wissel, M., Author
Rehling, P.1, Author              
Deckers, M., Author
Affiliations:
1Max Planck Fellow Peter Rehling, ou_1298545              

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 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 Coxl, Cox2 and Cox3, which associate with nuclear-encoded subunits and cofactors. In the yeast Saccharomyces cerevisiae, the cytochrome c oxidase associates with the bc(1)-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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Language(s): eng - English
 Dates: 2016-04-122016-07
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bbamcr.2016.04.007
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Title: Biochimica et Biophysica Acta - Molecular Cell Research
Source Genre: Journal
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Pages: - Volume / Issue: 1863 (7) Sequence Number: - Start / End Page: 1624 - 1632 Identifier: -