<HashMap><database>biostudies-other</database><scores/><additional><omics_type>Unknown</omics_type><submitter>Dr. Michele Brischigliaro</submitter><funding>AFM-T&amp;amp;#x00E9;l&amp;amp;#x00E9;thon</funding><funding>Fondazione Telethon (FT)</funding><funding>Associazione Luigi Comini ONLUS</funding><funding>ZonMw (Netherlands Organisation for Health Research and Development)</funding><funding>Institut de France (Institute of France)</funding><journal>EMBO Reports</journal><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-SCDT-EMBOR-2022-54825-T</full_dataset_link><abstract>The mitochondrial respiratory chain (MRC) is composed of four multiheteromeric enzyme complexes. According to the endosymbiotic origin of mitochondria, eukaryotic MRC derives from ancestral proteobacterial respiratory structures consisting of a minimal set of complexes formed by a few subunits associated with redox prosthetic groups. These enzymes, which are the "core" redox centers of respiration, acquired additional subunits and increased their complexity throughout evolution. Cytochrome c oxidase (COX), the terminal component of MRC, has a highly interspecific heterogeneous composition. Mammalian COX consists of 14 different polypeptides, of which COX7B is considered the evolutionarily youngest subunit. We applied proteomic, biochemical, and genetic approaches to investigate the COX com</abstract><repository>biostudies-other</repository><funding_grant_id>GGP19007</funding_grant_id><funding_grant_id>23706</funding_grant_id><funding_grant_id>NRJ Fondation</funding_grant_id><funding_grant_id>91217009</funding_grant_id><funding_grant_id>GGP20013</funding_grant_id><pubmed_authors>Dr. Erika Fernandez-Vizarra</pubmed_authors><pubmed_authors>Prof. Stefano Moro</pubmed_authors><pubmed_authors>Prof. Martijn, A. Huynen</pubmed_authors><pubmed_authors>Dr. Alfredo Cabrera-Orefice</pubmed_authors><pubmed_authors>Mr. Dei, Martinez Elurbe</pubmed_authors><pubmed_authors>Dr. Susanne Arnold</pubmed_authors><pubmed_authors>Ms. Elena Frigo</pubmed_authors><pubmed_authors>Dr. Mattia Sturlese</pubmed_authors><pubmed_authors>Prof. Massimo Zeviani</pubmed_authors><pubmed_authors>Dr. Michele Brischigliaro</pubmed_authors><pubmed_authors>Prof. Carlo Viscomi</pubmed_authors></additional><is_claimable>false</is_claimable><name>CG7630 is the D. melanogaster homolog of the cytochrome c oxidase subunit COX7B</name><description>The mitochondrial respiratory chain (MRC) is composed of four multiheteromeric enzyme complexes. According to the endosymbiotic origin of mitochondria, eukaryotic MRC derives from ancestral proteobacterial respiratory structures consisting of a minimal set of complexes formed by a few subunits associated with redox prosthetic groups. These enzymes, which are the "core" redox centers of respiration, acquired additional subunits and increased their complexity throughout evolution. Cytochrome c oxidase (COX), the terminal component of MRC, has a highly interspecific heterogeneous composition. Mammalian COX consists of 14 different polypeptides, of which COX7B is considered the evolutionarily youngest subunit. We applied proteomic, biochemical, and genetic approaches to investigate the COX com</description><dates><release>2022-07-10T00:00:00Z</release><modification>2022-07-10T10:37:10.851Z</modification><creation>2022-07-10T10:37:10.851Z</creation></dates><accession>S-SCDT-EMBOR-2022-54825-T</accession><cross_references><doi>10.15252/embr.202254825</doi></cross_references></HashMap>