{"doi":"10.1074/jbc.ra118.002496","title":"Cox15 interacts with the cytochrome bc1 dimer within respiratory supercomplexes as well as in the absence of cytochrome c oxidase","abstract":null,"journal":"Journal of Biological Chemistry","year":2018,"id":682319,"datarank":0.42498200160843247,"base_score":2.833213344056216,"endowment":2.833213344056216,"self_citation_contribution":0.42498200160843247,"citation_network_contribution":0.0,"self_endowment_contribution":0.42498200160843247,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":16,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1124244,"name":"Elise D. Rivett","orcid":"0000-0002-5118-2612","position":1,"is_corresponding":false},{"id":469476,"name":"Antoineen J. White","orcid":"0000-0002-2934-2309","position":2,"is_corresponding":false},{"id":611020,"name":"Eric L. Hegg","orcid":"0000-0003-2055-5495","position":3,"is_corresponding":false},{"id":1782570,"name":"Emily J. Herwaldt","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Cox15 interacts with the cytochrome bc1 dimer within respiratory supercomplexes as well as in the absence of cytochrome c oxidase","abstract":"The heme <i>a</i> molecule is an obligatory cofactor in the terminal enzyme complex of the electron transport chain, cytochrome <i>c</i> oxidase. Heme <i>a</i> is synthesized from heme <i>o</i> by a multi-spanning inner membrane protein, heme <i>a</i> synthase (Cox15 in the yeast <i>Saccharomyces cerevisiae</i>). The insertion of heme <i>a</i> is critical for cytochrome <i>c</i> oxidase function and assembly, but this process has not been fully elucidated. To improve our understanding of heme <i>a</i> insertion into cytochrome <i>c</i> oxidase, here we investigated the protein-protein interactions that involve Cox15 in <i>S. cerevisiae</i> In addition to observing Cox15 in homooligomeric complexes, we found that a portion of Cox15 also associates with the mitochondrial respiratory supercomplexes. When supercomplex formation was abolished, as in the case of stalled cytochrome <i>bc</i><sub>1</sub> or cytochrome <i>c</i> oxidase assembly, Cox15 maintained an interaction with select proteins from both respiratory complexes. In the case of stalled cytochrome <i>bc</i><sub>1</sub> assembly, Cox15 interacted with the late-assembling cytochrome <i>c</i> oxidase subunit, Cox13. When cytochrome <i>c</i> oxidase assembly was stalled, Cox15 unexpectedly maintained its interaction with the cytochrome <i>bc</i><sub>1</sub> protein, Cor1. Our results indicate that Cox15 and Cor1 continue to interact in the cytochrome <i>bc</i><sub>1</sub> dimer even in the absence of supercomplexes or when the supercomplexes are destabilized. These findings reveal that Cox15 not only associates with respiratory supercomplexes, but also interacts with the cytochrome <i>bc</i><sub>1</sub> dimer even in the absence of cytochrome <i>c</i> oxidase.","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"30181213","pmcid":"PMC6200925","openalex_id":null,"authors":[],"funders":[{"funder_name":"HHS | National Institutes of Health (NIH)","grant_id":"GM101386","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM101386","title":null}],"total_grants":2,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"http://www.jbc.org/article/S0021925820351085/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925820351085?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925820351085?httpAccept=text/plain","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1074/jbc.RA118.002496","host_type":"publisher"},{"url":"http://www.jbc.org/content/293/42/16426.full.pdf","host_type":"Unpaywall"}],"fields_of_study":[],"mesh_terms":["Saccharomyces cerevisiae","Cytochrome-c Oxidase Deficiency","Heme","Electron Transport Complex IV","Electron Transport Complex III","Saccharomyces cerevisiae Proteins","Membrane Proteins"],"keywords":["Mitochondria","Saccharomyces cerevisiae","Membrane protein","Respiratory chain","Protein-protein interaction","Cytochrome C Oxidase (Complex Iv)","Cox15","Heme A Synthase","Cytochrome Bc1 (Complex Iii)","Mitochondrial Respiratory Supercomplexes"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"gen"},{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-17T20:05:06.448632Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}