{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Brown BM"],"funding":["NIGMS NIH HHS"],"pagination":["13541-8"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8901122"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["43(42)"],"pubmed_abstract":["Cytochrome c oxidase requires multiple heme and copper cofactors to catalyze the reduction of molecular oxygen to water. Although significant progress has been made in understanding the transport and incorporation of the copper ions, considerably less is known about the trafficking and insertion of the heme cofactors. Heme O synthase (HOS) and heme A synthase (HAS) from Rhodobacter sphaeroides (Cox10 and Cox15, respectively) and Bacillus subtilis (CtaB and CtaA, respectively) have been cloned and expressed in Escherichia coli. Our results demonstrate that HOS copurifies with HAS and that HAS copurifies with HOS, indicating that HOS and HAS interact and may form a physiologically relevant complex in vivo. Consistent with this hypothesis, the presence of HAS alters the total level of farnesy"],"journal":["Biochemistry"],"pubmed_title":["Heme O synthase and heme A synthase from Bacillus subtilis and Rhodobacter sphaeroides interact in Escherichia coli."],"pmcid":["PMC8901122"],"funding_grant_id":["R01 GM066236","GM66236"],"pubmed_authors":["Cricco JA","Brown BM","Brown KR","Wang Z","Hegg EL"],"additional_accession":[]},"is_claimable":false,"name":"Heme O synthase and heme A synthase from Bacillus subtilis and Rhodobacter sphaeroides interact in Escherichia coli.","description":"Cytochrome c oxidase requires multiple heme and copper cofactors to catalyze the reduction of molecular oxygen to water. Although significant progress has been made in understanding the transport and incorporation of the copper ions, considerably less is known about the trafficking and insertion of the heme cofactors. Heme O synthase (HOS) and heme A synthase (HAS) from Rhodobacter sphaeroides (Cox10 and Cox15, respectively) and Bacillus subtilis (CtaB and CtaA, respectively) have been cloned and expressed in Escherichia coli. Our results demonstrate that HOS copurifies with HAS and that HAS copurifies with HOS, indicating that HOS and HAS interact and may form a physiologically relevant complex in vivo. Consistent with this hypothesis, the presence of HAS alters the total level of farnesy","dates":{"release":"2004-01-01T00:00:00Z","publication":"2004 Oct","modification":"2025-04-22T22:01:27.45Z","creation":"2025-04-06T03:53:27.586Z"},"accession":"S-EPMC8901122","cross_references":{"pubmed":["15491161"],"doi":["10.1021/bi048469k"]}}