Cytochrome c oxidase assembly factors with thioredoxin fold are conserved among prokaryotes and eukaryotes
dc.contributor.author | Chinenov, Yurii V. | en_US |
dc.date.accessioned | 2006-09-08T19:44:05Z | |
dc.date.available | 2006-09-08T19:44:05Z | |
dc.date.issued | 2000-07 | en_US |
dc.identifier.citation | Chinenov, Yurii V.; (2000). "Cytochrome c oxidase assembly factors with thioredoxin fold are conserved among prokaryotes and eukaryotes." Journal of Molecular Medicine 78(5): 239-242. <http://hdl.handle.net/2027.42/41878> | en_US |
dc.identifier.issn | 0946-2716 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/41878 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=10954195&dopt=citation | en_US |
dc.description.abstract | Cytochrome c oxidase (COX) is a multi-subunit terminal oxidase of the eukaryotic respiratory chain involved in the reduction of oxygen to water. Numerous lines of evidence suggest that the assembly of COX is a multi-step, assisted process that depends on several assembly factors with largely unknown functions. Sco1/2 proteins have been isolated as high-copy number suppressors of a deletion of copper chaperone Cox17, implicating Sco1/2 in copper transport to COX subunits I or II. Here I report the similarity of Sco1/2 assembly factors to peroxiredoxins and thiol:disulfide oxidoreductases with a thioredoxin fold, suggesting that Sco-related proteins perform a catalytic rather than a copper transport function. Reported sequence similarities, together with the functional role of bacterial Sco-related proteins suggest that Sco-related proteins represent a new class of membrane-anchored thiol:disulfide oxidoreductases involved in COX maturation. | en_US |
dc.format.extent | 93757 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Springer-Verlag | en_US |
dc.subject.other | Sco Cytochrome C Oxidase Peroxiredoxins Thioredoxin Fold Cox17 | en_US |
dc.subject.other | Legacy | en_US |
dc.title | Cytochrome c oxidase assembly factors with thioredoxin fold are conserved among prokaryotes and eukaryotes | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Medicine (General) | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Howard Hughes Medical Institute, University of Michigan Medical Center, 4570 MSRB II, 1150 W. Medical Center Drive, Ann Arbor, MI 48109-0650, USA, | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 10954195 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/41878/1/109-78-5-239_s001090000110.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/s001090000110 | en_US |
dc.identifier.source | Journal of Molecular Medicine | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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