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dc.contributor.authorCherak, Stephana J
dc.contributor.authorTurner, Raymond J
dc.date.accessioned2017-09-01T22:13:38Z
dc.date.available2017-09-01T22:13:38Z
dc.date.issued2017-08-08
dc.identifier.citationBioMol Concepts DOI 10.1515/bmc-2017-0011en_US
dc.identifier.urihttp://hdl.handle.net/1880/52204
dc.description.abstractProtein folding and assembly into macromolecule complexes within the living cell is a complex process requiring intimate coordination. The biogenesis of complex iron sulphur molybdoenzymes (CISM) requires use of a system specific chaperone – a redox enzyme maturation protein (REMP) – to help mediate final folding and assembly. The CISM Dimethyl sulfoxide (DMSO) reductase is a bacterial anaerobic respiratory oxidoreductase that utilizes DMSO as a final electron acceptor to survive within anoxic conditions. The REMP DmsD strongly interacts with DMSO reductase to facilitate folding, cofactor-insertion, subunit assembly and targeting of the multi-subunit enzyme prior to membrane translocation and final assembly and maturation into a bioenergetic catalytic unit. In this article, we discuss the biogenesis of DMSO reductase as an example of the participant network for bacterial CISM maturation pathways.en_US
dc.language.isoenen_US
dc.publisherDe Gruyteren_US
dc.subjectprotein foldingen_US
dc.subjectprotein biogenesisen_US
dc.subjectsystem specific chaperoneen_US
dc.subjectiron sulfur molybdoenzymesen_US
dc.subjectdimethyl sulfoxide reductaseen_US
dc.subjecttwin-arginine translocateen_US
dc.titleAssembly Pathway of a Bacterial Complex Iron Sulfur Molybdoenzymeen_US
dc.typejournal article
dc.description.refereedYesen_US
dc.publisher.facultyScienceen_US
dc.description.grantingagencyCIHRen_US
dc.publisher.departmentBiological Sciencesen_US
dc.publisher.institutionUniversity of Calgaryen_US
dc.identifier.doihttp://dx.doi.org/10.11575/PRISM/30231


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