Cherak, Stephana JTurner, Raymond J2017-09-012017-09-012017-08-08BioMol Concepts DOI 10.1515/bmc-2017-0011http://hdl.handle.net/1880/52204Protein 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.enprotein foldingprotein biogenesissystem specific chaperoneiron sulfur molybdoenzymesdimethyl sulfoxide reductasetwin-arginine translocatejournal article10.11575/PRISM/30231