Assembly Pathway of a Bacterial Complex Iron Sulfur Molybdoenzyme

Protein 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.
protein folding, protein biogenesis, system specific chaperone, iron sulfur molybdoenzymes, dimethyl sulfoxide reductase, twin-arginine translocate
BioMol Concepts DOI 10.1515/bmc-2017-0011