Assembly Pathway of a Bacterial Complex Iron Sulfur Molybdoenzyme

Abstract

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.