Extracellular organic disulfide reduction by MR-1.

Microbial reduction of organic disulfides affects the macromolecular structure and chemical reactivity of natural organic matter. Currently, the enzymatic pathways that mediate disulfide bond reduction in soil and sedimentary organic matter are poorly understood. In this study, we examined the extracellular reduction of 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) by strain MR-1. A transposon mutagenesis screen performed with resulted in the isolation of a mutant that lost ~90% of its DTNB reduction activity. Genome sequencing of the mutant strain revealed that the transposon was inserted into the gene, which encodes for an oxidoreductase involved in cytochrome maturation. Complementation of the mutant strain with the wild-type partially restored DTNB reduction activity. Because DsbD catalyzes a critical step in the assembly of multi-heme -type cytochromes, we further investigated the role of extracellular electron transfer cytochromes in organic disulfide reduction. The results indicated that mutants lacking proteins in the Mtr system were severely impaired in their ability to reduce DTNB. These findings provide new insights into extracellular organic disulfide reduction and the enzymatic pathways of organic sulfur redox cycling.Organic sulfur compounds in soils and sediments are held together by disulfide bonds. This study investigates how breaks apart extracellular organic sulfur compounds. The results show that an enzyme involved in the assembly of -type cytochromes as well as proteins in the Mtr respiratory pathway is needed for to transfer electrons from the cell surface to extracellular organic disulfides. These findings have important implications for understanding how organic sulfur decomposes in terrestrial ecosystems.