Redox cycling by DsrC protein suggests reason for interaction with dissimilatory sulfite reductase
Wednesday, January 8, 2014 - 08:00
in Physics & Chemistry
Scientists recently isolated and characterized oxidized and reduced forms of the protein DsrC, an important step toward understanding DsrC's critical role in sulfate respiration. DsrC is known to interact closely with the essential enzyme dissimilatory sulfite reductase, or DsrAB, which catalyzes the six electron reduction of sulfite to sulfide. Thus, DsrC operates within the metabolic process by which bacterially mediated sulfate reduction generates most of the biogenic sulfide—around one gigaton annually—in the global biogeochemical sulfur cycle.