A protein trisulfide couples dissimilatory sulfate reduction to energy conservation

Sulfate reduction via a trisulfide Microorganisms can respire sulfur compounds in the absence of oxygen, eventually leading to the production of hydrogen sulfide. This ancient metabolism is common in modern anoxic environments, but the enzymatic pathways aren't yet fully resolved. Through in vivo and in vitro experiments, Santos et al. clarify the enzymology of the sulfate reduction pathway in both bacteria and archaea (see the Perspective by Fritz and Kroneck). Reduction of the sulfite intermediate results in the linkage of two cysteine residues to a third sulfur atom from sulfite, forming a trisulfide product. Because the reduction of sulfite conveys a strong isotopic signature on sulfur in the environment, isotope fractionation models should account for this additional step. Science , this issue p. 1541 ; see also p. 1476