A protein trisulfide couples dissimilatory sulfate reduction to energy conservation

André A. Santos, Sofia S. Venceslau, Fabian Grein, William D. Leavitt, Christiane Dahl, David T. Johnston, Ines Antunes Pereira

Research output: Contribution to journalArticlepeer-review

118 Citations (Scopus)

Abstract

Microbial sulfate reduction has governed Earth's biogeochemical sulfur cycle for at least 2.5 billion years. However, the enzymatic mechanisms behind this pathway are incompletely understood, particularly for the reduction of sulfite - a key intermediate in the pathway. This critical reaction is performed by DsrAB, a widespread enzyme also involved in other dissimilatory sulfur metabolisms. Using in vitro assays with an archaeal DsrAB, supported with genetic experiments in a bacterial system, we show that the product of sulfite reduction by DsrAB is a protein-based trisulfide, in which a sulfite-derived sulfur is bridging two conserved cysteines of DsrC. Physiological studies also reveal that sulfate reduction rates are determined by cellular levels of DsrC. Dissimilatory sulfate reduction couples the four-electron reduction of the DsrC trisulfide to energy conservation.

Original languageEnglish
Pages (from-to)1541-1545
Number of pages5
JournalScience
Volume350
Issue number6267
DOIs
Publication statusPublished - 18 Dec 2015

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