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The Sox pathway found in many sulfur bacteria oxidizes thiosulfate to sulfate. Pathway intermediates are covalently bound to a cysteine residue in the carrier protein SoxYZ. We have used biochemical complementation by SoxYZ-conjugates to probe the identity of the intermediates in the Sox pathway. We find that unconjugated SoxYZ and SoxYZ-S-sulfonate are unlikely to be intermediates during normal turnover in disagreement with current models. By contrast, conjugates with multiple sulfane atoms are readily metabolised by the Sox pathway. The most parsimonious interpretation of these data is that the true carrier species in the Sox pathway is a SoxYZ-S-sulfane adduct.

Original publication

DOI

10.1371/journal.pone.0173395

Type

Journal article

Journal

PLoS One

Publication Date

2017

Volume

12

Keywords

Bacteria, Carrier Proteins, Cysteine, Oxidation-Reduction, Oxidoreductases Acting on Sulfur Group Donors, Protein Binding, Signal Transduction, Sulfur, Thiosulfates