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Here, we experimentally expand understanding of the reactions and enzymes involved in  Acidithiobacillus thiooxidans  ATCC 19377 S 0  andS  2   ⁢   O  3   2  -metabolism by developing models that integrate gene expression analyzed by RNA-Seq, solution sulfur speciation, electron microscopy and spectroscopy. The  A. thiooxidansS  2   ⁢   O  3   2  -metabolism model involves the conversion ofS  2   ⁢   O  3   2  -toSO  4   2  -, S 0  andS  4   ⁢   O  6   2  -,mediated by the sulfur oxidase complex (Sox), tetrathionate hydrolase (TetH), sulfide quinone reductase (Sqr), and heterodisulfate reductase (Hdr) proteins. These same proteins, with the addition of rhodanese (Rhd), were identified to convert S 0  toSO  3   2  -,S  2   ⁢   O  3   2  -and polythionates in the  A. thiooxidans  S 0  metabolism model. Our combined results shed light onto the important role specifically of TetH inS  2   ⁢   O  3   2  -metabolism. Also, we show that activity of Hdr proteins rather than Sdo are likely associated with S 0  oxidation. Finally, our data suggest that formation of intracellularS  2   ⁢   O  3   2  -is a critical step in S 0  metabolism, and that recycling of internally generatedSO  3   2  -occurs, through comproportionating reactions that result inS  2   ⁢   O  3   2  -. Electron microscopy and spectroscopy confirmed intracellular production and storage of S 0  during growth on both S 0  andS  2   ⁢   O  3   2  -substrates.

frontiers in microbiology

New Insights Into Acidithiobacillus thiooxidans Sulfur Metabolism Through Coupled Gene Expression, Solution Chemistry, Microscopy, and Spectroscopy Analyses