Bacterial CS^sub 2^ Hydrolases from Acidithiobacillus thiooxidans Strains Are Homologous to the Archaeal Catenane CS^sub 2^ Hydrolase

• Published in: Journal of bacteriology Vol. 195; no. 18; p. 4046
• Main Authors: Smeulders, Marjan J, Pol, Arjan, Venselaar, Hanka, Barends, Thomas RM, Hermans, John, Jetten, Mike SM, den Camp, Huub JM Op
• Format: Journal Article
• Language: English
• Published: Washington American Society for Microbiology 01-09-2013
• Subjects: Amino acids; Bacteria; Bacteriology; Carbon dioxide; Hydrogen sulfide; Solvents
• EISSN: 1098-5530
• ISSN: 0021-9193

Carbon disulfide (CS2) and carbonyl sulfide (COS) are important in the global sulfur cycle, and CS2 is used as a solvent in the viscose industry. These compounds can be converted by sulfur-oxidizing bacteria, such as Acidithiobacillus thiooxidans species, to carbon dioxide (CO2) and hydrogen sulfide (H2S), a property used in industrial biofiltration of CS2-polluted airstreams. We report on the mechanism of bacterial CS2 conversion in the extremely acidophilic A. thiooxidans strains S1p and G8. The bacterial CS2 hydrolases were highly abundant. They were purified and found to be homologous to the only other described (archaeal) CS2 hydrolase from Acidianus strain A1-3, which forms a catenane of two interlocked rings. The enzymes cluster in a group of β-carbonic anhydrase (β-CA) homologues that may comprise a subclass of CS2 hydrolases within the β-CA family. Unlike CAs, the CS2 hydrolases did not hydrate CO2 but converted CS2 and COS with H2O to H2S and CO2. The CS2 hydrolases of A. thiooxidans strains G8, 2Bp, Sts 4-3, and BBW1, like the CS2 hydrolase of Acidianus strain A1-3, exist as both octamers and hexadecamers in solution. The CS2 hydrolase of A. thiooxidans strain S1p forms only octamers. Structure models of the A. thiooxidans CS2 hydrolases based on the structure of Acidianus strain A1-3 CS2 hydrolase suggest that the A. thiooxidans strain G8 CS2 hydrolase may also form a catenane. In the A. thiooxidans strain S1p enzyme, two insertions (positions 26 and 27 [PD] and positions 56 to 61 [TPAGGG]) and a nine-amino-acid-longer C-terminal tail may prevent catenane formation. [PUBLICATION ABSTRACT]