Characterization of Tetrathionate Hydrolase from Acidothermophilic Sulfur-Oxidizing Archaeon <i>Metallosphaera cuprina</i> Ar-4.

ABSTRACT: Tetrathionate hydrolase (TTH) is a key enzyme for the oxidation of reduced inorganic sulfur compounds (RISCs) with the S₄I pathway, which is distributed in autotrophic or facultative autotrophic sulfur-oxidizing bacteria and archaea. In this study, the enzyme TTH_Mc from the acidothermophilic archaeon Metallosphaera cuprina Ar-4^T, encoded by mcup_1281 and belonging to the pyrroloquinoline quinone (PQQ) family, has been shown to possess tetrathionate hydrolysis activity. The molecular mass of the single subunit of TTH_Mc was determined to be 57 kDa. TTH_Mc is proved to be located in the cytoplasm, periplasmic space, and membrane, and the activity of them accounted for 72.3%, 24.0%, and 3.7% of the total activity. Optimal acti

SUBMITTER: Wang P 

PROVIDER: S-EPMC11818568 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature