Analysis of the interactions between thiocyanate dehydrogenase and thioredoxin like protein using bioinformatics methods

Abstract

Resently a novel copper-containing enzyme thiocyanate dehydrogenase (TcDH) was isolated from the periplasm of some thiocyanate converting haloalkaliphilic sulfur-oxidizing bacteria (SOB). TCDH catalyzes oxidative thiocyanate conversion into cyanate, elemental sulfur, and two reducing equivalents without involvement of molecular oxygen. In the genomes of some SOB the gene of TcDH is adjacent to the gene of thioredox-in-like protein (TLP). According to our preliminary data TcDH forms a stable complex with TLP in the periplasm of bacterium Thiohalobacter thiocyanaticus HRh1. However, the details of the complex formation are un-known.