Thiocyanate dehydrogenase (TcDH)

Thiocyanate oxidation is primarily catalyzed in biology by **thiocyanate dehydrogenase (TcDH)**, a copper-containing oxidoreductase enzyme. This enzyme mediates the two-electron oxidation of thiocyanate (SCN⁻) to cyanate and elemental sulfur, transferring electrons to external acceptors such as cytochromes[2][4][8]. In mammals, peroxidases such as lactoperoxidase and myeloperoxidase catalyze oxidation of SCN⁻ to hypothiocyanite (OSCN⁻) using hydrogen peroxide, yielding antimicrobial species critical for innate immunity[6][7][10]. Thiocyanate oxidation also occurs chemically, with various oxidants (peroxomonosulfate, iodate) yielding different products under specific conditions[3][5][9][10]. TcDH genes are present in bacteria that use thiocyanate as an energy source, especially *Thioalkalivibrio* genus, and are important for both natural and biotechnological applications such as industrial wastewater treatment[4][2]. OSCN⁻ generation is clinically relevant due to its high antimicrobial efficacy and minimal host toxicity, making modulation of thiocyanate oxidation a promising therapeutic strategy[6][7]. If the intention was to identify a discrete molecular target (enzyme, receptor, etc.), the correct entity is **"Thiocyanate dehydrogenase (TcDH)"** and not the general reaction "Thiocyanate oxidation". Using the process name as a target is incorrect; all information above refers to the enzyme TcDH or the peroxidase enzymes that mediate thiocyanate oxidation[2][4][6][8][10].

Other names

Thiocyanate:cytochrome c oxidoreductaseTcDHthiocyanate-degrading enzyme

Catalysis of SCN⁻ oxidation to cyanate, hypothiocyanite, elemental sulfur, or sulfate depending on the enzyme and cofactor/oxidant Generation of antimicrobial OSCN⁻ through peroxidase-mediated oxidation in secretory mucosa