Rhodanese is a mitochondrial enzyme that detoxifies cyanide (CN−) by converting it to thiocyanate (SCN−, also known as "rhodanate").

In the second step, the persulfide reacts with cyanide to produce thiocyanate, re-generating the cysteine thiol 1.

This domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.

15938 The use of thiosulfate solution as an antidote for cyanide poisoning is based on the activation of this enzymatic cycle.

The following other human genes match the "Rhodanese-like" domain on InterPro, but are not the rodanase with its catalytic activity (see also the list of related families in #Structure and mechanism): Although the standard nomenclature rules for enzymes indicate that their names are to end with the letters "-ase", rhodanese was first described in 1933,[7] prior to the 1955 establishment of the Enzyme Commission; as such, the older name had already attained widespread usage.