The enzyme usually exists as a homodimer, each monomer consisting of two functional domains. Tryptic cleavage of rat liver sulphite oxidase yields two fragments corresponding to these domains. The enzyme usually exists as a homodimer, each monomer consisting of three domains.
Sulphite oxidase is a homodimer, each monomer consisting of three structural domains.
The Moco is bound at the centre of this domain and is contacted by discontinuous stretches of the polypeptide chain. The Moco consists of a single molybdopterin and Mo ion. Mo is pentacoordinated, with two oxygen and three thiolate ligands. The mononuclear molybdenum enzymes. Tryptic cleavage of rat liver sulfite oxidase.