||Sulfite oxidase comprises the recombinant molybdenumC-terminal domain of Homo sapiens, purified from a TP1000 Escherichia colistrain.
||Sulfite oxidase (EC 220.127.116.11) is a homodimeric proteinlocalized in the intermembrane space of mitochondria of all eukaryoticorganisms. Each subunit contains an N-terminal domain, with a heme cofactor,and a C-terminal domain, with a molybdopterin cofactor (MoVI). The enzymecatalyzes the oxidation of sulfite to sulfate, which takes place at themolybdenum centre, and is the final reaction in the oxidative degradation ofthe sulfur amino acids cystein and methionine.
||One unit of sulfiteoxidase activity is defined as the amount of enzyme required to oxidize 1.0µmol of sulfite to sulfate, per min, in a coupled assay where the hydrogenperoxide formed in the first reaction is reduced by an NADH-peroxidase in thepresence of NADH, at 25 °C and pH 8.5.
||>95%, asdetermined by SDS-PAGE
|Temperature and pHoptimum:
||The optimum pH andtemperature are 8.5 and 25 °C, respectively.
||Sulfite oxidase should be stored at 4 °C and will remain stableup to 3 years if stored as specified.