Abstract
A fluorescent oxidation product of the molybdenum cofactor was isolated from Escherichia coli nitrate reductase (EC 1.9.6.1) and bovine milk xanthine oxidase (EC 1.2.3.2.), which showed a visible absorption band at 395 nm and was dephosphorylated by alkaline phosphatase but not by phosphodiesterase I. The dephosphyrylated species was oxidized by periodate to thieno [3,2-g]pterin-2-carbaldehyde which was quantitatively converted to thieno [3,2-g]pterin-2-carboxylic acid by subsequent treatment with Ag 2O in 2 N NaOH. These results indicate that the oxidation product of the molybdenum cofactor is a thieno-[3,2-g]pterin derivative with an unidentified side chain in the 2 position.
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