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Biofactors. 1995-1996;5(2):93-7.

Identification of molybdopterins in molybdenum- and selenium-containing enzymes.

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  • 1National Institutes of Health, Bethesda, MD 20892, USA.


Selenium is coordinated to a molybdenum atom in nicotinic acid hydroxylase (NAH) from Clostridium barkeri and formate dehydrogenase H (FDH) from Escherichia coli. Selenium is present in FDH in a selenocysteine residue whereas in NAH in occurs in an unidentified labile cofactor. In this paper we describe a simple procedure for isolation and identification of molybdopterins from Mo-containing enzymes. The molybdopterin, after release from the protein with guanidine-hydrochloride, is reduced with KBH4, alkylated with iodoacetamide and separated on a reverse-phase HPLC column. The carboxam-idomethylated pterin compound is further characterized by UV spectroscopy and mass-spectrometry. We found that FDH contains molybdopterin guanine dinucleotide whereas NAH contains molybdopterin cytosine dinucleotide.

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