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- W2419031004 abstract "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." @default.
- W2419031004 created "2016-06-24" @default.
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- W2419031004 date "1995-01-01" @default.
- W2419031004 modified "2023-09-25" @default.
- W2419031004 title "Identification of molybdopterins in molybdenum- and selenium-containing enzymes." @default.
- W2419031004 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8722123" @default.
- W2419031004 hasPublicationYear "1995" @default.
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