Identification of molybdopterin guanine dinucleotide in formate dehydrogenase from Methanobacterium formicicum.
The pterin cofactor in formate dehydrogenase isolated from Methanobacterium formicium is identified as molybdopterin guanine dinucleotide. The pterin, stabilized as the alkylated, dicarboxamidomethyl derivative, is shown to have absorption and chromatographic properties identical to those of the previously characterized authentic compound. Treatment with nucleotide pyrophosphatase produced the expected degradation products GMP and carboxyamidomethyl molybdopterin. The molybdopterin guanine dinucleotide released from the enzyme by treatment with 95% dimethyl sulfoxide is shown to be functional in the in vitro reconstitution of the cofactor-deficient nitrate reductase in extracts of the Neurospora crassa nit-1 mutant.
Johnson
J L
JL
Department of Biochemistry, Duke University Medical Center, Durham, NC 27710.
Bastian
N R
NR
Schauer
N L
NL
Ferry
J G
JG
Rajagopalan
K V
KV
D002851:Chromatography, High Pressure Liquid; D019605:Euryarchaeota / Q000201:enzymology*; D005560:Formate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism; D006150:Guanine Nucleotides / Q000032:analysis*; D011622:Pterins / Q000032:analysis*; D013053:Spectrophotometry
D006150:Guanine Nucleotides; D011622:Pterins; C063761:molybdopterin guanine dinucleotide; D005560:Formate Dehydrogenases