Identification of molybdopterin guanine dinucleotide in formate dehydrogenase from Methanobacterium formicicum

Jean L. Johnson; Neil R. Bastian; Neil L. Schauer; James G. Ferry; K. V. Rajagopalan

doi:10.1111/j.1574-6968.1991.tb04350.x

Identification of molybdopterin guanine dinucleotide in formate dehydrogenase from Methanobacterium formicicum

Jean L. Johnson, Neil R. Bastian, Neil L. Schauer, James G. Ferry, K. V. Rajagopalan

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

37 Scopus citations

Abstract

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 carboxamidomethyl 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.

Original language	English (US)
Pages (from-to)	213-216
Number of pages	4
Journal	FEMS Microbiology Letters
Volume	77
Issue number	2-3
DOIs	https://doi.org/10.1111/j.1574-6968.1991.tb04350.x
State	Published - Jan 15 1991

All Science Journal Classification (ASJC) codes

Microbiology
Molecular Biology
Genetics

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10.1111/j.1574-6968.1991.tb04350.x

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title = "Identification of molybdopterin guanine dinucleotide in formate dehydrogenase from Methanobacterium formicicum",

abstract = "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 carboxamidomethyl 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.",

author = "Johnson, {Jean L.} and Bastian, {Neil R.} and Schauer, {Neil L.} and Ferry, {James G.} and Rajagopalan, {K. V.}",

note = "Funding Information: This work was supported in part by Grant number GM00091 from the National Institutes of Health to K.V.R. and in part by NSF Grant number DMB-8409558 to J.G.F.N.R.B. was supported by a postdoctoral training Grant ES07031 from the National Institutes of Health. We thank Mr. Ralph D. Wiley for his assistance in purification of chicken liver sulfite oxidase.",

year = "1991",

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doi = "10.1111/j.1574-6968.1991.tb04350.x",

language = "English (US)",

volume = "77",

pages = "213--216",

journal = "FEMS Microbiology Letters",

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T1 - Identification of molybdopterin guanine dinucleotide in formate dehydrogenase from Methanobacterium formicicum

AU - Johnson, Jean L.

AU - Bastian, Neil R.

AU - Schauer, Neil L.

AU - Ferry, James G.

AU - Rajagopalan, K. V.

N1 - Funding Information: This work was supported in part by Grant number GM00091 from the National Institutes of Health to K.V.R. and in part by NSF Grant number DMB-8409558 to J.G.F.N.R.B. was supported by a postdoctoral training Grant ES07031 from the National Institutes of Health. We thank Mr. Ralph D. Wiley for his assistance in purification of chicken liver sulfite oxidase.

PY - 1991/1/15

Y1 - 1991/1/15

N2 - 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 carboxamidomethyl 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.

AB - 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 carboxamidomethyl 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.

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Identification of molybdopterin guanine dinucleotide in formate dehydrogenase from Methanobacterium formicicum

Abstract

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