Identification of molybdopterin guanine dinucleotide in formate dehydrogenase from Methanobacterium formicicum

Johnson, Jennifer L.

doi:10.1016/0378-1097(91)90554-n

Cited by 6 publications

(6 citation statements)

References 8 publications

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“…The wellcoinciding determined values of 0.64 g-atom of molybdenum and 0.72 mol of 5'-GMP per mol of S-FDH suggest a ratio of 1 mol of intact molybdopterin guanine dinucleotide per mol of native enzyme. This type of cofactor in the A. eutrophus enzyme, molybdopterin guanine dinucleotide is identical to the one already known from FDH of the facultatively anaerobic bacterium E. coli (29,46) and the obligate anaerobe archaeon M. formicicum (27), which leads to the interesting question about molybdopterin guanine dinucleotide as the possibly common type of molybdenum cofactor in prokaryotic FDH.…”

Section: Discussionsupporting

confidence: 57%

Physiological and biochemical characterization of the soluble formate dehydrogenase, a molybdoenzyme from Alcaligenes eutrophus

1993

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Organoautotrophic growth ofAlcaligenes eutrophus on formate was dependent on the presence of molybdate in the medium. Supplementation of the medium with tungstate lead to growth cessation. (2,23,26,34,50), aerobic (1,17,30,32,33,41,60) and anaerobic (3,18,36,39,59) (18,31,36,48,58).Whereas FDH from methylotrophic yeasts have very similar overall properties, considerable diversity is found for bacterial FDH concerning their size, structure, cofactor and metal content, electron acceptor spectrum, and other features (19).

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Section: Discussionsupporting

confidence: 57%

Physiological and biochemical characterization of the soluble formate dehydrogenase, a molybdoenzyme from Alcaligenes eutrophus

1993

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“…The genes encoding the five subunits form a transcription unit ( fmdEFACDB ) and are cotranscribed with a gene, fmdF , predicted to encode a polyferredoxin possibly containing eight [4Fe‐4S] clusters [130]. FmdB has deduced sequence similarity to the formate dehydrogenase of Methanobacterium formicicum which also contains a molybdopterin cofactor [58]suggesting FmdB is the catalytic subunit. In addition, FmdB has the potential to bind one [4Fe‐4S] cluster.…”

Section: Carbon Dioxide Reductionmentioning

confidence: 99%

Enzymology of one-carbon metabolism in methanogenic pathways

1999

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Methanoarchaea, the largest and most phylogenetically diverse group in the Archaea domain, have evolved energy-yielding pathways marked by one-carbon biochemistry featuring novel cofactors and enzymes. All of the pathways have in common the two-electron reduction of methyl-coenzyme M to methane catalyzed by methyl-coenzyme M reductase but deviate in the source of the methyl group transferred to coenzyme M. Most of the methane produced in nature derives from acetate in a pathway where the activated substrate is cleaved by CO dehydrogenase/acetyl-CoA synthase and the methyl group is transferred to coenzyme M via methyltetrahydromethanopterin or methyltetrahydrosarcinapterin. Electrons for reductive demethylation of the methyl-coenzyme M originate from oxidation of the carbonyl group of acetate to carbon dioxide by the synthase. In the other major pathway, formate or H2 is oxidized to provide electrons for reduction of carbon dioxide to the methyl level and reduction of methyl-coenzyme to methane. Methane is also produced from the methyl groups of methanol and methylamines. In these pathways specialized methyltransferases transfer the methyl groups to coenzyme M. Electrons for reduction of the methyl-coenzyme M are supplied by oxidation of the methyl groups to carbon dioxide by a reversal of the carbon dioxide reduction pathway. Recent progress on the enzymology of one-carbon reactions in these pathways has raised the level of understanding with regard to the physiology and molecular biology of methanogenesis. These advances have also provided a foundation for future studies on the structure/function of these novel enzymes and exploitation of the recently completed sequences for the genomes from the methanoarchaea Methanobacterium thermoautotrophicum and Methanococcus jannaschii.

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“…Formate dehydrogenase catalyzes the oxidation of formate, which supplies electrons for the reduction of carbon dioxide to methane. The formate dehydrogenase of M. fonnicicum is an iron-sulfur enzyme containing molybdopterin guanine dinucleotide and flavin adenine dinucleotide (13,18,25,26). The enzyme contains two subunits with molecular weights of approximately 85,000 and 35,000 (25).…”

mentioning

confidence: 99%

Identification of formate dehydrogenase-specific mRNA species and nucleotide sequence of the fdhC gene of Methanobacterium formicicum

White

Ferry

1992

J Bacteriol

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The overlappingfdhA andfdhB genes of Methanobacteriumformicicum, which encode the a and 13 subunits, respectively, of formate dehydrogenase, were cotranscribed as part of an approximately 4.5-kb transcript. An additional gene (fdhC) upstream offdhA was cotranscribed with fdhA and fdhB. The deduced amino acid sequence suggested thatfdhC has the potential to encode a hydrophobic polypeptide with a calculated molecular weight of 29,417. A hydropathy plot of the hypothetical polypeptide indicated several potential membranespanning regions. The putativefdhC gene product had 28% identity with the deduced amino acid sequence of the nirC gene from Salmonella typhimurium. Northern (RNA) blot analyses and primer extension assays located a transcription start site 268 bp upstream of the initiation codon offdhC. A sequence identical to the consensus promoter sequence for methanogenic organisms was situated between -35 and -25 bp from the proposed transcription start site. In addition to the 4.5-kb transcript, Northern blot analyses detected a 1.1-kb transcript with anfdhC-specific probe and a 3.4-kb transcript with either anfdhA-orfdhB-specific probe. The levels of all three transcripts were significantly greater in cells grown in media supplemented with molybdate.Methanobacterium formicicum is an archaeon (32) which utilizes either formate or carbon dioxide and hydrogen as the sole sources of carbon and energy. Formate dehydrogenase catalyzes the oxidation of formate, which supplies electrons for the reduction of carbon dioxide to methane. The formate dehydrogenase of M. fonnicicum is an iron-sulfur enzyme containing molybdopterin guanine dinucleotide and flavin adenine dinucleotide (13,18,25,26). The enzyme contains two subunits with molecular weights of approximately 85,000 and 35,000 (25). The level of formate dehydrogenase protein in the cell is regulated in response to the amount of molybdate in the growth medium (18).The fdhA and fdhB genes, which encode the two subunits of the formate dehydrogenase from M. formicicum, have been cloned and sequenced (27). The deduced amino acid sequence of fdhA, encoding the large subunit, has 40% identity with the deduced amino acid sequence of fdhF, which encodes the 80,000-Da subunit of formate dehydrogenase-H from Escherichia coli (36). The fdhAB genes of M. formicicum overlap by 1 bp, which suggests that they may be cotranscribed as part of a polycistronic operon. Approximately 3.6 kbp upstream of the initiation codon offdhA is a 60-bp sequence with 61% identity to a sequence upstream of the fdhF gene of E. coli (4, 20). It was previously suggested that the fdhA and fdhB genes are cotranscribed as part of an approximately 12-kb transcript initiating within 50 bp downstream of this 60-bp sequence (20). Here, we reexamine the transcription offdhAB and present evidence that these genes are cotranscribed as part of a 4.5-kb transcript. In addition, we report the nucleotide sequence of fdhC, which was cotranscribed with fdhA and fdhB. MATERIALS AND METHODSBacterial strains, bacterio...

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Identification of molybdopterin guanine dinucleotide in formate dehydrogenase from Methanobacterium formicicum

Cited by 6 publications

References 8 publications

Physiological and biochemical characterization of the soluble formate dehydrogenase, a molybdoenzyme from Alcaligenes eutrophus

Physiological and biochemical characterization of the soluble formate dehydrogenase, a molybdoenzyme from Alcaligenes eutrophus

Enzymology of one-carbon metabolism in methanogenic pathways

Identification of formate dehydrogenase-specific mRNA species and nucleotide sequence of the fdhC gene of Methanobacterium formicicum

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