Molybdopterin adenine dinucleotide and molybdopterin hypoxanthine dinucleotide in formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum (Marburg)

@article{Brner1991MolybdopterinAD,
  title={Molybdopterin adenine dinucleotide and molybdopterin hypoxanthine dinucleotide in formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum (Marburg)},
  author={G. B{\"o}rner and M. Karrasch and Rudolf K Thauer},
  journal={FEBS Letters},
  year={1991},
  volume={290}
}
Formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum was purified to apparent homogeneity and found to contain per mol (apparent molecular mass 110 kDa) 0.6 mol molybdenum, 4 mol non‐heme iron, 4 mol acid‐labile sulfur, in addition, 0.7 mol of a pterin‐containing co‐factor (apparent molecular mass 800 Da) which has been characterized. The pterin material was extracted after alkylation by iodoacetamide and the extract subjected to HPLC on Lichrospher 100 RP‐18. Three pterin… Expand
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References

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The molybdenum cofactor of formylmethanofuran dehydrogenase from Methanosarcina barkeri is a molybdopterin guanine dinucleotide
TLDR
Results demonstrate that the molybdenum cofactor isolated from formylmethanofuran dehydrogenase contains the phosphoric anhydride of molybdopterin and 5'‐GMP. Expand
Molybdopterin guanine dinucleotide: a modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans.
TLDR
Results established that the pterin isolated from dimethyl sulfoxide reductase contains the phosphoric anhydride of molybdopterin and 5'-GMP, which is designated molybdenum guanine dinucleotide. Expand
The molybdoenzyme formylmethanofuran dehydrogenase from Methanosarcina barkeri contains a pterin cofactor.
Recently formylmethanofuran dehydrogenase from the archaebacterium Methanosarcina barkeri has been shown to be a novel molybdo-iron-sulfur protein. We report here that the enzyme contains one mol ofExpand
Isolation and characterization of a second molybdopterin dinucleotide: molybdopterin cytosine dinucleotide.
TLDR
The fact that molybdoenzyme CO dehydrogenase pterin cytosine dinucleotide and molybdopterin guanine din nucleotide contain molyBDopterin in their structure shows that the pterIn moiety, with its unique dithiolene-containing sidechain, is a structural element which is common to the organic portion of themolybdenum cofactors of many molyBdoenzymes. Expand
Identification of molybdopterin guanine dinucleotide in formate dehydrogenase from Methanobacterium formicicum.
TLDR
The pterin cofactor in formate dehydrogenase isolated from Methanobacterium formicium is identified as molybdopterin guanine dinucleotide, which is shown to have absorption and chromatographic properties identical to those of the previously characterized authentic compound. Expand
The structure of the molybdenum cofactor. Characterization of di-(carboxamidomethyl)molybdopterin from sulfite oxidase and xanthine oxidase.
TLDR
1H NMR spectra of the phosphorylated and dephosphorylated forms of alkylated molyBDopterin, in conjunction with the other data, have provided strong corroboration of the validity of the proposed structure of molybdopterin. Expand
Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg).
TLDR
The heterodisulfide reductase catalyzing this step was purified 80-fold to apparent homogeneity from Methanobacterium thermoautotrophicum, and the enzyme was highly specific for CoM-S- S-HTP and H-s-CoM plus H-S -HTP. Expand
The role of formylmethanofuran: tetrahydromethanopterin formyltransferase in methanogenesis from carbon dioxide.
TLDR
Reconstitution experiments established that the formyltransferase is an essential enzyme for the conversion of carbon dioxide to methane and substantiate the role of 5-formyl-H4MPT as an intermediate of methanogenesis. Expand
Formylmethanofuran dehydrogenase activity in cell extracts of Methanobacterium thermoautotrophicum and of Methanosarcina barkeri
TLDR
Cell extracts of Methanobacterium thermoautotrophicum catalyzed the reduction of methyl viologen with formylmethanofuran at a specific rate of 4 μmol · min−1 · mg protein−1 and an enzyme system with very similar properties was also found to be present in cell extracts of methanosarcina barkeri grown on methanol. Expand
UNUSUAL COENZYMES OF METHANOGENESIS
Abstract An isolated area of biochemistry has yielded some surprises — six new cofactors including the first nickel-tetrapyrrole and a new method of CO 2 fixation.
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