Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1984 Apr;81(7):1976–1980. doi: 10.1073/pnas.81.7.1976

Formaldehyde activation factor, tetrahydromethanopterin, a coenzyme of methanogenesis

Jorge C Escalante-Semerena *, John A Leigh *, Kenneth L Rinehart Jr †, Ralph S Wolfe *,‡
PMCID: PMC345419  PMID: 16593444

Abstract

An oxygen-labile formaldehyde activation factor (FAF) was isolated in highly purified form by use of anoxic fractionation procedures. The molecular weight of FAF was determined to be 776 and that of methanopterin (MPT) 772 by fast-atom-bombardment mass spectrometry (FABMS). High-resolution FABMS measurements on MPT and FAF indicated molecular formulas of C30H41N6O16P and C30H45N6O16P, respectively. The presence of phosphorus was confirmed by 100-MHz 31P NMR. The 360-MHz 1H NMR spectrum of FAF in deuterium oxide was similar to that of MPT. A functional relationship between MPT and FAF was documented; both compounds stimulated the reductive demethylation of 2-(methylthio)ethanesulfonic acid (CH3-S-CoM) to CH4 when formaldehyde oxidation provided a source of electrons, and FAF replaced MPT in the CH3-S-CoM-stimulated conversion of CO2 to CH4 under H2 (the RPG effect). MPT was enzymically converted to FAF during the reduction of CH3-S-CoM, and HCHO to CH4 under H2. Evidence indicates that FAF is tetrahydromethanopterin.

Keywords: methanopterin, Methanobacterium

Full text

PDF
1976

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Eirich L. D., Vogels G. D., Wolfe R. S. Distribution of coenzyme F420 and properties of its hydrolytic fragments. J Bacteriol. 1979 Oct;140(1):20–27. doi: 10.1128/jb.140.1.20-27.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Eirich L. D., Vogels G. D., Wolfe R. S. Proposed structure for coenzyme F420 from Methanobacterium. Biochemistry. 1978 Oct 31;17(22):4583–4593. doi: 10.1021/bi00615a002. [DOI] [PubMed] [Google Scholar]
  3. Ellefson W. L., Whitman W. B., Wolfe R. S. Nickel-containing factor F430: chromophore of the methylreductase of Methanobacterium. Proc Natl Acad Sci U S A. 1982 Jun;79(12):3707–3710. doi: 10.1073/pnas.79.12.3707. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Gunsalus R. P., Tandon S. M., Wolfe R. S. A procedure for anaerobic column chromatography employing an anaerobic Freter-type chamber. Anal Biochem. 1980 Jan 15;101(2):327–331. doi: 10.1016/0003-2697(80)90195-5. [DOI] [PubMed] [Google Scholar]
  5. Gunsalus R. P., Wolfe R. S. Methyl coenzyme M reductase from Methanobacterium thermoautotrophicum. Resolution and properties of the components. J Biol Chem. 1980 Mar 10;255(5):1891–1895. [PubMed] [Google Scholar]
  6. Keltjens J. T., Daniels L., Jannsen H. G., Borm P. J., Vogels G. D. A novel one-carbon carrier (carboxy-5,6,7,8-tetrahydromethanopterin) isolated from Methanobacterium thermoautotrophicum and derived from methanopterin. Eur J Biochem. 1983 Feb 15;130(3):545–552. doi: 10.1111/j.1432-1033.1983.tb07184.x. [DOI] [PubMed] [Google Scholar]
  7. Keltjens J. T., Huberts M. J., Laarhoven W. H., Vogels G. D. Structural elements of methanopterin, a novel pterin present in Methanobacterium thermoautotrophicum. Eur J Biochem. 1983 Feb 15;130(3):537–544. doi: 10.1111/j.1432-1033.1983.tb07183.x. [DOI] [PubMed] [Google Scholar]
  8. Leigh J. A., Wolfe R. S. Carbon dioxide reduction factor and methanopterin, two coenzymes required for CO2 reduction to methane by extracts of Methanobacterium. J Biol Chem. 1983 Jun 25;258(12):7536–7540. [PubMed] [Google Scholar]
  9. Romesser J. A., Balch W. E. Coenzyme M: preparation and assay. Methods Enzymol. 1980;67:545–552. doi: 10.1016/s0076-6879(80)67067-0. [DOI] [PubMed] [Google Scholar]
  10. Taylor C. D., Wolfe R. S. Structure and methylation of coenzyme M(HSCH2CH2SO3). J Biol Chem. 1974 Aug 10;249(15):4879–4885. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES