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Journal of Bacteriology logoLink to Journal of Bacteriology
. 1985 Feb;161(2):696–701. doi: 10.1128/jb.161.2.696-701.1985

Tetrahydromethanopterin-dependent methanogenesis from non-physiological C1 donors in Methanobacterium thermoautotrophicum.

J C Escalante-Semerena, R S Wolfe
PMCID: PMC214938  PMID: 3838170

Abstract

Methanogenesis from the non-physiological C1 donors thioproline, thiazolidine, hexamethylenetetramine, formaldehyde (HCHO), and HOCH2-S-coenzyme M (CoM) was catalyzed by cell extracts of Methanobacterium thermoautotrophicum under a hydrogen atmosphere. Tetrahydromethanopterin (H4MPT) and HS-CoM were required in the reaction mixture. The non-physiological compounds were found to be in chemical equilibrium with HCHO, which has been shown to react spontaneously with H4MPT to form methylene-H4MPT, an intermediate of the methanogenic pathway at the formaldehyde level of oxidation. Highfield (360 MHZ) 1H and 13C nuclear magnetic resonance studies performed on the interaction between HCHO and HS-CoM showed that these compounds are in equilibrium with HOCH2-S-CoM and that the equilibrium is pH dependent. When methanogenesis from the non-physiological donors was followed under a nitrogen atmosphere, the C1 moiety from each compound underwent a disproportionation, forming methenyl-H4MPT+ and methane. The compounds tested served as substrates for the enzymatic synthesis of methenyl-H4MPT+.

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Selected References

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  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. Ellefson W. L., Wolfe R. S. Component C of the methylreductase system of Methanobacterium. J Biol Chem. 1981 May 10;256(9):4259–4262. [PubMed] [Google Scholar]
  5. Escalante-Semerena J. C., Leigh J. A., Rinehart K. L., Wolfe R. S. Formaldehyde activation factor, tetrahydromethanopterin, a coenzyme of methanogenesis. Proc Natl Acad Sci U S A. 1984 Apr;81(7):1976–1980. doi: 10.1073/pnas.81.7.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Escalante-Semerena J. C., Rinehart K. L., Jr, Wolfe R. S. Tetrahydromethanopterin, a carbon carrier in methanogenesis. J Biol Chem. 1984 Aug 10;259(15):9447–9455. [PubMed] [Google Scholar]
  7. Escalante-Semerena J. C., Wolfe R. S. Formaldehyde oxidation and methanogenesis. J Bacteriol. 1984 May;158(2):721–726. doi: 10.1128/jb.158.2.721-726.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gunsalus R. P., Romesser J. A., Wolfe R. S. Preparation of coenzyme M analogues and their activity in the methyl coenzyme M reductase system of Methanobacterium thermoautotrophicum. Biochemistry. 1978 Jun 13;17(12):2374–2377. doi: 10.1021/bi00605a019. [DOI] [PubMed] [Google Scholar]
  9. 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]
  10. KUNITZ M. Crystalline inorganic pyrophosphatase isolated from baker's yeast. J Gen Physiol. 1952 Jan;35(3):423–450. doi: 10.1085/jgp.35.3.423. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kallen R. G., Jencks W. P. The mechanism of the condensation of formaldehyde with tetrahydrofolic acid. J Biol Chem. 1966 Dec 25;241(24):5851–5863. [PubMed] [Google Scholar]
  12. 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]
  13. NASH T. The colorimetric estimation of formaldehyde by means of the Hantzsch reaction. Biochem J. 1953 Oct;55(3):416–421. doi: 10.1042/bj0550416. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Nagle D. P., Jr, Wolfe R. S. Component A of the methyl coenzyme M methylreductase system of Methanobacterium: resolution into four components. Proc Natl Acad Sci U S A. 1983 Apr;80(8):2151–2155. doi: 10.1073/pnas.80.8.2151. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Romesser J. A., Wolfe R. S. Coupling of methyl coenzyme M reduction with carbon dioxide activation in extracts of Methanobacterium thermoautotrophicum. J Bacteriol. 1982 Nov;152(2):840–847. doi: 10.1128/jb.152.2.840-847.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Romesser J. A., Wolfe R. S. Interaction of coenzyme M and formaldehyde in methanogenesis. Biochem J. 1981 Sep 1;197(3):565–571. doi: 10.1042/bj1970565. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. 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]
  18. van Beelen P., Stassen A. P., Bosch J. W., Vogels G. D., Guijt W., Haasnoot C. A. Elucidation of the structure of methanopterin, a coenzyme from Methanobacterium thermoautotrophicum, using two-dimensional nuclear-magnetic-resonance techniques. Eur J Biochem. 1984 Feb 1;138(3):563–571. doi: 10.1111/j.1432-1033.1984.tb07951.x. [DOI] [PubMed] [Google Scholar]

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