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. 1985 Jul;163(1):126–131. doi: 10.1128/jb.163.1.126-131.1985

Evidence of a common pathway of carbon dioxide reduction to methane in methanogens.

W J Jones, M I Donnelly, R S Wolfe
PMCID: PMC219089  PMID: 3924891

Abstract

The roles of methanofuran and tetrahydromethanopterin as carriers of C1 moieties in the reduction of carbon dioxide to methane were studied in representatives of diverse groups of methanogens, confirming that these roles, first reported for Methanobacterium thermoautotrophicum, are common for methanogenesis in general. Extracts of the methanogens tested converted formyl-methanofuran and methyl-tetrahydromethanopterin to methane; the extractable cofactors derived from the same methanogens, with one exception, complemented a methanofuran- and tetrahydromethanopterin-deficient enzyme system from M. thermoautotrophicum. The amounts of extractable methanofuran and tetrahydromethanopterin were determined for each representative methanogen.

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Selected References

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  1. Balch W. E., Fox G. E., Magrum L. J., Woese C. R., Wolfe R. S. Methanogens: reevaluation of a unique biological group. Microbiol Rev. 1979 Jun;43(2):260–296. doi: 10.1128/mr.43.2.260-296.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Balch W. E., Wolfe R. S. Specificity and biological distribution of coenzyme M (2-mercaptoethanesulfonic acid). J Bacteriol. 1979 Jan;137(1):256–263. doi: 10.1128/jb.137.1.256-263.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. Gunsalus R. P., Wolfe R. S. Stimulation of CO2 reduction to methane by methylcoenzyme M in extracts Methanobacterium. Biochem Biophys Res Commun. 1977 Jun 6;76(3):790–795. doi: 10.1016/0006-291x(77)91570-4. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. Leigh J. A. Levels of water-soluble vitamins in methanogenic and non-methanogenic bacteria. Appl Environ Microbiol. 1983 Mar;45(3):800–803. doi: 10.1128/aem.45.3.800-803.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Leigh J. A., Rinehart K. L., Jr, Wolfe R. S. Methanofuran (carbon dioxide reduction factor), a formyl carrier in methane production from carbon dioxide in Methanobacterium. Biochemistry. 1985 Feb 12;24(4):995–999. doi: 10.1021/bi00325a028. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. McBride B. C., Wolfe R. S. A new coenzyme of methyl transfer, coenzyme M. Biochemistry. 1971 Jun 8;10(12):2317–2324. doi: 10.1021/bi00788a022. [DOI] [PubMed] [Google Scholar]
  13. Mullakhanbhai M. F., Larsen H. Halobacterium volcanii spec. nov., a Dead Sea halobacterium with a moderate salt requirement. Arch Microbiol. 1975 Aug 28;104(3):207–214. doi: 10.1007/BF00447326. [DOI] [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., 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]
  16. 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]
  17. SISTROM W. R. The kinetics of the synthesis of photopigments in Rhodopseudomonas spheroides. J Gen Microbiol. 1962 Sep;28:607–616. doi: 10.1099/00221287-28-4-607. [DOI] [PubMed] [Google Scholar]
  18. Schloss J. V., Phares E. F., Long M. V., Norton I. L., Stringer C. D., Hartman F. C. Isolation, characterization, and crystallization of ribulosebisphosphate carboxylase from autotrophically grown Rhodospirillum rubrum. J Bacteriol. 1979 Jan;137(1):490–501. doi: 10.1128/jb.137.1.490-501.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. 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]
  20. Whitman W. B., Ankwanda E., Wolfe R. S. Nutrition and carbon metabolism of Methanococcus voltae. J Bacteriol. 1982 Mar;149(3):852–863. doi: 10.1128/jb.149.3.852-863.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Whitman W. B., Wolfe R. S. Activation of the methylreductase system from Methanobacterium bryantii by ATP. J Bacteriol. 1983 May;154(2):640–649. doi: 10.1128/jb.154.2.640-649.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. 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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