Skip to main content
PMC 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
. 1988 Jan;85(1):60–63. doi: 10.1073/pnas.85.1.60

Physiological importance of the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate in the reduction of carbon dioxide to methane in Methanobacterium.

T A Bobik 1, R S Wolfe 1
PMCID: PMC279481  PMID: 3124103

Abstract

The heterodisulfide of the two coenzymes 2-mercaptoethanesulfonic acid (coenzyme M, HS-CoM) and N-(7-mercaptoheptanoyl)threonine O3-phosphate (HS-HTP) increased the rate of CO2 reduction to methane by cell extracts 42-fold. The stimulation resulted from activation of the initial step of methanogenesis, the production of formylmethanofuran from methanofuran and CO2. These results establish a role for this heterodisulfide (CoM-S-S-HTP) in the reduction of CO2 to formylmethanofuran. Evidence indicates that CoM-S-S-HTP is the labile intermediate that accounts for the coupling of the reduction of 2-(methylthio)ethanesulfonic acid by the methylreductase to formylmethanofuran biosynthesis, the "RPG effect." The heterodisulfide was found to be labile in cell extracts due to enzyme-catalyzed reduction and possibly thioldisulfide exchange.

Full text

PDF
60

Selected References

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

  1. Ankel-Fuchs D., Thauer R. K. Methane formation from methyl-coenzyme M in a system containing methyl-coenzyme M reductase, component B and reduced cobalamin. Eur J Biochem. 1986 Apr 1;156(1):171–177. doi: 10.1111/j.1432-1033.1986.tb09563.x. [DOI] [PubMed] [Google Scholar]
  2. Bobik T. A., Donnelly M. I., Rinehart K. L., Jr, Wolfe R. S. Structure of a methanofuran derivative found in cell extracts of Methanosarcina barkeri. Arch Biochem Biophys. 1987 May 1;254(2):430–436. doi: 10.1016/0003-9861(87)90121-4. [DOI] [PubMed] [Google Scholar]
  3. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  4. CLELAND W. W. DITHIOTHREITOL, A NEW PROTECTIVE REAGENT FOR SH GROUPS. Biochemistry. 1964 Apr;3:480–482. doi: 10.1021/bi00892a002. [DOI] [PubMed] [Google Scholar]
  5. DiMarco A. A., Donnelly M. I., Wolfe R. S. Purification and properties of the 5,10-methenyltetrahydromethanopterin cyclohydrolase from Methanobacterium thermoautotrophicum. J Bacteriol. 1986 Dec;168(3):1372–1377. doi: 10.1128/jb.168.3.1372-1377.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Donnelly M. I., Wolfe R. S. The role of formylmethanofuran: tetrahydromethanopterin formyltransferase in methanogenesis from carbon dioxide. J Biol Chem. 1986 Dec 15;261(35):16653–16659. [PubMed] [Google Scholar]
  7. ELLMAN G. L. A colorimetric method for determining low concentrations of mercaptans. Arch Biochem Biophys. 1958 Apr;74(2):443–450. doi: 10.1016/0003-9861(58)90014-6. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. Ellermann J., Kobelt A., Pfaltz A., Thauer R. K. On the role of N-7-mercaptoheptanoyl-O-phospho-L-threonine (component B) in the enzymatic reduction of methyl-coenzyme M to methane. FEBS Lett. 1987 Aug 17;220(2):358–362. doi: 10.1016/0014-5793(87)80846-3. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. 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]
  12. 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]
  13. Hartzell P. L., Wolfe R. S. Requirement of the nickel tetrapyrrole F430 for in vitro methanogenesis: reconstitution of methylreductase component C from its dissociated subunits. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6726–6730. doi: 10.1073/pnas.83.18.6726. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Hartzell P. L., Zvilius G., Escalante-Semerena J. C., Donnelly M. I. Coenzyme F420 dependence of the methylenetetrahydromethanopterin dehydrogenase of Methanobacterium thermoautotrophicum. Biochem Biophys Res Commun. 1985 Dec 31;133(3):884–890. doi: 10.1016/0006-291x(85)91218-5. [DOI] [PubMed] [Google Scholar]
  15. Jones W. J., Nagle D. P., Jr, Whitman W. B. Methanogens and the diversity of archaebacteria. Microbiol Rev. 1987 Mar;51(1):135–177. doi: 10.1128/mr.51.1.135-177.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. 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]
  17. 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]
  18. Noll K. M., Donnelly M. I., Wolfe R. S. Synthesis of 7-mercaptoheptanoylthreonine phosphate and its activity in the methylcoenzyme M methylreductase system. J Biol Chem. 1987 Jan 15;262(2):513–515. [PubMed] [Google Scholar]
  19. Noll K. M., Rinehart K. L., Jr, Tanner R. S., Wolfe R. S. Structure of component B (7-mercaptoheptanoylthreonine phosphate) of the methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum. Proc Natl Acad Sci U S A. 1986 Jun;83(12):4238–4242. doi: 10.1073/pnas.83.12.4238. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Noll K. M., Wolfe R. S. The role of 7-mercaptoheptanoylthreonine phosphate in the methylcoenzyme M methylreductase system from Methanobacterium thermoautotrophicum. Biochem Biophys Res Commun. 1987 May 29;145(1):204–210. doi: 10.1016/0006-291x(87)91307-6. [DOI] [PubMed] [Google Scholar]
  21. 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]
  22. 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]
  23. 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