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Structure and Methylation of Coenzyme M (HSCH2CH2SO3)
Open accessAbstract
Coenzyme M is a recently discovered cofactor which is involved in methyl transfer reactions in Methanobacterium. Information derived from infrared, proton NMR, and ultraviolet spectroscopy as well as from chemical tests and quantitative elemental analysis reveals that the coenzyme is 2,2′-dithiodiethanesulfonic acid. Verification of this structure resides in the comparison of authentic with chemically synthesized 2,2′-dithiodiethanesulfonic acid. Evidence indicates that an active form of this cofactor is 2-mercaptoethanesulfonic acid which is methylated producing 2-(methylthio) ethanesulfonic acid; this derivative is subsequently reductively demethylated, yielding methane.
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Cited by
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Thauer, R. K., Jungermann, K., & Decker, K. (1977) · Bacteriological Reviews · doi:10.1128/br.41.1.100-180.1977 · Cited by 4,146
Phylogenetic structure of the prokaryotic domain: The primary kingdoms
Woese, C. R., & Fox, G. E. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.11.5088 · Cited by 4,131
Balch, W. E., & Wolfe, R. S. (1976) · Applied and Environmental Microbiology · doi:10.1128/aem.32.6.781-791.1976 · Cited by 916
Self-citationGroundworks for an evolutionary biochemistry: The iron-sulphur world
Wächtershäuser, G. (1992) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(92)90022-x · Cited by 677
Use of “Specific” Inhibitors in Biogeochemistry and Microbial Ecology
Oremland, R. S., & Capone, D. G. (1988) · Advances in Microbial Ecology · doi:10.1007/978-1-4684-5409-3_8 · Cited by 498
Metadata
- Authors
- Taylor, C. D., & Wolfe, R. S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1974-08
- Volume
- 249
- Issue
- 15
- Pages
- 4879-4885
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1584539705
- Cited by
- 252
- References
- 0
- FWCI
- 3.07
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Taylor, C. D., & Wolfe, R. S. (1974). Structure and Methylation of Coenzyme M (HSCH2CH2SO3). Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)42403-4
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