Structural characterization and physiological function of component B from Methanosarcina thermophila

Andrew P. Clements, Robert H. White, James Gregory Ferry

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

The electron donor (component B) to the methyl coenzyme M methylreductase system from Methanosarcina thermophila was isolated as the 7-methyl derivative and characterized. Gas chromatography-mass spectrometry and 1H NMR analyses identified this derivative as 7-methylthioheptanoylthreonine phosphate (CH3-S-HTP), indicating that the original component B had the same structure (HS-HTP) as previously determined for component B from Methanobacterium thermoautotrophicum. The heterodisulfide of HS-HTP and coenzyme M (HS-CoM, 2-mercaptoethanesulfonate) was enzymatically reduced in cell extracts using electrons supplied by either H2 or CO, confirming that HS-HTP was a functional molecule in M. thermophila.

Original languageEnglish (US)
Pages (from-to)296-300
Number of pages5
JournalArchives of Microbiology
Volume159
Issue number3
DOIs
StatePublished - Mar 1 1993

All Science Journal Classification (ASJC) codes

  • Microbiology

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