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Structural characterization and physiological function of component B from Methanosarcina thermophila

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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.

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Authors and Affiliations

  1. Department of Anaerobic Microbiology, Virginia Polytechnic Institute and State University, 24061, Blacksburg, VA, USA

    Andrew P. Clements & James G. Ferry

  2. Department of Biochemistry and Nutrition, Virginia Polytechnic Institute and State University, 24061, Blacksburg, VA, USA

    Robert H. White

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  1. Andrew P. Clements
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  2. Robert H. White
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  3. James G. Ferry
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Clements, A.P., White, R.H. & Ferry, J.G. Structural characterization and physiological function of component B from Methanosarcina thermophila . Arch. Microbiol. 159, 296–300 (1993). https://doi.org/10.1007/BF00248487

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  • DOI: https://doi.org/10.1007/BF00248487

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