Structural characterization and physiological function of component B from Methanosarcina thermophila

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.

DOI: 10.1007/BF00248487

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Cite this paper

@article{Clements2004StructuralCA, title={Structural characterization and physiological function of component B from Methanosarcina thermophila}, author={Andrew P. Clements and Robert White and James G. Ferry}, journal={Archives of Microbiology}, year={2004}, volume={159}, pages={296-300} }