Structural characterization and physiological function of component B from Methanosarcina thermophila |
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| Authors: | Andrew P. Clements Robert H. White James G. Ferry |
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| Affiliation: | (1) Department of Anaerobic Microbiology, Virginia Polytechnic Institute and State University, 24061 Blacksburg, VA, USA;(2) Department of Biochemistry and Nutrition, Virginia Polytechnic Institute and State University, 24061 Blacksburg, VA, USA |
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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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| Keywords: | Methanogenesis HS-HTP Coenzyme M CoM-S-S-HTP Heterodisulfide reductase CO dehydrogenase Hydrogenase Acetate Methanosarcina thermophila |
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