Abstract
When 7-mercaptoheptanoylthreonine phosphate (HS-HTP) was used as the sole source of electrons for reductive demethylation of 2-(methylthio)-ethanesulfonic acid (CH 3-S-CoM) by cell extracts of Methanobacterium thermoautotrophicum strain ΔH, the heterodisulfide of coenzyme M and HS-HTP (CoM-S-S-HTP) was quantitatively produced: HS-HTP + CH 3-S-CoM → CH 4 + CoM-S-S-HTP. CH 4 and CoM-S-S-HTP were produced stoichiometrically in a ratio of 1:1. Coenzyme M (HS-CoM) inhibited HS-HTP driven methanogenesis indicating that CH 3-S-CoM rather than HS-CoM was the substrate for CoM-S-S-HTP formation.
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