Add time:08/05/2019         Source:sciencedirect.com

Cell extracts of Methanobacterium thermoautotrophicum (strain Marburg) were found to catalyze the reduction of the heterodisulfide of coenzyme M (CoM-S-H) and 7-mercaptoheptanoylthreonine phosphate (cas 104302-77-4) (H-S-HTP) with H2. All the activity was associated with the soluble cell fraction (160 000 × g supernatant). The enzyme system was purified sevenfold by anion-exchange chromatography. The partially purified system had a specific activity of 100 nmol CoM-S-S-HTP reduced per min and mg protein and exhibited an apparent Km for CoM-S-S-HTP of below 0.1 mM. The homodisulfides of CoM-S-H, of H-S-HTP, of cysteine, and of glutathione were not reduced. NADPH and NADH could not substitute for H2 as electron donor.

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