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Methanobacterium thermoautotrophicum contains a soluble enzyme system that specifically catalyzes the reduction of the heterodisulfide of coenzyme M and 7‐mercaptoheptanoylthreonine phosphate with H 2
Author(s) -
Hedderich R.,
Thauer R.K.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81339-5
Subject(s) - methanobacterium , cofactor , enzyme , chemistry , cysteine , biochemistry , stereochemistry , glutathione , atp synthase , enzyme assay , archaea , gene
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 (H‐S‐HTP) with H 2 . 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 K m 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 H 2 as electron donor.