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7‐Mercaptoheptanoylthreonine phosphate functions as component B in ATP‐independent methane formation from methyl‐CoM with reduced cobalamin as electron donor
Author(s) -
Ankel-Fuchs D.,
Böcher R.,
Thauer R.K.,
Noll K.M.,
Wolfe R.S.
Publication year - 1987
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(87)81476-x
Subject(s) - cobalamin , methanobacterium , chemistry , phosphate , methane , biochemistry , stereochemistry , adenosine triphosphate , organic chemistry , vitamin b12 , archaea , gene
Purified methyl‐CoM reductase of Methanobacterium thermoautotrophicum (strain Marburg) catalyzed the reduction of methyl‐CoM to methane with reduced cobalamin, when either synthetic 7‐mercaptoheptanoyl‐threonine phosphate (HS‐HTP) or naturally occurring component B was present. With both compounds the same maximal specific acitivity was obtained and ATP was neither required nor stimulatory. These findings indicate that HS‐HTP functions as component B and do not support the idea that HS‐HT is only active in an adenosine monophosphorylated form.