7‐Mercaptoheptanoylthreonine phosphate functions as component B in ATP‐independent methane formation from methyl‐CoM with reduced cobalamin as electron donor

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Abstract
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.