Abstract
The biochemistry of methanogenesis is characterized by the involvement of unique coenzymes [1]. Consequently, investigation of the enzymology of the pathway by which carbon dioxide is reduced to methane has been severely constrained. Until recently, only a single substrate of the pathway was known, 2-(methylthio)ethanesulfonate (CH3-S-CoM).The methylreductase system which catalyzes the reduction of CH3-S-CoM to methane has been extensively studied, but here, too, lack of knowledge of the components involved has hampered progress. The enzyme system consists of at least four proteins and displays an absolute requirement for a heat-stable cofactor, component B [2]. We have recently established that component B is 7-mercaptoheptanoylthreonine phosphate (HS-HTP) [3]. This structure was proposed based on analysis of the authentic cofactor and was confirmed by its complete chemical synthesis
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