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

FEBS Letters

Thauer, R.K.²  Böcher, R.²  Wolfe, R.S.¹  Noll, K.M.¹  Ankel-Fuchs, D.² 

[1] Department of Microbiology, University of Illinois, 407 South Goodwin Avenue, Urbana, IL 61801, USA;Fachbereich Biologie-Mikrobiologie, Philipps Universität, Karl-von-Frisch-Straße, D-3550 Marburg, FRG

关键词: Methanogenesis;    Methyl-CoM reductase;    Component B;    7-Mercaptoheptanoylthreonine phosphate;    (Methanobacterium);   

DOI  :  10.1016/0014-5793(87)81476-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown