Methanobacterium thermoautotrophicum contains a soluble enzyme system that specifically catalyzes the reduction of the heterodisulfide of coenzyme M and 7‐mercaptoheptanoylthreonine phosphate with H2

FEBS Letters

Thauer, R.K.¹  Hedderich, R.¹ 

[1] Mikrobiologie, Fachbereich Biologie, Philipps-Universität, Karl-von-Frisch-Straße, D-3550 Marburg, FRG

关键词: Methanogenic bacteria;    Methane formation;    Coenzyme M;    7-Mercaptoheptanoylthreonine phosphate;    Component B;    Methyl-CoM reductase;    Vitamin B12;    Hydrogenase;   

DOI  :  10.1016/0014-5793(88)81339-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 H₂. 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 H₂ as electron donor.

【 授权许可】

Unknown