Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1990.tb19331.x/fullpdf
Reference26 articles.
1. Novel biochemistry of methanogenesis.
2. Evidence that the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate is a product of the methylreductase reaction in Methanobacterium
3. The final step in methane formation. Investigations with highly purified methyl-CoM reductase (component C) from Methanobacterium thermoautotrophicum (strain Marburg)
4. Methyl-coenzyme-M reductase from Methanobacterium thermoautotrophicum (strain Marburg). Purity, activity and novel inhibitors
5. Methanobacterium thermoautotrophicum contains a soluble enzyme system that specifically catalyzes the reduction of the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate with H2
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