Open AccessThe methyl‐tetrahydromethanopterin: Coenzyme M methyltransferase of Methanosarcina strain Gö1 is a primary sodium pump
Author(s) -
Becher Burkhard,
Müller Volker,
Gottschalk Gerhard
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05215.x
Subject(s) - chemistry , sodium , amiloride , biochemistry , chromosomal translocation , cytosol , enzyme , organic chemistry , gene
Washed invested vesicle preparations of Methanosarcina strain Gö1 catalyzed the formation of methyl‐CoM from formaldehyde, H 2 and CoM in the presence of tetrahydromethanopterin and 2‐bromoethanesulfonate. The reaction was associated with the translocation of sodium ions into the lumen of the vesicles. This translocation was abolished by the Na + ionophore ETH 157 but it was insensitive to the addition of the uncoupler SF6847 and the Na + /H + antiport inhibitor amiloride and, therefore, is the result of a primary Na + pump. Since the translocation of Na + was also observed when formaldehyde + tetrahydromethanopterin was replaced by methyl‐tetrahydromethanopterin, it follows that the methyl transfer from tetrahydromethanopterin to CoM is the sodium‐motive reaction. Methyl‐tetrahydromethanopterin could be replaced by methyl‐tetrahydrofolate.