[N,N'-dicyclohexylcarbodiimide-sensitive K+-dependent ATPase activity in Escherichia coli].
ATPase activity sensitive to N,N'-dicyclohexylcarbodiimide and dependent on K+ content in medium is observed only in anaerobically grown Escherichia coli and as the analysis of mutants with defects in different subunits of (F0F1) H+-ATPase and in potassium transport shows only under the structural integrity of both F0F1 and K+-ionophore (the Trk system). The obtained results confirm the data on the H+/K+-exchange and indicate that the F0F1 and Trk systems in anaerobically grown bacteria unite into the same membrane supercomplex inside which the direct energy transfer occurs without a mediation of delta-mu H+.
Trchunian
A A
AA
Ogandzhanian
E S
ES
Martirosov
S M
SM
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000693:Anaerobiosis / Q000187:drug effects; D001692:Biological Transport / Q000187:drug effects; D002234:Carbodiimides / Q000494:pharmacology*; D027682:Cation Transport Proteins; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology*; D004926:Escherichia coli / Q000187:drug effects* / Q000201:enzymology; D009154:Mutation; D011188:Potassium / Q000378:metabolism; D011523:Protoplasts / Q000187:drug effects / Q000378:metabolism
D002234:Carbodiimides; D027682:Cation Transport Proteins; D004024:Dicyclohexylcarbodiimide; D000251:Adenosine Triphosphatases; C022761:potassium transporting ATPase; D011188:Potassium
Izuchenie N,N'-ditsiklogeksilkarbodiimid-chuvstvitel'noĭ K+-zavisimoĭ ATFaznoĭ aktivnosti u Escherichia coli.