These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: External succinate and potassium ions influence Dcu dependent FOF1-ATPase activity and H+ flux of Escherichia coli at different pHs.
    Author: Mikoyan G, Karapetyan L, Vassilian A, Trchounian A, Trchounian K.
    Journal: J Bioenerg Biomembr; 2020 Oct; 52(5):377-382. PubMed ID: 32700240.
    Abstract:
    During fermentation Escherichia coli transport succinate mainly via Dcu family carriers. Current paper describes the role of externally added succinate on N'N'-dicyclohexylcarbodiimide (DCCD) sensitive ATPase activity and H+ flux depending on potassium ions. At pH 7.5 in wild type membrane vesicles DCCD-sensitive ATPase activity was the same as in dcuACBD quadruple mutant. In dcuACB it was increased ~ 3.3 fold while in dcuD DCCD-sensitive ATPase activity was absent. The DCCD-sensitive H+ efflux was fully dependent on FOF1 only in dcuACB mutant. This activity depended on potassium ions and only in dcuACBD mutant DCCD-sensitive ATPase activity was stimulated ~ 3 fold. At pH 5.5 DCCD-sensitive ATPase activities were determined in dcuACB or dcuD mutants but not in wild type. Interestingly, addition of potassium ions enhanced DCCD-sensitive ATPase activity in dcuD mutant ~ 3-fold compared to wild type. In dcuD mutant ~ 3-fold higher H+ uptake was registered, compared to wild type. Taken together it can be concluded that at pH 7.5 the FOF1-activity depends on DcuACB. Moreover, DcuACB but not DcuD are working towards H+ uptake direction. DcuD contributes to H+ efflux at pH 7.5 while at pH 5.5 it affects H+ influx when external succinate is present.
    [Abstract] [Full Text] [Related] [New Search]