RT journal article
T1 Evidence for Escherichia coli DcuD carrier dependent FOF1-ATPase activity during fermentation of glycerol
A1 Karapetyan, L.
A1 Valle Gallardo, Antonio
A1 Bolívar Pérez, Jorge
A1 Trchounian, A.
A1 Trchounian, K.
A2 Bioquímica y Biología MolecularMicrobiología, Medicina Preventiva, Salud Pública
AB During fermentation Escherichia coli excrete succinate mainly via Dcu family carriers. Current workreveals the total and N,N’-dicyclohexylcarbodiimide (DCCD) inhibited ATPase activity at pH 7.5 and 5.5in E. coli wild type and dcu mutants upon glycerol fermentation. The overall ATPase activity was highestat pH 7.5 in dcuABCD mutant. In wild type cells 50% of the activity came from the FOF1-ATPase but indcuD mutant it reached ~80%. K+ (100 mM) stimulate total but not DCCD inhibited ATPase activity 40%and 20% in wild type and dcuD mutant, respectively. 90% of overall ATPase activity was inhibited byDCCD at pH 5.5 only in dcuABC mutant. At pH 7.5 the H+ fluxes in E. coli wild type, dcuD and dcuABCDmutants was similar but in dcuABC triple mutant the H+ flux decreased 1.4 fold reaching 1.15 mM/minwhen glycerol was supplemented. In succinate assays the H+ flux was higher in the strains where DcuDis absent. No significant differences were determined in wild type and mutants specific growth rateexcept dcuD strain. Taken together it is suggested that during glycerol fermentation DcuD has impacton H+ fluxes, FOF1-ATPase activity and depends on potassium ions.
PB Nature Publishing Group
SN 2045-2322
YR 2019
FD 2019-03
LK http://hdl.handle.net/10498/21180
UL http://hdl.handle.net/10498/21180
LA eng
DS Repositorio Institucional de la Universidad de Cádiz
RD 07-nov-2026