Evidence for Escherichia coli DcuD carrier dependent FOF1-ATPase activity during fermentation of glycerol

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URI: http://hdl.handle.net/10498/21180
DOI: 10.1038/s41598-019-41044-0
ISSN: 2045-2322
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2019-03Department
Bioquímica y Biología Molecular, Microbiología, Medicina Preventiva, Salud PúblicaSource
SCIENTIFIC REPORTS, 2019 Vol. 9 art. 4279Abstract
During fermentation Escherichia coli excrete succinate mainly via Dcu family carriers. Current work
reveals the total and N,N’-dicyclohexylcarbodiimide (DCCD) inhibited ATPase activity at pH 7.5 and 5.5
in E. coli wild type and dcu mutants upon glycerol fermentation. The overall ATPase activity was highest
at pH 7.5 in dcuABCD mutant. In wild type cells 50% of the activity came from the FOF1-ATPase but in
dcuD 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 by
DCCD at pH 5.5 only in dcuABC mutant. At pH 7.5 the H+ fluxes in E. coli wild type, dcuD and dcuABCD
mutants was similar but in dcuABC triple mutant the H+ flux decreased 1.4 fold reaching 1.15 mM/min
when glycerol was supplemented. In succinate assays the H+ flux was higher in the strains where DcuD
is absent. No significant differences were determined in wild type and mutants specific growth rate
except dcuD strain. Taken together it is suggested that during glycerol fermentation DcuD has impact
on H+ fluxes, FOF1-ATPase activity and depends on potassium ions.
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