The ATP-driven primary Na+ pump in subcellular vesicles of Vibrio alginolyticus.
Subcellular vesicles of Vibrio alginolyticus hydrolyze ATP and accumulate Na+ in an ATP-dependent fashion. The Na+ uptake is (i) strongly stimulated by delta psi-discharging agents, i.e., the protonophorous uncoupler CCCP or valinomycin + K+ and (ii) arrested by DCCD at a concentration strongly inhibiting ATP hydrolysis. Lower concentrations of DCCD stimulate the Na+ accumulation supported by ATP hydrolysis as well as by NADH oxidation. It is concluded that there is an electrogenic DCCD-sensitive Na+-ATPase in the cytoplasmic membrane of V. alginolyticus.
Dibrov
P A
PA
Department of Bioenergetics, A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Skulachev
V P
VP
Sokolov
M V
MV
Verkhovskaya
M L
ML
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone / Q000494:pharmacology; D027682:Cation Transport Proteins; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D007700:Kinetics; D008954:Models, Biological; D011188:Potassium / Q000494:pharmacology; D012964:Sodium / Q000378:metabolism*; D013347:Subcellular Fractions / Q000201:enzymology; D014634:Valinomycin / Q000494:pharmacology; D014733:Vibrio / Q000201:enzymology*
D027682:Cation Transport Proteins; D014634:Valinomycin; D004024:Dicyclohexylcarbodiimide; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone; D000255:Adenosine Triphosphate; D012964:Sodium; D000251:Adenosine Triphosphatases; C021838:sodium-translocating ATPase; D011188:Potassium