ATP synthesis by F-type ATP synthase is obligatorily dependent on the transmembrane voltage.
ATP synthase is the universal enzyme that manufactures cellular ATP using the energy stored in a transmembrane ion gradient. This energy gradient has two components: the concentration difference (DeltapH or DeltapNa(+)) and the electrical potential difference DeltaPsi, which are thermodynamically equivalent. However, they are not kinetically equivalent, as the mitochondrial and bacterial ATP synthases require a transmembrane potential, DeltaPsi, but the chloroplast enzyme has appeared to operate on DeltapH alone. Here we show that, contrary to the accepted wisdom, the 'acid bath' procedure used to study the chloroplast enzyme develops not only a DeltapH but also a membrane potential, and that this potential is essential for ATP synthesis. Thus, for the chloroplast and other ATP synthases, the membrane potential is the fundamental driving force for their normal operation. We discuss the biochemical reasons for this phenomenon and a model that is consistent with these new experimental facts.
Kaim
G
G
Mikrobiologisches Institut, Eidgenössische Technische Hochschule, ETH-Zentrum, Schmelzbergstrasse 7, CH-8092 Zürich, Switzerland.
Dimroth
P
P
D000255:Adenosine Triphosphate / Q000096:biosynthesis*; D002264:Carboxylic Acids / Q000737:chemistry; D002463:Cell Membrane Permeability; D004926:Escherichia coli / Q000235:genetics; D006863:Hydrogen-Ion Concentration; D008564:Membrane Potentials; D011424:Propionibacterium / Q000201:enzymology; D006180:Proton-Translocating ATPases / Q000378:metabolism*
D002264:Carboxylic Acids; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases