Krasnoselskaya I A, Papa S, Skulachev V P
A.N. Belozersky Laboratory for Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
FEBS Lett. 1991 Jun 24;284(2):273-6. doi: 10.1016/0014-5793(91)80702-5.
An F0F1-ATPase was isolated from the membranes of the marine bacterium Vibrio alginolyticus. Homology between the subunits of the F0-complexes from E. coli and V. alginolyticus was found using antibodies against subunits a, b and c of the E. coli F0F1-ATPase. The F0F1-complex from V. alginolyticus was reconstituted into proteoliposomes, which were competent in ATP-dependent proton uptake. This process was inhibited by triphenyltin, DCCD, and venturicidin. Na+ did not affect proton translocation.
从海洋细菌溶藻弧菌的膜中分离出一种F0F1 - ATP酶。利用针对大肠杆菌F0F1 - ATP酶亚基a、b和c的抗体，发现大肠杆菌和溶藻弧菌F0复合物的亚基之间存在同源性。将溶藻弧菌的F0F1复合物重组到蛋白脂质体中，该蛋白脂质体具有依赖ATP的质子摄取能力。此过程受到三苯基锡、二环己基碳二亚胺（DCCD）和抗霉素A的抑制。钠离子不影响质子转运。
