%0 Journal Article %1 Xing_2004_2148 %A Xing, Jianhua %A Wang, Hongyun %A von Ballmoos, Christoph %A Dimroth, Peter %A Oster, George %D 2004 %J Biophys. J. %K ATPases; Adenosine Bacterial Biological; Chemical; Comparative Computer Conformation; Energy Fusobacteria; Gov't, Gov't; Models, Molecular Molecular; Motors; Non-P.H.S.; Non-U.S. P.H.S.; Protein Proton-Translocating Relationship; Research Simulation; Structure-Activity Study; Support, Torque Transfer; Triphosphate; U.S. %N 4 %P 2148--2163 %R 10.1529/biophysj.104.042093 %T Torque generation by the Fo motor of the sodium ATPase. %U http://dx.doi.org/10.1529/biophysj.104.042093 %V 87 %X Based on recent structural and functional findings, we have constructed a mathematical model for the sodium-driven Fo motor of the F1Fo-ATPase from the anaerobic bacterium Propionigenium modestum. The model reveals the mechanochemical principles underlying the Fo motor's operation, and explains all of the existing experimental data on wild-type and mutant Fo motors. In particular, the model predicts a nonmonotonic dependence of the ATP hydrolysis activity on the sodium concentration, a prediction confirmed by new experiments. To explain experimental observations, the positively charged stator residue (R227) must assume different positions in the ATP synthesis and hydrolysis directions. This work also illustrates how to extract a motor mechanism from dynamical experimental observations in the absence of complete structural information.

@article{Xing_2004_2148, abstract = {Based on recent structural and functional findings, we have constructed a mathematical model for the sodium-driven Fo motor of the F1Fo-ATPase from the anaerobic bacterium Propionigenium modestum. The model reveals the mechanochemical principles underlying the Fo motor's operation, and explains all of the existing experimental data on wild-type and mutant Fo motors. In particular, the model predicts a nonmonotonic dependence of the ATP hydrolysis activity on the sodium concentration, a prediction confirmed by new experiments. To explain experimental observations, the positively charged stator residue (R227) must assume different positions in the ATP synthesis and hydrolysis directions. This work also illustrates how to extract a motor mechanism from dynamical experimental observations in the absence of complete structural information.}, added-at = {2009-06-03T11:20:58.000+0200}, author = {Xing, Jianhua and Wang, Hongyun and von Ballmoos, Christoph and Dimroth, Peter and Oster, George}, biburl = {https://www.bibsonomy.org/bibtex/2cbf2b2958aabac308d8e4a3709614640/hake}, description = {The whole bibliography file I use.}, doi = {10.1529/biophysj.104.042093}, interhash = {07b00f68fbc9599332b25d3e5d323754}, intrahash = {cbf2b2958aabac308d8e4a3709614640}, journal = {Biophys. J.}, keywords = {ATPases; Adenosine Bacterial Biological; Chemical; Comparative Computer Conformation; Energy Fusobacteria; Gov't, Gov't; Models, Molecular Molecular; Motors; Non-P.H.S.; Non-U.S. P.H.S.; Protein Proton-Translocating Relationship; Research Simulation; Structure-Activity Study; Support, Torque Transfer; Triphosphate; U.S.}, month = Oct, number = 4, pages = {2148--2163}, pii = {87/4/2148}, pmid = {15454418}, timestamp = {2009-06-03T11:21:38.000+0200}, title = {Torque generation by the Fo motor of the sodium ATPase.}, url = {http://dx.doi.org/10.1529/biophysj.104.042093}, volume = 87, year = 2004 }