Affiliation: University of Virginia
- Rotational coupling in the F0F1 ATP synthaseR K Nakamoto
Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville 22906, USA
Annu Rev Biophys Biomol Struct 28:205-34. 1999..Mutational analyses have shown that the rotor subunits are responsible for coupling and in doing so transmit specific conformational information between transport and catalysis...
- Molecular mechanisms of rotational catalysis in the F(0)F(1) ATP synthaseR K Nakamoto
Department of Molecular Physiology and Biological Physics, University of Virginia, P O Box 10011, Charlottesville, VA 22906 0011, USA
Biochim Biophys Acta 1458:289-99. 2000..Amino acid replacements in the transport domain also affect the steady state catalytic transition state indicating that rotation is involved in coupling to transport...
- Mitochondria in nonalcoholic fatty liver diseaseStephen H Caldwell
Division of Gastroenterology and Hepatology, University of Virginia Health System, PO Box 800708, Charlottesville, VA 22908, USA
Clin Liver Dis 8:595-617, x. 2004..The prominent role of mitochondrial dysfunction in NAFL provides a new and exciting paradigm in which to view this disorder, its complications, and potential dietary and pharmacologic intervention...
- Determination of the partial reactions of rotational catalysis in F1-ATPaseJoanne A Baylis Scanlon
Department of Molecular Physiology and Biological Physics, University of Virginia, P O Box 800736, Charlottesville, Virginia 22908 0736, USA
Biochemistry 46:8785-97. 2007..P., Leslie, A. G. W., Lutter, R., and Walker, J. E. (1994) Nature 370, 621-628)...
- The rotary mechanism of the ATP synthaseRobert K Nakamoto
Department of Molecular Physiology and Biological Physics, University of Virginia, P O Box 800736, Charlottesville, VA 22908 0736, USA
Arch Biochem Biophys 476:43-50. 2008..This review addresses the role of rotation in catalysis of ATP synthesis/hydrolysis and the transport of protons or sodium...
- A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysisJoanne A Baylis Scanlon
Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia 22908, USA
J Biol Chem 283:26228-40. 2008..This analysis provides additional insights into how the enzyme achieves efficient coupling and implicates the betaGlu-381 residue for proper formation of the rate-limiting transition state involving gamma subunit rotation...
- F0 cysteine, bCys21, in the Escherichia coli ATP synthase is involved in regulation of potassium uptake and molecular hydrogen production in anaerobic conditionsNelli Mnatsakanyan
Department of Biophysics, Yerevan State University, 1 Alex Manougian Street, 375049 Yerevan, Armenia
Biosci Rep 22:421-30. 2002..These results indicate a role for the F0 subunit bCys21 in the functionality of F0F1 and coupling to other membranous activities under fermentative conditions...
- Special issue on transport ATPasesGiuseppe Inesi
Arch Biochem Biophys 476:1-2. 2008