Abstract

The proton-ATPase is a crucial transport enzyme in bacteria, plants and animals. It is also responsible for most of the ATP synthesis in these systems. Our work has shown that the enzyme requires both metal (magnesium) and tightly-bound nucleotide in order to function. Our current research is aimed at finding out how these moieties are used by the enzyme. This is the most complex enzyme known, and its function is of topical importance since it converts chemical and electrical energy at high efficiency at ordinary temperatures.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM025349-08
Application #
3272956
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1978-09-01
Project End
1986-08-31
Budget Start
1985-09-01
Budget End
1986-08-31
Support Year
8
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of Rochester
Department
Type
Schools of Medicine
DUNS #
208469486
City
Rochester
State
NY
Country
United States
Zip Code
14627

  Publications

Senior, Alan E; Muharemagic, Alma; Wilke-Mounts, Susan (2006) Assembly of the stator in Escherichia coli ATP synthase. Complexation of alpha subunit with other F1 subunits is prerequisite for delta subunit binding to the N-terminal region of alpha. Biochemistry 45:15893-902
Ahmad, Zulfiqar; Senior, Alan E (2006) Inhibition of the ATPase activity of Escherichia coli ATP synthase by magnesium fluoride. FEBS Lett 580:517-20
Ahmad, Zulfiqar; Senior, Alan E (2005) Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase. J Biol Chem 280:27981-9
Ahmad, Zulfiqar; Senior, Alan E (2005) Identification of phosphate binding residues of Escherichia coli ATP synthase. J Bioenerg Biomembr 37:437-40
Wilkens, Stephan; Borchardt, Dan; Weber, Joachim et al. (2005) Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy. Biochemistry 44:11786-94
Ahmad, Zulfiqar; Senior, Alan E (2005) Involvement of ATP synthase residues alphaArg-376, betaArg-182, and betaLys-155 in Pi binding. FEBS Lett 579:523-8
Weber, Joachim; Senior, Alan E (2004) Fluorescent probes applied to catalytic cooperativity in ATP synthase. Methods Enzymol 380:132-52
Weber, Joachim; Wilke-Mounts, Susan; Nadanaciva, Sashi et al. (2004) Quantitative determination of direct binding of b subunit to F1 in Escherichia coli F1F0-ATP synthase. J Biol Chem 279:11253-8
Weber, Joachim; Muharemagic, Alma; Wilke-Mounts, Susan et al. (2004) Analysis of sequence determinants of F1Fo-ATP synthase in the N-terminal region of alpha subunit for binding of delta subunit. J Biol Chem 279:25673-9
Senior, Alan E; Weber, Joachim (2004) Happy motoring with ATP synthase. Nat Struct Mol Biol 11:110-2

Showing the most recent 10 out of 90 publications