Dr. Joachim Weber
Title: Associate Professor
Education: Ph.D., Medical University of Lübeck, Germany, 1990
Postdoctoral, University of Rochester, NY, 1990-1995
Research Assistant Professor, University of Rochester, NY, 1995-2003
Research Area: Biochemistry
Office: Chemistry 413-D
Webpage: Research Group
Principal Research Interests
- ATP Synthase – The World's Smallest Rotary Motor
- Mutational Analysis of Enzymatic Function
- Biophysical Chemistry
Dr. Weber's current work focuses on the question how ATP binding and hydrolysis in the catalytic site drive subunit rotation, using a variety of approaches. The applied techniques range from molecular biology (site-directed mutagenesis) to biochemistry (protein chemistry, enzyme kinetics) to biophysical chemistry (fluorescence spectroscopy) and molecular modeling. Molecular dynamics simulations and torque measurements by single-molecule analysis are performed in collaboration with other laboratories. Noteworthy recent results of this research were (a) the identification of the catalytically-active nucleotide binding site, (b) the functional analysis of a unique hydrogen-bonding network between two subunits of the enzyme, and (c) further insight into the coupling mechanism between catalysis and rotation.
Research in Dr. Weber's lab is supported by the NIH.
- "Escherichia coli ATP synthase with a b/delta fusion protein allows analysis of the functions of the individual b subunits", Gajadeera, C.S.; Weber, J., J. Biol. Chem. 2013, 288, in press.
- "P-glycoprotein is fully active after multiple tryptophan substitutions", Swartz, D.J.; Weber, J.; Urbatsch, I.L., Biochim. Biophys. Acta 2013, 1828, 1159-1168.
- "The beta subunit loop that couples catalysis and rotation in ATP synthase has a critical length", Mnatsakanyan, N.; Kemboi, S.K.; Salas, J.; Weber, J., J. Biol. Chem. 2011, 286, 29788-29796.
- "Toward the ATP synthase mechanism", Weber, J., Nat. Chem. Biol. 2010, 6, 794-795.
- "ATP synthase with its gamma subunit reduced to the N-terminal helix can still catalyze ATP synthesis", Mnatsakanyan, N.; Hook, J.A.; Quisenberry, L.; Weber, J., J. Biol. Chem. 2009, 284, 26519-26525.
- "The role of the betaDELSEED-loop of ATP synthase", Mnatsakanyan, N.; Krishnakumar, A.M.; Suzuki, T.; Weber, J., J. Biol. Chem. 2009, 284, 11336-11345.
- "An essential hydrogen-bonding network at the beta(DP)/alpha(DP) interface of ATP synthase", Mao, H.Z.; Abraham, C.G.; Krishnakumar, A.M.; Weber, J. J. Biol. Chem., 2008, 283, 24781-24788.
- "Identification of the beta(TP) site in the x-ray structure of F1-ATPase as the high-affinity catalytic site", Mao, H.Z.; Weber, J. Proc. Natl. Acad. Sci. U. S. A.2007, 104, 18478-18483.
- "ATP synthase - the structure of the stator stalk", Weber, J. Trends Biochem. Sci. 2007, 32, 53-56.
- "Does F1-ATPase have a catalytic site that preferentially binds MgADP?", Mao, H.Z.; Gray, W.D.; Weber, J. FEBS Lett. 2006, 580, 4131-4135.
- "ATP synthase: subunit-subunit interactions in the stator stalk", Weber, J. Biochim. Biophys. Acta2006, 1757, 1162-1170.
- "Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy", Wilkens, S.; Borchardt, D.; Weber, J.; Senior, A.E. Biochemistry2005, 44, 11786-11794.
- "Happy motoring with ATP synthase", Senior, A.E.; Weber, J. Nature Struct. Mol. Biol.2004, 11, 110-112.
- "Fluorescent probes applied to catalytic cooperativity in ATP synthase", Weber, J.; Senior, A.E. Methods Enzymol.2004, 380, 132-152.
- "Quantitative determination of direct binding of b subunit to F1 in Escherichia coli F1F0-ATP synthase", Weber, J.; Wilke-Mounts, S.; Nadanaciva, S.; Senior, A.E. J. Biol. Chem.2004, 279, 11253-11258.