Robert H. Fillingame
Position title: Professor Emeritus
Phone: (608) 262-1439
6204A Biochemical Sciences Building
440 Henry Mall, Madison, WI 53706
• BS 1968, Washington State University
• PhD 1973, University of Washington, Seattle
• Postdoctoral, 1973-75, Harvard Medical School (E.P. Kennedy)
Honors & Awards
• Medical Alumni Named Professorship, 1988
• NIH Merit Award, 1994
• WARF Mid-Career Faculty Researcher Award, 1998
• Dean’s Teaching Award (School of Medicine), 2008
• Chancellor’s Teaching Award , 2012
My research focuses on the molecular mechanism of ATP synthesis during oxidative phosphorylation. ATP synthesis is driven by a trans membrane proton gradient generated by the electron transport system. The enzyme catalyzing ATP synthesis is biologically unique in using the electrochemical energy of the proton gradient to drive the rotation of a molecular motor which in turn drives ATP synthesis. The ATP synthase has been termed the “world’s smallest rotary motor”. The process works as follows. Proton transport through the Fo membrane sector of the enzyme is coupled with the rotation of a molecular rotor composed of multiple c subunits. The c oligomeric rotor in turn drives ATP synthesis via the rotation of two attached subunits (gamma and epsilon) which cycle between circularly arranged multiple catalytic sites in the extramembranous F1 sector of the enzyme. In the complete process of ATP synthesis the electrochemical energy of the proton gradient is converted into mechanical energy and, via structural/mechanical changes in the catalytic sites, ultimately into the chemical energy of ATP. Our long term goal is to elucidate the structure and molecular mechanism of this fascinating machine.
Perform a customized PubMed literature search for Robert H. Fillingame
- Steed, P.R., K.A. Kraft, and R.H. Fillingame. (2014). Interacting cytoplasmic loops of subunits a and c of Escherichia coli F1F0 ATP synthase gate H+ transport to the cytoplasm. Proceedings of the National Academy of Sciences of the United States of America, 111: 16730-5.
- Fillingame, R.H., and P.R. Steed. (2014). Half channels mediating H(+) transport and the mechanism of gating in the Fo sector of Escherichia coli F1Fo ATP synthase. Biochimica et biophysica acta, 1837: 1063-8.
- Steed, P.R., and R.H. Fillingame. (2014). Residues in the polar loop of subunit c in Escherichia coli ATP synthase function in gating proton transport to the cytoplasm. The Journal of biological chemistry, 289: 2127-38.
- Moore, K.J., and R.H. Fillingame. (2013). Obstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase. The Journal of biological chemistry, 288: 25535-41.
- DeLeon-Rangel, J., R.R. Ishmukhametov, W. Jiang, R.H. Fillingame, and S.B. Vik. (2013). Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking. FEBS letters, 587: 892-7.
- Uhlemann, E.M., H.E. Pierson, R.H. Fillingame, and O.Y. Dmitriev. (2012). Cell-free synthesis of membrane subunits of ATP synthase in phospholipid bicelles: NMR shows subunit a fold similar to the protein in the cell membrane. Protein science : a publication of the Protein Society, 21: 279-88.
- Dong, H., and R.H. Fillingame. (2010). Chemical reactivities of cysteine substitutions in subunit a of ATP synthase define residues gating H+ transport from each side of the membrane. The Journal of biological chemistry, 285: 39811-8.
- Steed, P.R., and R.H. Fillingame. (2009). Aqueous accessibility to the transmembrane regions of subunit c of the Escherichia coli F1F0 ATP synthase. The Journal of biological chemistry, 284: 23243-50.
- Moore, K.J., and R.H. Fillingame. (2008). Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase. The Journal of biological chemistry, 283: 31726-35.
- Moore, K.J., C.M. Angevine, O.D. Vincent, B.E. Schwem, and R.H. Fillingame. (2008). The cytoplasmic loops of subunit a of Escherichia coli ATP synthase may participate in the proton translocating mechanism. The Journal of biological chemistry, 283: 13044-52.