Research Topics
| C HunteSummaryAffiliation: Max Planck Institute of Biophysics Country: Germany Publications
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Detail Information
Publications
Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragmentC Hunte
Max Planck Institut fur Biophysik, Abt Molekulare Membranbiologie, Frankfurt, 60528, Germany
Structure 8:669-84. 2000..This integral membrane protein complex catalyzes electron transfer from ubiquinol to cytochrome c. It couples the electron transfer to the electrogenic translocation of protons across the membrane via a so-called Q cycle mechanism...- Protonmotive pathways and mechanisms in the cytochrome bc1 complexCarola Hunte
Department Molecular Membrane Biology, Max Planck Institute Biophysics, D 60439 Frankfurt am Main, Germany
FEBS Lett 545:39-46. 2003..In this review we discuss pathways for proton conduction linked to ubiquinone redox reactions with particular reference to recently determined structures of the yeast bc(1) complex... - Insights from the structure of the yeast cytochrome bc1 complex: crystallization of membrane proteins with antibody fragmentsC Hunte
Max Planck Institut fur Biophysik, Abteilung Molekulare Membranbiologie, Heinrich Hoffmann Strasse 7, D 60528, Frankfurt am Main, Germany
FEBS Lett 504:126-32. 2001..The high-resolution structure of the yeast protein reveals details of the catalytic sites of the complex, which are important for electron and proton transfer... - Specific protein-lipid interactions in membrane proteinsC Hunte
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max von Laue Str 3, D 60438 Frankfurt, Germany
Biochem Soc Trans 33:938-42. 2005.... - The monoclonal antibody 1F6 identifies a pH-dependent conformational change in the hydrophilic NH(2) terminus of NhaA Na(+)/H(+) antiporter of Escherichia coliM Venturi
Max Planck Institut fur Biophysik, Abteilung Molekulare Membranbiologie, Heinrich Hoffmann Strasse 7, D 60528 Frankfurt Main, Germany
J Biol Chem 275:4734-42. 2000.... - Crystallisation of membrane proteins mediated by antibody fragmentsCarola Hunte
Max Planck Institut fur Biophysik, Abt Molekulare Membranbiologie, Heinrich Hoffmann Strasse 7, D 60528 Frankfurt am Main, Germany
Curr Opin Struct Biol 12:503-8. 2002..Antibody-fragment-mediated crystallisation appears to be a valuable tool in particular for membrane proteins with very small hydrophilic or flexible domains... 
A structural analysis of the transient interaction between the cytochrome bc1 complex and its substrate cytochrome cAjeeta Nyola
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max von Laue Strasse 3, D 60438 Frankfurt am Main, Germany
Biochem Soc Trans 36:981-5. 2008....- Probing the role of E272 in quinol oxidation of mitochondrial complex IIITina Wenz
Department Molecular Membrane Biology, Max-Planck-Institute of Biophysics, 60438 Frankfurt am Main, Germany
Biochemistry 45:9042-52. 2006..The conserved glutamate appears to influence the accurate formation of the enzyme-substrate complex and to govern the efficiency of catalysis... - Mutational analysis of cytochrome b at the ubiquinol oxidation site of yeast complex IIITina Wenz
Department Molecular Membrane Biology, Max Planck Institute of Biophysics, D 60438 Frankfurt am Main, Germany
J Biol Chem 282:3977-88. 2007..Altered center N kinetics and activation of ubiquinol oxidation by binding of cytochrome c in the Y132F and E272D enzymes indicate long range effects of these mutations... - A comparison of stigmatellin conformations, free and bound to the photosynthetic reaction center and the cytochrome bc1 complexC Roy D Lancaster
Max Planck Institute of Biophysics, Max von Laue Str 3, D 60438 Frankfurt, Germany
J Mol Biol 368:197-208. 2007..The free rotation about the chi1 dihedral angle is an essential factor for allowing stigmatellin to bind in both the reaction center and the cytochrome bc1 pocket... - Redox-linked protonation state changes in cytochrome bc1 identified by Poisson-Boltzmann electrostatics calculationsAstrid R Klingen
Structural Biology Bioinformatics Group, University of Bayreuth, Germany
Biochim Biophys Acta 1767:204-21. 2007..The cardiolipin molecule bound close to the Q(i)-site stabilises protons in this cluster of lysine residues... - A structural perspective on mechanism and function of the cytochrome bc (1) complexCarola Hunte
Dept Molecular Membrane Biology, Max Planck Institute of Biophysics, 60438, Frankfurt, Germany
Results Probl Cell Differ 45:253-78. 2008..Yet, open questions regarding key steps of the mechanism still remain. The role of the complex as a major source of reactive oxygen species and its implication in pathophysiological conditions has recently gained interest... - Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transferSozanne R N Solmaz
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany
J Biol Chem 283:17542-9. 2008..Four core interactions encircle the heme cofactors surrounded by variable interactions. The core interface may be a feature to gain specificity for formation of the reactive complex... - Epitope mapping of conformational monoclonal antibodies specific to NhaA Na+/H+ antiporter: structural and functional implicationsAbraham Rimon
Department of Biochemistry, Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, 91904 Jerusalem, Israel
J Mol Biol 379:471-81. 2008..The revealed location of the mAbs suggests that mAb binding distorts the unique NhaA TMS IV/XI assembly and thus inhibits the activity of NhaA. The noninhibitory mAb 6F9 binds to the functionally dispensable C-terminus of NhaA... - Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pHCarola Hunte
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max von Laue Str 3, D 60438 Frankfurt, Germany
Nature 435:1197-202. 2005..This ion-exchange machinery is regulated by a conformational change elicited by a pH signal perceived at the entry to the cytoplasmic funnel... - Lipids in membrane protein structuresHildur Palsdottir
Department of Molecular Membrane Biology, Max-Planck-Institute of Biophysics, Marie-Curie-Strasse 15, D-60439 Frankfurt, Germany
Biochim Biophys Acta 1666:2-18. 2004..A newly identified cardiolipin binding site in the yeast cytochrome bc(1) complex is described. Assignment of unsaturated lipid chains and evolutionary aspects of lipid binding are discussed... - Electron transfer between yeast cytochrome bc(1) complex and cytochrome c: a structural analysisCarola Hunte
Max Planck Institute of Biophysics, Dept Molecular Membrane Biology, Heinrich Hoffmann Str 7, 60528 Frankfurt M, Germany
Biochim Biophys Acta 1555:21-8. 2002..Remarkably, CYC binds only to one of the two possible binding sites of the homodimeric complex and binding appears to be coordinated with the presence of ubiquinone at the Q(i) site. Regulatory aspects of CYC reduction are discussed... - Monoclonal antibodies for the structural analysis of the Na+/H+ antiporter NhaA from Escherichia coliMiro Venturi
Structural Biology Section, Vaccine Research Center National Institutes of Health, Bethesda, MD 20892, USA
Biochim Biophys Acta 1610:46-50. 2003..The generated conformation-specific antibody fragments are highly valuable reagents for co-crystallization attempts and structure determination of the antiporter... - Functional implications from an unexpected position of the 49-kDa subunit of NADH:ubiquinone oxidoreductaseVolker Zickermann
, Fachbereich Medizin, , D-60590 Frankfurt am Main, Germany
J Biol Chem 278:29072-8. 2003..This contradicts all hypothetical mechanisms discussed in the field that link proton translocation directly to redox events and suggests an indirect mechanism of proton pumping by redox-driven conformational energy transfer... - Structure of the yeast cytochrome bc1 complex with a hydroxyquinone anion Qo site inhibitor boundHildur Palsdottir
Abt. Molekulare Membranbiologie, , Marie-Curie-Strasse 15, D-60439 Frankfurt, Germany
J Biol Chem 278:31303-11. 2003..Binding of the alkyl-6-hydroxy-4,7-dioxobenzothiazole is discussed as resembling an intermediate step of ubiquinol oxidation, supporting a single occupancy model at the Qo site... 
Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome cChristian Lange
Max Planck Institute for Biophysics, Heinrich-Hoffmann-Strasse 7, D-60528 Frankfurt am Main, Germany
Proc Natl Acad Sci U S A 99:2800-5. 2002..Obviously, cytochrome c reduction by the cytochrome bc1 complex can be regulated in response to respiratory conditions...- Molecular basis for atovaquone binding to the cytochrome bc1 complexJacques J Kessl
Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755, USA
J Biol Chem 278:31312-8. 2003..These results provide the first molecular description of how atovaquone binds to the bc1 complex and explain the differential inhibition of the fungal versus mammalian enzymes... - Cardiolipin stabilizes respiratory chain supercomplexesKathy Pfeiffer
Zentrum der Biologischen Chemie, , D-60590 Frankfurt, Germany
J Biol Chem 278:52873-80. 2003..We show that a cardiolipin-deficient strain harbored almost inactive resting cytochrome c oxidase in the membrane. Transition to the fully active pulsed state occurred on a minute time scale... - Direct evidence for the interaction of stigmatellin with a protonated acidic group in the bc(1) complex from Saccharomyces cerevisiae as monitored by FTIR difference spectroscopy and 13C specific labelingMichaela Ritter
, , Theodor-Stern-Kai 7, Haus 74, 60590 Frankfurt am Main, Germany
Biochemistry 43:8439-46. 2004..Koepke, J., Lange, C., Rossmanith, T., and Michel, H. (2000) Structure 8, 669-684; Palsdottir, H., Lojero, C. G., Trumpower, B. L., and Hunte, C. (2003) J. Biol. Chem. 278, 31303-31311]... - Crucial steps in the structure determination of the Na+/H+ antiporter NhaA in its native conformationEmanuela Screpanti
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max von Laue Str 3, D 60438 Frankfurt, Germany
J Mol Biol 362:192-202. 2006..Thus, the antiporter is in a native conformation in the 3D crystals... - Lipids and membrane protein structuresCarola Hunte
Institute of Membrane and Systems Biology, University of Leeds, Leeds, UK
Curr Opin Struct Biol 18:406-11. 2008..Specific protein-lipid interactions not only require careful evaluation and interpretation, but also permit a directed approach to elucidate the structural and/or functional role of these interactions... - High level production of functional antibody Fab fragments in an oxidizing bacterial cytoplasmMiro Venturi
Max Planck Institut fur Biophysik, Abteilung für Molekulare Membranbiologie, Heinrich Hoffmann Str 7, Frankfurt am Main, D 60528, Germany
J Mol Biol 315:1-8. 2002..Such a capacity opens new perspectives for investigating metabolic and regulatory pathways in vivo and also provides a powerful selection system for functional genomics... - Monitoring redox-dependent contribution of lipids in Fourier transform infrared difference spectra of complex I from Escherichia coliRuth Hielscher
Institut fur Biophysik, Johann Wolfgang Goethe Universitat, Max von Laue Strasse 1, D 60438 Frankfurt am Main, Germany
Biopolymers 82:291-4. 2006.... - Cell free expression and functional reconstitution of eukaryotic drug transportersThorsten Keller
Institute of Anatomy and Cell Biology, University of Wurzburg, Koellikerstrasse 6, 97070 Wurzburg, Germany
Biochemistry 47:4552-64. 2008..The V max of PAH (-)/KG (2-) antiport was increased by Cl (-) in a manner independent of gradients, and PAH (-)/KG (2-) antiport was independent of membrane potential in the absence or presence of Cl (-)... - Modulation of the antigenic peptide transporter TAP by recombinant antibodies binding to the last five residues of TAP1Gabriele Plewnia
Institute of Biochemistry, Biocenter, Johann Wolfgang Goethe University, Max von Laue Strasse 9, D 69438 Frankfurt a M, Germany
J Mol Biol 369:95-107. 2007..Based on our results we suggest that the C terminus of TAP1 modulates TAP function presumably as part of the dimer interface of the NBDs... - Discontinuous membrane helices in transport proteins and their correlation with functionEmanuela Screpanti
Department Molecular Membrane Biology, Max Planck Institute of Biophysics, Max von Laue Str 3, D 60438 Frankfurt, Germany
J Struct Biol 159:261-7. 2007..The extended peptides with their backbone atoms, the helix termini and the polar/charged amino acid residues in close vicinity provide the basis for ion recognition, binding and translocation... - Multiconformation continuum electrostatics analysis of the NhaA Na+/H+ antiporter of Escherichia coli with functional implicationsElena Olkhova
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max von Laue Strasse 3, D 60438 Frankfurt am Main, Germany
Proc Natl Acad Sci U S A 103:2629-34. 2006..The results of the calculations provide valuable information on the activation of the antiporter and the role of individual amino acid residues, and provide a solid framework for further experiments...