Publications of the Department of Molecular Membrane Biology

Lancaster, C. R. D.; Sauer, U. S.; Groß, R.; Haas, A.; Graf, J.; Schwalbe, H.; Mäntele, W.; Simon, J.; Madej, G. M.: Experimental support for the "E pathway hypothesis" of coupled transmembrane e^- and H⁺ transfer in dihemic quinol:fumarate reductase. Proceedings of the National Academy of Sciences of the United States of America 102 (52), pp. 18860 - 18865 (2005)

Mileni, M.; Haas, A. H.; Mäntele, W.; Simon, J.; Lancaster, C. R. D.: Probing Heme Propionate Involvement in Transmembrane Proton Transfer Coupled to Electron Transfer in Dihemic Quinol: Fumarate Reductase by ¹³C-Labeling and FTIR Difference Spectroscopy. Biochemistry 44 (50), pp. 16718 - 16728 (2005)

Haas, A. H.; Sauer, U. S.; Gross, R.; Simon, J.; Mäntele, W.; Lancaster, C. R. D.: FTIR Difference Spectra of Wolinella succinogenes Quinol: Fumarate Reductase Support a Key Role of Glu C180 within the "E-Pathway Hypothesis" of Coupled Transmembrane Electron and Proton Transfer. Biochemistry 44 (42), pp. 13949 - 13961 (2005)

Olkhova, E.; Helms, V.; Michel, H.: Titration Behavior of Residues at the Entrance of the D-Pathway of Cytochrome c Oxidase from Paracoccus denitrificans Investigated by Continuum Electrostatic Calculations. Biophysical Journal 89 (4), pp. 2324 - 2331 (2005)

Zuber, D.; Krause, R.; Venturi, M.; Padan, E.; Bamberg, E.; Fendler, K.: Kinetics of charge translocation in the passive downhill uptake mode of the Na⁺/H⁺ antiporter NhaA of Escherichia coli. Biochimica et Biophysica Acta, Bioenergetics 1709 (3), pp. 240 - 250 (2005)

Mander, G. J.; Weiss, M. S.; Hedderich, R.; Kahnt, J.; Ermler, U.; Warkentin, E.: X-ray structure of the γ-subunit of a dissimilatory sulfite reductase: Fixed and flexible C-terminal arms. FEBS Letters 579 (21), pp. 4600 - 4604 (2005)

Aufhammer, S. W.; Warkentin, E.; Ermler, U.; Hagemeier, C. H.; Thauer, R. K.; Shima, S.: Crystal structure of methylenetetrahydromethanopterin (Mer) in complex with coenzyme F₄₂₀: Architecture of the F₄₂₀/FMN binding site of enzymes within the nonprolyl cis-peptide containing bacterial luciferase family. Protein Science 14 (7), pp. 1840 - 1849 (2005)

Hunte, C.; Screpanti, E.; Venturi, M.; Rimon, A.; Padan, E.; Michel, H.: Structure of a Na⁺/H⁺ antiporter and insights into mechanism of action and regulation by pH. Nature 435 (7046), pp. 1197 - 1202 (2005)

Katsemi, V.; Lücke, C.; Koepke, J.; Löhr, F.; Maurer, S.; Fritzsch, G.; Rüterjans, H.: Mutational and Structural Studies of the Diisopropylfluorophosphatase from Loligo vulgaris Shed New Light on the Catalytic Mechanism of the Enzyme. Biochemistry 44 (25), pp. 9022 - 9033 (2005)

Scheffel, F.; Warkentin, E.; Hülsmann, A.; Schneider, E.; Ermler, U.: Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius. FEBS Letters 579 (13), pp. 2953 - 2958 (2005)

Hofmann, C.; Michel, H.; van Heel, M.; Köhler, J.: Multivariate Analysis of Single-Molecule Spectra: Surpassing Spectral Diffusion. Physical Review Letters 94 (19), 195501 (2005)

Acharya, P.; Gornrich, M.; Hagemeier, C.; Vorholt, J. A.; Thauer, R. K.; Ermler, U.: How an Enzyme Binds the C₁ Carrier Tetrahydromethanopterin. Structure of the Tetrahydromethanopterin-Dependent Formaldehyde-Activating Enzyme (Fae) from Methylobacterium extorquens AM1. The Journal of Biological Chemistry 280 (14), pp. 13712 - 13719 (2005)

Ma, X.; Koepke, J.; Panjikar, S.; Fritzsch, G.; Stöckigt, J.: Crystal Structure of Vinorine Synthase, the First Representative of the BAHD Superfamily. The Journal of Biological Chemistry 280 (14), pp. 13576 - 13583 (2005)

Fufezan, C.; Drepper, F.; Juhnke, H.; Lancaster, C. R. D.; Un, S.; Rutherford, A.W.; Krieger-Liszkay, A.: Herbicide-induced Changes in Charge Recombination and Redox Potential of Q_A in the T4 Mutant of Blastochloris viridis. Biochemistry 44 (15), pp. 5931 - 5939 (2005)

Barleben, L.; Ma, X.; Koepke, J.; Peng, G.; Michel, H.; Stöckigt, J.: Expression, purification, crystallization and preliminary X-ray analysis of strictosidine glucosidase, an enzyme initiating biosynthetic pathways to a unique diversity of indole alkaloid skeletons. Proteins & Proteomics, pp. 89 - 92 (2005)

Srinivasan, V.; Rajendran, C.; Sousa, F. L.; Melo, A. M.P.; Saraiva, L. M.; Pereira, M. M.; Santana, M.; Teixeira, M.; Michel, H.: Structure at 1.3 Å Resolution of Rhodothermus marinus caa₃ Cytochrome c Domain. Journal of Molecular Biology (London) 345 (5), pp. 1047 - 1057 (2005)

Ermler, U.: On the mechanism of methyl-coenzyme M reductase. Dalton Transactions 21, pp. 3451 - 3458 (2005)

Richter, O.-M. H.; Dürr, K. L.; Kannt, A.; Ludwig, B.; Scandurra, F. M.; Giuffrè, A.; Sarti, P.; Hellwig, P.: Probing the access of protons to the K pathway in the Paracoccus denitrificans cytochrome c oxidase. The FEBS Journal 272 (2), pp. 404 - 412 (2005)

Warkentin, E.; Hagemeier, C.; Shima, S.; Thauer, R. K.; Ermler, U.: The structure of F₄₂₀-dependent methylenetetrahydromethanopterin dehydrogenase: a crystallographic 'superstructure' of the selenomethionine-labelled protein crystal structure. Acta Crystallographica. Section D: Biological Crystallography (Copenhagen), pp. 198 - 202 (2005)

Pálsdóttir, H.: Structure-function relationships in the cytochrome bc₁ complex from Saccharomyces cerevisiae. Dissertation, 139 pp., Fachbereich 14: Chemische und Pharmazeutische Wissenschaften, Johann Wolfgang Goethe-Universität Frankfurt, Frankfurt am Main (2005)