Acharya, P., M. Groenrich, C.H. Hagemeier, U. Demmer, J.A. Vorholt, R.K. Thauer and U. Ermler: How an enzyme binds the C-1 carrier tetrahydromethanopterin - Structure of the tetrahydromethanopterin-dependent formaldehyde-aactivating enzyme (Fae) from Methylobacterium extorquens AM1. J. Biol. Chem. 280, 13712-13719 (2005).

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

Barleben L., X.  Ma, J. Koepke, G. Peng, H. Michel and J. Stöckigt: Expression, purification, cyrystallization and preliminary X-ray analysis of strictosidine glucosidase, an enzyme initiating biosynthetic pathways to a unique diversity of indole alkaloid skeletons. Biochim. Biophys. Acta 1747, 89-92 (2005).

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

Fufezan, C., F. Drepper, H.D. Juhnke, C.R.D. Lancaster, S. Un, A.W. Rutherford and A. Krieger-Liszkay: Herbicide-induced changes in charge recombination and redox potential of Q_A in the T4 mutant of Blastochloris viridis. Biochemistry 44, 5931-5939 (2005).

Haas, A.H., U.S. Sauer, R. Groß, J. Simon, W. Mäntele and C.R.D. Lancaster: 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, 13949-13961 (2005).

Hofmann, C., H. Michel, M. van Heel and J. Köhler: Multivariate Analysis of Single-Molecule Spectra: Surpassing Spectral Diffusion. Phys. Rev. Lett. 94, 195501-1 - 195501-4 (2005).

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

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

Lancaster, C.R.D., U.S. Sauer, R. Groß, A.H. Haas, J. Graf, H. Schwalbe, W. Mäntele, J. Simon and M.G. Madej: Experimental support for the “E-pathway hypothesis” of coupled transmembrane e^- and H⁺ transfer in dihemic quinol:fumarate reductase. Proc. Natl. Acad. Sci. U.S.A. 102, 18860-18865 (2005).

Ma, X., J. Koepke, S. Panjikar, G. Fritzsch and J. Stöckigt: Crystal Structure of Vinorine Synthase, the First Representative of the BAHD Superfamily. J. Biol. Chem. 280, 13576-13583 (2005).

Mander, G.J., M.S. Weiss, R. Hedderich, J. Kahnt, U. Ermler and E. Warkentin: X-ray structure of the gamma-subunit of the dissimilatory sulfite reductase: redox-active and structural disulfide bonds. FEBS Lett. 579, 4600-4604 (2005).

Mileni, M., A.H. Haas, W. Mäntele, J. Simon and C.R.D. Lancaster: 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, 16718-16728 (2005).

Olkhova, E., V. Helms and H. Michel: Titration Behavior of Residues at the Entrance of the D-pathway of Cytochrome c Oxidase from Paracoccus denitrificans Investigated by Continuum Electrostatic Calculations. Biophys. J. 89, 2324-2331 (2005).

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

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

Srinivasan, V., C. Rajendran, F.L. Sousa, A.M. Melo, L.M. Saraiva, M.M. Pereira, M. Santana, M. Teixeira and H. Michel: Structure at 1.3 Å resolution of Rhodothermus marinus caa3 cytochrome c domain. J. Mol. Biol. 345, 1047-1057 (2005).

Warkentin, E., C.H. Hagemeier, S. Shima, R.K. Thauer and U. Ermler: The structure of F420-dependent methylenetetrahydromethanopterin dehydrogenase: a crystallographic ‘superstructure’ f the selenomethionine-labelled protein crystal structure. Acta Crystallogr. D61, 198-202 (2005).


Ph.D. Theses

Mileni, M.: Biochemical, structural and functional characterization of diheme-containing quinol:fumarate reductases: the role of heme propionates and the enzymes from pathogenic epsilon-proteobacteria. Frankfurt 2005.

Palsdottir, H.: Structure-function relationships in the cytochrome bc₁ complex from Saccharomyces cerevisiae. Frankfurt 2005.


Diploma Theses

Angerer, H.: Herstellung rekombinanter aa₃- und ba₃-Cytochrom-c-Oxidasen von Aeropyrum pernix K1 in Paracoccus denitrificans und Reinigung der Wildtyp-aa₃- und ba₃-Cytochrom-c-Oxidasen aus Aeropyrum pernix K1. Frankfurt 2005.

Berner, N.M.:  Produktion der C₄-Dicarboxylat-Transporter DcuA, DcuB, DcuC und “Transporter” aus Salmonella typhimurium in Escherichia coli. Frankfurt 2005.

Hiltscher, H.: Generierung durch gezielten Aminosäureaustausch von Varianten der Succinat-Dehydrogenase aus Wolinella succinogenes und deren Charakterisierung. Frankfurt 2005.

Marcia, M.: Purification and Characterization of the Sulfide:Quinone Oxidoreductase and the Cytochrome bd:Quinol Oxidase from Aquifex aeolicus. Bologna and Frankfurt 2005.

Schäfer, U.: Untersuchungen zur Interaktion zwischen Cytochrom-bc₁-Komplex und Cytochrom c. Frankfurt 2005.