Researcher Portfolio
Fritzsch, Günter
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, Department of Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society
Researcher Profile
Position: Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society
Position: Department of Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons137659
Publications
(1 - 25 of 60)
: Koepke, J., Krammer, E.-M., Klingen, A. R., Sebban, P., Ullmann, G. M., & Fritzsch, G. (2007). pH Modulates the Quinone Position in the Photosynthetic Reaction Center from Rhodobacter sphaeroides in the Neutral and Charge Separated States. Journal of Membrane Biology, 371(2), 396-409. doi:10.1016/j.jmb.2007.04.082. [PubMan] : Katsemi, V., Lücke, C., Koepke, J., Löhr, F., Maurer, S., Fritzsch, G., & Rüterjans, H. (2005). Mutational and Structural Studies of the Diisopropylfluorophosphatase from Loligo vulgaris Shed New Light on the Catalytic Mechanism of the Enzyme. Biochemistry, 44(25), 9022-9033. doi:10.1021/bi0500675. [PubMan] : Ma, X., Koepke, J., Panjikar, S., Fritzsch, G., & Stöckigt, J. (2005). Crystal Structure of Vinorine Synthase, the First Representative of the BAHD Superfamily. The Journal of Biological Chemistry, 280(14), 13576-13583. doi:10.1074/jbc.M414508200. [PubMan] : Ma, X., Koepke, J., Fritzsch, G., Diem, R., Kutchan, T. M., Michel, H., & Stöckigt, J. (2004). Crystallization and preliminary X-ray crystallographic analysis of strictosidine synthase from Rauvolfia: the first member of a novel enzyme family. Biochimica et Biophysica Acta-Proteins and Proteomics, 1702, 121-124. doi:10.1016/j.bbapap.2004.06.013. [PubMan] : Ma, X., Koepke, J., Bayer, A., Linhard, V., Fritzsch, G., Zhang, B., Michel, H., & Stöckigt, J. (2004). Vinorine synthase from Rauvolfia: the first example of crystallization and preliminary X-ray diffraction analysis of an enzyme of the BAHD superfamily. Biochimica et Biophysica Acta-Proteins and Proteomics, 1701(1-2), 129-132. doi:10.1016/j.bbapap.2004.06.011. [PubMan] : Koepke, J., Scharff, E. I., Luecke, C., Rueterjans, H., & Fritzsch, G. (2003). Statistical analysis of crystallographic data obtained from squid ganglion DFPase at 0.85 Å resolution. Acta Crystallographica. Section D: Biological Crystallography (Copenhagen), D59(10), 1744-1754. doi:10.1107/S0907444903016135. [PubMan] : Peng, G., Fritzsch, G., Zickermann, V., Schaegger, H., Mentele, R., Lottspeich, F., Bostina, M., Radermacher, M., Huber, R., Stetter, K. O., & Michel, H. (2003). Isolation, Characterization and Electron Microscopic Single Particle Analysis of the NADH:Ubiquinone Oxidoreductase (Complex I) from the Hyperthermophilic Eubacterium Aquifex aeolicus. Biochemistry, 42(10), 3032-3039. doi:10.1021/bi026876v. [PubMan] : Koepke, J., Scharff, E. I., Lücke, C., Rüterjans, H., & Fritzsch, G. (2002). Atomic resolution crystal structure of squid ganglion DFPase. Acta Crystallographica Section D-Biological Crystallography, D58(Part 10 Special Issue 1), 1757-1759. [PubMan] : Psylinakis, E., Fritzsch, G., & Ghanotakis, D. F. (2002). Isolation and crystallization of CP47, a Photosystem II chlorophyll binding protein. Degradation of CP47 upon dissociation from the core complex. Photosynthesis Research, 72(2), 211-216. doi:10.1023/A:1016136801753. [PubMan] : Fritzsch, G., Koepke, J., Diem, R., Kuglstatter, A., & Baciou, L. (2002). Charge separation induces conformational changes in the photosynthetic reaction centre of purple bacteria. Acta Crystallographica Section D-Biological Crystallography, D58(Part 10 Special Issue 1), 1660-1663. [PubMan] : Scharff, E. I., Koepke, J., Fritzsch, G., Lücke, C., & Rüterjahns, H. (2001). Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris. Structure, 9(6), 493-502. doi:10.1016/S0969-2126(01)00610-4. [PubMan] : Kuglstatter, A., Ermler, U., Michel, H., Baciou, L., & Fritzsch, G. (2001). X-ray Structure Analyses of Photosynthetic Reaction Center Variants from Rhodobacter sphaeroides: Structural Changes Induced by Point Mutations at Position L209 Modulate Electron and Proton Transfer. Biochemistry, 40(14), 4253-4260. doi:10.1021/bi001589h. [PubMan] : Scharff, E. I., Lücke, C., Fritzsch, G., Koepke, J., Hartleib, J., Dierl, S., & Rüterjans, H. (2001). Crystallization and preliminary X-ray crystallographic analysis of DFPase from Loligo vulgaris. Acta Crystallographica Section D-Biological Crystallography, 57(1), 148-149. doi:10.1107/S0907444900014232. [PubMan] : Kuglstatter, A., Miksovska, J., Sebban, P., & Fritzsch, G. (2000). Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides reconstituted with anthraquinone as primary quinone QA. FEBS Letters, (1), 114-116. doi:10.1016/S0014-5793(00)01447-2. [PubMan] : Kuglstatter, A., Hellwig, P., Fritzsch, G., Wachtveitl, J., Oesterhelt, D., Mäntele, W., & Michel, H. (1999). Identification of a hydrogen bond in the Phe M197→Tyr mutant reaction center of the photosynthetic purple bacterium Rhodobacter sphaeroides by X-ray crystallography and FTIR spectroscopy. FEBS Letters, 463(1-2), 169-174. doi:10.1016/s0014-5793(99)01614-2. [PubMan] : Fyfe, P. K., McAuley-Hecht, K. E., Ridge, J. P., Prince, S. M., Fritzsch, G., Isaacs, N. W., Cogdell, R. J., & Jones, M. R. (1998). Crystallographic studies of mutant reaction centres from Rhodobacter sphaeroides. Photosynthesis Research, 55, 133-140. doi:10.1023/A:1006095520441. [PubMan] : Fritzsch, G., Kampmann, L., Kapaun, G., & Michel, H. (1998). Water clusters in the reaction centre of Rhodobacter sphaeroides. Photosynthesis Research, 55, 127-132. doi:10.1023/A:1006088232755. [PubMan] : Fritzsch, G. (1998). Obtaining crystal structures from bacterial photosynthetic reaction centers. In Methods in Enzymology (pp. 57-77). Academic Press. doi:10.1016/S0076-6879(98)97007-0. [PubMan] : Somogyi, A. A., Rumrich, G., Fritzsch, G., & Ullrich, K. J. (1996). Stereospecificity in contraluminal and luminal transporters of organic cations in the rat renal proximal tubule. Journal of Pharmacology and Experimental Therapeutics, 278(1), 31-36. [PubMan] : Muegge, I., Apostolakis, J., Ermler, U., Fritzsch, G., Lubitz, W., & Knapp, E. (1996). Shift of the Special Pair Redox Potential: Electrostatic Energy Computations of Mutants of the Reaction Center from Rhodobacter sphaeroides. Biochemistry, 35(25), 8359-8370. doi:10.1021/bi952214c. [PubMan] : Apostolakis, J., Muegge, I., Ermler, U., Fritzsch, G., & Knapp, E. (1996). Free Energy Computations on the Shift of the Special Pair Redox Potential: Mutants of the Reaction Center of Rhodobacter sphaeroides. Journal of the American Chemical Society, 118(15), 3743-3752. doi:10.1021/ja9535219. [PubMan] : Fritzsch, G., Ermler, U., Merckel, M. C., & Michel, H. (1996). Crystallization and Structure of the Photosynthetic Reaction Centres from Rhodobacter sphaeroides - wild type and mutants. In M.-E. Michel-Beyerle (Ed. ), The Reaction Center of Photosynthetic Bacteria (pp. 3-13). Berlin, Heidelberg: Springer. [PubMan] : Muegge, I., Ermler, U., Fritzsch, G., & Knapp, E. W. (1995). Free Energy of Cofactors at the Quinone-QA Site of the Photosynthetic Reaction Center of Rhodobacter sphaeroides Calculated by Minimizing the Statistical Error. The Journal of Physical Chemistry, 99(51), 17917-17925. doi:10.1021/j100051a017. [PubMan] : Ermler, U., Fritzsch, G., Buchanan, S. K., & Michel, H. (1994). Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 A resolution: cofactors and protein-cofactor interactions. Structure, 2(10), 925-936. doi:10.1016/s0969-2126(94)00094-8. [PubMan] : Scherer, P., Fischer, S., Lancaster, C. R. D., Fritzsch, G., Schmidt, S., Arlt, T., Dressler, K., & Zinth, W. (1994). Time-resolved spectroscopy of the excited electronic state of reaction centers of Rhodopseudomonas viridis. Chemical Physics Letters, 223(1-2), 110-115. doi:10.1016/0009-2614(94)00427-7. [PubMan]