Zobrazeno 1 - 10
of 56
pro vyhledávání: '"Günter Fritzsch"'
Autor:
Günter Fritzsch, Pierre Sebban, Astrid R. Klingen, Eva-Maria Krammer, G. Matthias Ullmann, Juergen Koepke
Publikováno v:
Journal of Molecular Biology. 371:396-409
The structure of the photosynthetic reaction-center from Rhodobacter sphaeroides has been determined at four different pH values (6.5, 8.0, 9.0, 10.0) in the neutral and in charge separated states. At pH 8.0, in the neutral state, we obtain a resolut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f9e559692054b2ff4b1f59584e783f3
https://doi.org/10.1016/j.jmb.2007.04.082
https://doi.org/10.1016/j.jmb.2007.04.082
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 61:690-693
Strictosidine synthase (STR1) is a central enzyme that participates in the biosynthesis of almost all plant monoterpenoid indole alkaloids. After heterologous expression in Escherichia coli, crystals of STR1 and its substrate complex with tryptamine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97a64cea8bec18431d82b1531bc6f218
https://doi.org/10.1107/s0907444904029348
https://doi.org/10.1107/s0907444904029348
Autor:
Hartmut Michel, Joachim Stöckigt, Juergen Koepke, Anja Bayer, Bin Zhang, Xueyan Ma, Günter Fritzsch, Verena Linhard
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1701:129-132
Crystals of vinorine synthase (VS) from medicinal plant Rauvolfia serpentina expressed in Escherichia coli have been obtained by the hanging-drop technique at 305 K with ammonium sulfate and PEG 400 as precipitants. The enzyme is involved in the bios
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0aa370f585a322a11c98bcf2e8c026d
https://doi.org/10.1016/j.bbapap.2004.06.011
https://doi.org/10.1016/j.bbapap.2004.06.011
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 58:1660-1663
X-ray structures of the wild-type reaction centre from Rhodobacter sphaeroides have been determined to a resolution of 1.87 Å in the neutral (dark) state and to 2.06 Å in the charge-separated (light-excited) state. Whereas the overall protein struc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3721efd4264a23a89b65ee9ac29ec168
https://doi.org/10.1107/s0907444902014178
https://doi.org/10.1107/s0907444902014178
Publikováno v:
Structure. 9:493-502
Background: Phosphotriesterases (PTE) are enzymes capable of detoxifying organophosphate-based chemical warfare agents by hydrolysis. One subclass of these enzymes comprises the family of diisopropylfluorophosphatases (DFPases). The DFPase reported h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd00b2fd1a2797ad960b542dc3416306
https://doi.org/10.1016/s0969-2126(01)00610-4
https://doi.org/10.1016/s0969-2126(01)00610-4
Autor:
Josef Wachtveitl, Hartmut Michel, Petra Hellwig, Andreas Kuglstatter, Werner Mäntele, Dieter Oesterhelt, Günter Fritzsch
Publikováno v:
FEBS Letters. 463:169-174
In bacterial reaction centers the charge separation process across the photosynthetic membrane is predominantly driven by the excited state of the bacteriochlorophyll dimer (D). An X-ray structure analysis of the Phe M197→Tyr mutant reaction center
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b1ca6e39dec9d96855208025a3384025
https://doi.org/10.1016/s0014-5793(99)01614-2
https://doi.org/10.1016/s0014-5793(99)01614-2
Publikováno v:
Photosynthesis Research. 55:127-132
The structure of the reaction centre from Rhodobacter sphaeroides has been refined up to 2.4 A resolution. Several clusters of firmly bound water molecules were found proximal to the primary and secondary quinones. They represent putative pathways fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e007c3dabd0338beb234974346fab36d
https://doi.org/10.1023/a:1006088232755
https://doi.org/10.1023/a:1006088232755
Autor:
Neil W. Isaacs, Steve M. Prince, Günter Fritzsch, Katherine E. McAuley-Hecht, Michael R. Jones, Justin P. Ridge, Paul K. Fyfe, Richard J. Cogdell
Publikováno v:
Photosynthesis Research. 55:133-140
X-ray structures have been determined for five mutant reaction centres from Rhodobacter sphaeroides, at resolutions varying between 3.4 A and 2.3 A. The aim was to examine the effects of mutagenesis of polar residues in the binding pocket of the reac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::901c8cffd43736207b0d779e82761b29
https://doi.org/10.1023/a:1006095520441
https://doi.org/10.1023/a:1006095520441
Publikováno v:
Journal of the American Chemical Society. 118:3743-3752
Shifts of the special pair redox potential of photosynthetic reaction centers of Rhodobacter sphaeroides for five different mutants are considered. The shifts are calculated by the method of free energy perturbation which is based on dynamics simulat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2b2639dcfa74860f75189541b632ba7d
https://doi.org/10.1021/ja9535219
https://doi.org/10.1021/ja9535219
Publikováno v:
The Journal of Physical Chemistry. 99:17917-17925
The free energy difference of the binding of benzoquinones and naphthoquinones at the Q{sub A} site of the photosynthetic reaction center from Rhodobacter sphaeroides immersed in water and hexane is calculated and compared with experimental values. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4b03bc7214590357171df5a63a0eef1f
https://doi.org/10.1021/j100051a017
https://doi.org/10.1021/j100051a017