Experts and Doctors on rhodobacter sphaeroides in Germany

Summary

Locale: Germany
Topic: rhodobacter sphaeroides

Top Publications

  1. Geisselbrecht Y, Frühwirth S, Schroeder C, Pierik A, Klug G, Essen L. CryB from Rhodobacter sphaeroides: a unique class of cryptochromes with new cofactors. EMBO Rep. 2012;13:223-9 pubmed publisher
    ..The latter closely resembles the iron-sulphur cluster harbouring the large primase subunit PriL, indicating that PriL is evolutionarily related to the CryPro class of cryptochromes. ..
  2. Borovykh I, Ceola S, Gajula P, Gast P, Steinhoff H, Huber M. Distance between a native cofactor and a spin label in the reaction centre of Rhodobacter sphaeroides by a two-frequency pulsed electron paramagnetic resonance method and molecular dynamics simulations. J Magn Reson. 2006;180:178-85 pubmed
    ..Both MD methods yield similar distances, but the second method has a trend towards a wider distance distribution. ..
  3. Jäger S, Jager A, Klug G. CIRCE is not involved in heat-dependent transcription of groESL but in stabilization of the mRNA 5'-end in Rhodobacter capsulatus. Nucleic Acids Res. 2004;32:386-96 pubmed
    ..The RNA structure leads to a slight stabilization of the groESL mRNA that is more pronounced at normal growth temperature than under heat shock conditions. ..
  4. Flores M, Savitsky A, Paddock M, Abresch E, Dubinskii A, Okamura M, et al. Electron-nuclear and electron-electron double resonance spectroscopies show that the primary quinone acceptor QA in reaction centers from photosynthetic bacteria Rhodobacter sphaeroides remains in the same orientation upon light-induced reduction. J Phys Chem B. 2010;114:16894-901 pubmed publisher
    ..Our results show that Q(A) is initially in an orientation that is favorable for its light-driven reduction. This diminishes the reorganization requirements for fast electron reduction and high quantum efficiency. ..
  5. Sadeghian K, Bocola M, Schütz M. A conclusive mechanism of the photoinduced reaction cascade in blue light using flavin photoreceptors. J Am Chem Soc. 2008;130:12501-13 pubmed publisher
    ..The flip of these two residues might be the trigger for the large conformational change of this protein which is consequently transmitted as the signal to the biological environment. ..
  6. Sinnecker S, Flores M, Lubitz W. Protein-cofactor interactions in bacterial reaction centers from Rhodobacter sphaeroides R-26: effect of hydrogen bonding on the electronic and geometric structure of the primary quinone. A density functional theory study. Phys Chem Chem Phys. 2006;8:5659-70 pubmed
    ..The significance of hydrogen bonding to the quinone cofactors in biological systems is discussed. ..
  7. Roy A, Shukla A, Haase W, Michel H. Employing Rhodobacter sphaeroides to functionally express and purify human G protein-coupled receptors. Biol Chem. 2008;389:69-78 pubmed
    ..To the best of our knowledge, this is the first report of successful use of a bacterial host--R. sphaeroides--to produce functional recombinant GPCRs under the control of a photosynthetic gene promoter. ..
  8. Metz S, Haberzettl K, Frühwirth S, Teich K, Hasewinkel C, Klug G. Interaction of two photoreceptors in the regulation of bacterial photosynthesis genes. Nucleic Acids Res. 2012;40:5901-9 pubmed publisher
    ..These results elucidate for the first time how a bacterial cryptochrome affects gene expression. ..
  9. Woelke A, Galstyan G, Galstyan A, Meyer T, Heberle J, Knapp E. Exploring the possible role of Glu286 in CcO by electrostatic energy computations combined with molecular dynamics. J Phys Chem B. 2013;117:12432-41 pubmed publisher

More Information

Publications44

  1. Hendrischk A, Braatsch S, Glaeser J, Klug G. The phrA gene of Rhodobacter sphaeroides encodes a photolyase and is regulated by singlet oxygen and peroxide in a sigma(E)-dependent manner. Microbiology. 2007;153:1842-51 pubmed
    ..Thus, the sigma(E) regulon is involved not only in the response to singlet oxygen but also in the hydrogen peroxide response. ..
  2. Kwa L, Wegmann D, Brugger B, Wieland F, Wanner G, Braun P. Mutation of a single residue, beta-glutamate-20, alters protein-lipid interactions of light harvesting complex II. Mol Microbiol. 2008;67:63-77 pubmed
    ..These findings suggest that the LH2 complex, specifically beta-glutamate-20 and the carotenoids' polar head group, contribute to the shaping of the photosynthetic membrane by specific interactions with surrounding lipid molecules. ..
  3. Erb T, Fuchs G, Alber B. (2S)-Methylsuccinyl-CoA dehydrogenase closes the ethylmalonyl-CoA pathway for acetyl-CoA assimilation. Mol Microbiol. 2009;73:992-1008 pubmed publisher
    ..This allowed defining the minimum set of enzymes necessary for its operation and to screen for further organisms following this acetyl-CoA assimilation strategy. ..
  4. Drepper T, Arvani S, Rosenau F, Wilhelm S, Jaeger K. High-level transcription of large gene regions: a novel T(7) RNA-polymerase-based system for expression of functional hydrogenases in the phototrophic bacterium Rhodobacter capsulatus. Biochem Soc Trans. 2005;33:56-8 pubmed
  5. Cherepanov D, Krishtalik L, Mulkidjanian A. Photosynthetic electron transfer controlled by protein relaxation: analysis by Langevin stochastic approach. Biophys J. 2001;80:1033-49 pubmed
    ..Because the vast majority of the biological ET reactions are only slightly exothermic (DeltaG > or = -100 meV), the relaxationally controlled ET is likely to prevail in proteins. ..
  6. Klingen A, Ullmann G. Negatively charged residues and hydrogen bonds tune the ligand histidine pKa values of Rieske iron-sulfur proteins. Biochemistry. 2004;43:12383-9 pubmed
    ..Interestingly, the shift caused by neutralizing the negative charges in ferredoxin Rieske proteins is larger than the shift caused by removing the hydrogen bonds toward the cluster in bc-type Rieske proteins. ..
  7. Ishikita H, Loll B, Biesiadka J, Galstyan A, Saenger W, Knapp E. Tuning electron transfer by ester-group of chlorophylls in bacterial photosynthetic reaction center. FEBS Lett. 2005;579:712-6 pubmed
    ..This can be traced back to different orientations of the B(A) ester-group. This tuning ability of chlorophyll redox potentials modulates the electron transfer from SP* to B(A). ..
  8. Erb T, Retey J, Fuchs G, Alber B. Ethylmalonyl-CoA mutase from Rhodobacter sphaeroides defines a new subclade of coenzyme B12-dependent acyl-CoA mutases. J Biol Chem. 2008;283:32283-93 pubmed publisher
    ..In combination with molecular modeling, two signature sequences were identified that presumably contribute to the substrate specificity of these enzymes. ..
  9. Kohring G, Wiehr P, Jeworski M, Giffhorn F. Stereoselective oxidation of aliphatic diols and reduction of hydroxy-ketones with galactitol dehydrogenase from Rhodobacter sphaeroides D. Commun Agric Appl Biol Sci. 2003;68:309-12 pubmed
    ..The wide substrate spectrum on one hand and the selectivity in the reaction on the other hand make GDH a very interesting enzyme for the production of optically pure building blocks in the chemical synthesis of bioactive compounds. ..
  10. Koepke J, Krammer E, Klingen A, Sebban P, Ullmann G, Fritzsch G. pH modulates the quinone position in the photosynthetic reaction center from Rhodobacter sphaeroides in the neutral and charge separated states. J Mol Biol. 2007;371:396-409 pubmed
    ..These extended proton-transfer pathways, ending at either of the two oxo-groups of QB in its proximal position, provide additional evidence that ring-flipping is not required for complete protonation of QB upon reduction. ..
  11. Ishikita H, Knapp E. Energetics of proton transfer pathways in reaction centers from Rhodobacter sphaeroides. The Glu-H173 activated mutants. J Biol Chem. 2005;280:12446-50 pubmed
    ..bRC possesses subunit H, which has no counterpart in photosystem II. Thus, bRC may possess alternative PT pathways involving water channels in subunit H, which becomes active in case the main PT pathway is blocked. ..
  12. Zirak P, Penzkofer A, Schiereis T, Hegemann P, Jung A, Schlichting I. Photodynamics of the small BLUF protein BlrB from Rhodobacter sphaeroides. J Photochem Photobiol B. 2006;83:180-94 pubmed
    ..The flavin-semiquinone further reduces and the reduced flavin re-oxidizes back in the dark. A photo-dynamics scheme is presented and relevant quantum efficiencies and time constants are determined. ..
  13. Remes B, Rische Grahl T, Müller K, Förstner K, Yu S, Weber L, et al. An RpoHI-Dependent Response Promotes Outgrowth after Extended Stationary Phase in the Alphaproteobacterium Rhodobacter sphaeroides. J Bacteriol. 2017;199: pubmed publisher
    ..These findings provide the first insight into the regulatory mechanisms enabling efficient outgrowth. ..
  14. Neumann M, Leimkuhler S. Heavy metal ions inhibit molybdoenzyme activity by binding to the dithiolene moiety of molybdopterin in Escherichia coli. FEBS J. 2008;275:5678-89 pubmed publisher
    ..Our study shows that the activity of molybdoenzymes, such as sulfite oxidase, is inhibited by high concentrations of heavy metals in the cell, which will help to further the understanding of metal toxicity in E. coli. ..
  15. Rentmeister A, Mayer G, Kuhn N, Famulok M. Secondary structures and functional requirements for thiM riboswitches from Desulfovibrio vulgaris, Erwinia carotovora and Rhodobacter spheroides. Biol Chem. 2008;389:127-34 pubmed publisher
    ..Our study shows that aptamer domains in riboswitches with high similarity in their secondary structures can communicate with a broad variety of non-related expression domains by similar mechanisms. ..
  16. Baciou L, Michel H. Interruption of the water chain in the reaction center from Rhodobacter sphaeroides reduces the rates of the proton uptake and of the second electron transfer to QB. Biochemistry. 1995;34:7967-72 pubmed
    ..The relative decrease of the kAB(2) rate values in the mutants is more pronounced above pH 8. Our results indicate that the mutations have specifically altered the pathway of proton transfer to QB.(ABSTRACT TRUNCATED AT 250 WORDS) ..
  17. Hendrischk A, Frühwirth S, Moldt J, Pokorny R, Metz S, Kaiser G, et al. A cryptochrome-like protein is involved in the regulation of photosynthesis genes in Rhodobacter sphaeroides. Mol Microbiol. 2009;74:990-1003 pubmed publisher
    ..sphaeroides. Thus, for the first time a role of a bacterial cryptochrome in gene regulation together with a biological function is demonstrated...
  18. Mank N, Berghoff B, Hermanns Y, Klug G. Regulation of bacterial photosynthesis genes by the small noncoding RNA PcrZ. Proc Natl Acad Sci U S A. 2012;109:16306-11 pubmed publisher
  19. Han Y, Meyer M, Keusgen M, Klug G. A haem cofactor is required for redox and light signalling by the AppA protein of Rhodobacter sphaeroides. Mol Microbiol. 2007;64:1090-104 pubmed
    ..Based on this we present a model for the transmission of light and redox signals by AppA. ..
  20. Geyer T, Lauck F, Helms V. Molecular stochastic simulations of chromatophore vesicles from Rhodobacter sphaeroides. J Biotechnol. 2007;129:212-28 pubmed
    ..Some new experiments are proposed by which the DeltapH dependent characteristic of the bc(1) complex or the proton buffering capacity of the vesicle could be determined...
  21. Happ H, Braatsch S, Broschek V, Osterloh L, Klug G. Light-dependent regulation of photosynthesis genes in Rhodobacter sphaeroides 2.4.1 is coordinately controlled by photosynthetic electron transport via the PrrBA two-component system and the photoreceptor AppA. Mol Microbiol. 2005;58:903-14 pubmed publisher
    ..Both signalling pathways involve redox-dependent steps that finally determine the effect of light on gene expression...
  22. Farchaus J, Barz W, Grünberg H, Oesterhelt D. Studies on the expression of the pufX polypeptide and its requirement for photoheterotrophic growth in Rhodobacter sphaeroides. EMBO J. 1992;11:2779-88 pubmed
  23. Li K, Pasternak C, Härtig E, Haberzettl K, Maxwell A, Klug G. Thioredoxin can influence gene expression by affecting gyrase activity. Nucleic Acids Res. 2004;32:4563-75 pubmed
    ..Furthermore, inhibition of gyrase activity strongly reduces puf and puc expression. Our results reveal a new signaling pathway by which oxygen can affect the expression of bacterial genes...
  24. Ermler U, Fritzsch G, Buchanan S, Michel H. Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 A resolution: cofactors and protein-cofactor interactions. Structure. 1994;2:925-36 pubmed
    ..The newly discovered water chain to the QB binding site suggests a pathway for the protonation of the secondary quinone QB...
  25. Papenbrock J, Grafe S, Kruse E, Hanel F, Grimm B. Mg-chelatase of tobacco: identification of a Chl D cDNA sequence encoding a third subunit, analysis of the interaction of the three subunits with the yeast two-hybrid system, and reconstitution of the enzyme activity by co-expression of recombinant C. Plant J. 1997;12:981-90 pubmed
    ..In vitro Mg2+ insertion into protoporphyrin IX was demonstrated in protein extracts of yeast strains expressing the three subunits of tobacco Mg-chelatase. The reconstitution of the recombinant enzyme activity required additional ATP. ..
  26. Kuglstatter A, Ermler U, Michel H, Baciou L, Fritzsch G. 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. 2001;40:4253-60 pubmed
    ..In the Pro L209 --> Glu reaction center, the carboxylic side chain of Glu L209 is located within the water chain, and the binding site of Q(B) remains unchanged compared to the wild-type structure. ..
  27. Klamt S, Schuster S, Gilles E. Calculability analysis in underdetermined metabolic networks illustrated by a model of the central metabolism in purple nonsulfur bacteria. Biotechnol Bioeng. 2002;77:734-51 pubmed
    ..A new software tool, the FluxAnalyzer, is introduced. It allows quantitative and structural analysis of metabolic networks in a graphical user interface. ..
  28. Bhat J, Miličić G, Thieulin Pardo G, Bracher A, Maxwell A, Ciniawsky S, et al. Mechanism of Enzyme Repair by the AAA+ Chaperone Rubisco Activase. Mol Cell. 2017;67:744-756.e6 pubmed publisher
    ..The pulling force of Rca is fine-tuned to avoid global destabilization and allow for precise enzyme repair. ..
  29. Zarzycki J, Schlichting A, Strychalsky N, M ller M, Alber B, Fuchs G. Mesaconyl-coenzyme A hydratase, a new enzyme of two central carbon metabolic pathways in bacteria. J Bacteriol. 2008;190:1366-74 pubmed publisher
    ..A similar yet distinct class of enzymes containing only one hydratase domain was found in various other bacteria, such as Streptomyces species. The role of this widely distributed new enzyme is discussed...
  30. Metz S, J ger A, Klug G. Role of a short light, oxygen, voltage (LOV) domain protein in blue light- and singlet oxygen-dependent gene regulation in Rhodobacter sphaeroides. Microbiology. 2012;158:368-79 pubmed publisher
    ..RsLOV affects not only blue light-dependent gene expression but also redox-dependent regulation...
  31. Mueller Cajar O, Stotz M, Wendler P, Hartl F, Bracher A, Hayer Hartl M. Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase. Nature. 2011;479:194-9 pubmed publisher
    ..Understanding Rubisco activation may facilitate efforts to improve CO(2) uptake and biomass production by photosynthetic organisms...
  32. Pradella S, Allgaier M, Hoch C, Päuker O, Stackebrandt E, Wagner Dobler I. Genome organization and localization of the pufLM genes of the photosynthesis reaction center in phylogenetically diverse marine Alphaproteobacteria. Appl Environ Microbiol. 2004;70:3360-9 pubmed
    ..The large number and significant size of the linear plasmids found especially in isolates from dinoflagellates might account for the metabolic versatility and presumed symbiotic association with eukaryotic hosts in these bacteria...
  33. Han Y, Braatsch S, Osterloh L, Klug G. A eukaryotic BLUF domain mediates light-dependent gene expression in the purple bacterium Rhodobacter sphaeroides 2.4.1. Proc Natl Acad Sci U S A. 2004;101:12306-11 pubmed
    ..This finding implies that the BLUF domain is fully modular and can relay signals to completely different output domains...
  34. Meister M, Saum S, Alber B, Fuchs G. L-malyl-coenzyme A/beta-methylmalyl-coenzyme A lyase is involved in acetate assimilation of the isocitrate lyase-negative bacterium Rhodobacter capsulatus. J Bacteriol. 2005;187:1415-25 pubmed
    ..We therefore propose that L-malyl-CoA/beta-methylmalyl-CoA lyase encoded by mcl1 is involved in acetate assimilation by R. capsulatus and possibly other glyoxylate cycle-negative bacteria. ..
  35. Alber B, Spanheimer R, Ebenau Jehle C, Fuchs G. Study of an alternate glyoxylate cycle for acetate assimilation by Rhodobacter sphaeroides. Mol Microbiol. 2006;61:297-309 pubmed publisher
    ..In a second part glyoxylate and propionyl-CoA are converted with another molecule of acetyl-CoA and CO(2) to l-malyl-CoA and succinyl-CoA...