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Rhodobacter sphaeroides

Prisner T F, van der Est A, BittI R, Lubitz W, Stehlik D and Mdbius K 1995 Time-resolved W-band (95 GHz) EPR spectroscopy of Zn-substituted reaction centers of Rhodobacter sphaeroides R-26 Chem. Phys. 194 361-70... [Pg.1621]

Vos M H, Jones M R, Breton J, Lambry J-C and Martin J-L 1996 Vibrational dephasing of long- and short-lived primary donor states in mutant reaction centers ot Rhodobacter sphaeroides Biochemistry 35 2687-92... [Pg.1998]

Wynne K, Haran G, Reid G D, Moser 0 0, Dutton P L and Hochstrasser R M 1996 Femtosecond infrared spectroscopy of low-lying excited states in reaction centers of Rhodobacter sphaeroides J. Rhys. Chem. 100 5140-8... [Pg.1999]

Joo T, Jia Y, Yu J-Y, Jonas D M and Fleming G R 1996 Dynamics in isolated bacterial lightharvesting antenna (LH2) of Rhodobacter sphaeroides at room temperature J. Phys. Chem. 100 2399-409... [Pg.2000]

Streltsov A M, Aartsma T J, Hoff A J and Shuvalov V A 1997 Osoillations within the B absorption band of Rhodobacter sphaeroides reaotion oenters upon 30 femtoseoond exoitation at 865 nm Chem. Rhys. Lett. 266 347-52... [Pg.3032]

Jonas D M, Lang M J, Nagasawa Y, Joo T and Fleming G R 1996 Pump-probe polarization anisotropy study of femtoseoond energy transfer within the photosynthetio reaotion-oenter of Rhodobacter sphaeroides R26 J. Rhys. [Pg.3032]

Figure 12.23 Hydropathy plots for the polypeptide chains L and M of the reaction center of Rhodobacter sphaeroides. A window of 19 amino acids was used with the hydrophohicity scales of Kyte and Doolittle. The hydropathy index is plotted against the tenth amino acid of the window. The positions of the transmembrane helices as found by subsequent x-ray analysis by the group of G. Feher, La Jolla, California, ate indicated by the green regions. Figure 12.23 Hydropathy plots for the polypeptide chains L and M of the reaction center of Rhodobacter sphaeroides. A window of 19 amino acids was used with the hydrophohicity scales of Kyte and Doolittle. The hydropathy index is plotted against the tenth amino acid of the window. The positions of the transmembrane helices as found by subsequent x-ray analysis by the group of G. Feher, La Jolla, California, ate indicated by the green regions.
Table 12.2 Amino acid sequences of the transmembrane helices of the photosynthetic reaction center in Rhodobacter sphaeroides... Table 12.2 Amino acid sequences of the transmembrane helices of the photosynthetic reaction center in Rhodobacter sphaeroides...
Allen, J.R, et al. Structure of the reaction center from Rhodobacter sphaeroides R-26 the cofactors. Proc. Natl. Acad. Sd. USA 84 5730-5734, 1987. [Pg.249]

Figure 5.14 Electrospray spectrum of holocytochrome c". Reprinted from Biochim. Bio-phys. Acta, 1412, Klarskov, K., Leys, D., Backers, K., Costa, H. S., Santos, H., Guisez, Y. and Van Beeumen, 1. 1., Cytochrome c" from the obligate methylotroph Methy-lophilus methylotrophus, an unexpected homolog of sphaeroides heme protein from the phototroph Rhodobacter sphaeroides", 47-55, Copyright (1999), with permission from Elsevier Science. Figure 5.14 Electrospray spectrum of holocytochrome c". Reprinted from Biochim. Bio-phys. Acta, 1412, Klarskov, K., Leys, D., Backers, K., Costa, H. S., Santos, H., Guisez, Y. and Van Beeumen, 1. 1., Cytochrome c" from the obligate methylotroph Methy-lophilus methylotrophus, an unexpected homolog of sphaeroides heme protein from the phototroph Rhodobacter sphaeroides", 47-55, Copyright (1999), with permission from Elsevier Science.
The Rieske protein II (SoxF) from Sulfolobus acidocaldarius, which is part, not of a bci or b f complex, but of the SoxM oxidase complex 18), could be expressed in E. coli, both in a full-length form containing the membrane anchor and in truncated water-soluble forms 111). In contrast to the results reported for the Rieske protein from Rhodobacter sphaeroides, the Rieske cluster was more efficiently inserted into the truncated soluble forms of the protein. Incorporation of the cluster was increased threefold when the E. coli cells were subject to a heat shock (42°C for 30 min) before induction of the expression of the Rieske protein, indicating that chaperonins facilitate the correct folding of the soluble form of SoxF. The iron content of the purified soluble SoxF variant was calculated as 1.5 mol Fe/mol protein the cluster showed g values very close to those observed in the SoxM complex and a redox potential of E° = +375 mV 111). [Pg.146]

Photosynthetic reaction centers from Rhodobacter sphaeroides and bacteri-orhodopsin (BR) from purple membrane (PM) have been used for their unique optoelectronic properties and for their capability of providing light-induced proton and electron pumping. Once assembled they display extremely high thermal and temporal stability... [Pg.147]

Novak RT, RF Gritzer, ER Leadbetter, W Godchaux (2004) Phototrophic utilization of taurine by the purple nonsulfur bacteria Rhodopseudomonas palustris and Rhodobacter sphaeroides. Microbiology (UK) 150 1881-1891. [Pg.86]

Van Fleet-Stalder V, TG Chasteen, IJ Pickering, GN George, RC Prince (2000) Pate of selenate and selenite metabolized by Rhodobacter sphaeroides. Appl Environ Microbiol 66 4849-4853. [Pg.180]

Pullerits, T., S. Hess, J. L. Herek, and V. Sundstrom. 1997. Temperature dependence of excitation transfer in LH2 of Rhodobacter sphaeroides. J. Phys. Chem. B 101 10560-10567. [Pg.156]

Burghaus, O., M. Plato et al. (1991). 3mm EPR investigation of the primary donor cation radical in single crystals of Rhodobacter sphaeroides R-26 reaction centers. Chem. Phys. Lett. 185 381-386. [Pg.185]

Ishikita, H. Morra, G. Knapp, E.W., Redox potential of quinones in photosynthetic reaction centers from Rhodobacter sphaeroides dependence on protonation of Glu-L212 and Asp-L213, Biochemistry 2003, 42, 3882-3892... [Pg.461]

Ammonium Alcaligenes latus Pseudomonas oleovorans Pseudomonas cepacia Ralstonia eutrophus Rhodobacter sphaeroides Speudomonas sp. K. Methylocystus oarvus Thiosphaera pantotropha Rhizobium ORS 571... [Pg.56]

Potassium sulfate Bacillus thuringiensis Pseudomonas sp. K. Pseudomonas oleovorans Rho do spirillum rubrum Rhodobacter sphaeroids... [Pg.56]

Rhodospirillum rubrum Ha - Rhodospirillum rubrum ATCC 25903 —Acinetobacter sp. RA3849 —Aeromonas caviae FA440 —Rhodobacter sphaeroides... [Pg.90]

Yan B, Zhou J, Wang J, Du C, Hou H, Song Z, Bao Y (2004) Expression and characteristics of the gene encoding azoreductase from Rhodobacter sphaeroides AS 1.1737. FEMS Microbiol Lett 236 129-136... [Pg.207]

Brederode ME, Jones MR, Van Grondelle R (1997) Primary electron transfer kinetics in membrane-bound Rhodobacter sphaeroides reaction centers a global and target analysis. [Pg.111]

PHOTO-BIOLOGICAL HYDROGEN PRODUCTION BY THE UPTAKEHYDROGENASE AND PHB SYNTHASE DEFICIENT MUTANT OF RHODOBACTER SPHAEROIDES... [Pg.45]

A purple non-sulfur bacterium, Rhodobacter sphaeroides KD131 was isolated from nature and its mutants, Hup and /or Phb were derived by internal deletion of Hup SL and Phb C. [Pg.53]

M. Khatipov, J. Miyake, M. Miyake, Y. Asada (1998) Polyhydroxybutyrate accumulation and hydrogen evolution by Rhodobacter sphaeroides as a function of nitrogen availability, BioHydrogen, edited by Zaborsky et al. [Pg.54]

I.H. Lee, J.Y. Park, D.H. Kho, M.S. Kim and J.K. Lee (2002) Reductive effect of H2 uptake and poly-P-hydroxybutyrate formate on nitrogenase-mediated H2 accumulation of Rhodobacter sphaeroides according to light intensity. Appl. Microbiol. Biotechnol. [Pg.54]

I. Eroglu, K. Aslan, U. Gunduz, M. Yucel, and L.Turker (1998) Continuous hydrogen production by Rhodobacter sphaeroides O.U.OOl. BioHydrogen, edited by Zaborsky et al. [Pg.55]


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Initial Charge Separation in the Reaction Center of Rhodobacter sphaeroides

Kinetics of Electron Transfer in RC Protein from Rhodobacter sphaeroides

Photosynthetic Reaction Center of Rhodobacter sphaeroides

Photosynthetic bacteria Rhodobacter sphaeroides

Prokaryotic phototaxis Rhodobacter sphaeroides

Rhodobacter sphaeroides B850 complex

Rhodobacter sphaeroides absorption spectra

Rhodobacter sphaeroides bacteria reaction centers

Rhodobacter sphaeroides center

Rhodobacter sphaeroides denitrificans

Rhodobacter sphaeroides electron transfer from

Rhodobacter sphaeroides electron transfer rate

Rhodobacter sphaeroides growth

Rhodobacter sphaeroides methods

Rhodobacter sphaeroides mutant

Rhodobacter sphaeroides photosynthetic reaction center

Rhodobacter sphaeroides photosystems

Rhodobacter sphaeroides resonance Raman spectroscopy

Rhodobacter sphaeroides strain

Rhodobacter sphaeroides transition

Rhodobacter sphaeroides wild type strain

Rhodobacter sphaeroides with spheroidene

Rhodobacter sphaeroides, lipid

Rhodobacter sphaeroides, reaction centers

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