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Rhodospirillum rubrum properties

Ke B, Green M, Vernon LP, and Garcia AF. 1968. Some optical properties of a carotenoid complex derived from Rhodospirillum Rubrum. Biochimica et Biophysica Acta 162(3) 467 469. [Pg.56]

Furlong, C. E., and Preiss, J. 1969. Biosynthesis of bacterial glycogen synthesis. VII. Purification and properties of adenosine diphosphoglucose pyrophosphorylase of Rhodospirillum rubrum. J. Biol. Chem. 244,2539-2548. [Pg.177]

There are two exceptions from this generalization, one of which is the transhydrogenase factor isolated from Rhodospirillum rubrum chroma-tophores 109-112). This factor is obligatory for both energy-linked and non-energy-linked transhydrogenation its properties and function have already been reviewed (see Section III,D). Butlin 167 see also 73) re-... [Pg.78]

The ratio of the specificity in the carboxylase reaction to that of the oxygenase reaction is called "relative specificity (Sr)" [7]. This is a constant determined by the enzymatic properties of RuBisCO. RuBisCO from a photosynthetic bacterium, Rhodospirillum rubrum, has the Sr value of 10 the oxygenase reaction proceeds two-times faster than the carboxylase reaction in the ordinary atmosphere. The upper most in the Sr value has been thought to be possessed by RuBisCO from higher plants. The value reaches 90 to 95 [8] the carboxylase reaction is three to four times faster than the oxygenase reaction. The Sr value is a determinant of the CO2 compensation point, where CO2 fixation by RuBisCO and CO2 release from photorespiration are balanced and no net CO2 fixation is observed. [Pg.118]

Fig. 4. Difference absorption spectrum of photoreduced bacleriopheophytin (B Fig. 4. Difference absorption spectrum of photoreduced bacleriopheophytin (B<D) [AA(BO -Bd))] obtained by photochemicai accumulation. See text for experimental details. Figure source (A) Shuvalov, Klimov, Krakhmaleva, Moskalenko and Krasnovsky (1976) Photoconversion of bacteriopheophytin in reaction centers of Rhodospirillum rubrum and Chromatium minutissimum. DokI Akad Nauk SSSR 227 986 (B) Tiede, Prince and Dutton (1976) EPR and optical spectroscopic properties of the electron carrier intermediate between the reaction center bacteriochlorophylls and the primary acceptor in Chromatium vinosum. Biochim Biophys Acta 449 452 (C) van Grondelle, Romijn and Holmes (1976) Photoreduction of the long-wavelength bacteriopheophytin in reaction centers and chromatophores of the photosynthetic bacterium Chromatium vinosum. FEBS Lett 72 188.
Wiemken V and Bachofen R (1984) Probing the smallest functional unit of the reaction center of Rhodospirillum rubrum G-9 with proteinoses. FEBS Lett 166 155-159 Williams JC, Alden RG, Murchison HA, Peloquin JM, Woodbury NW and Allen IP (1992) Effects of mutations near the bacteriochlorophylls in reaction centers from Rhodobacter sphaeroides. Biochemistry 31 11029-11037 Yeates TO, Komiya H, Chirino A, Rees DC, Allen IP and Feher G (1988) Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1 Protein-cofactor bacterio-chlorophyll bacteriopheophytin and carotenoid interactions. Proc Natl Acad Sci USA 85 7993-7997 Zinth W, Knapp EW, Fischer SF, Kaiser W, Deisenhofer J and Michel H (1985) Correlation of structural and spectroscopic properties of a photo synthetic reaction center. Chem Phys Lett 119 1 ... [Pg.122]

Heterologous reconstitution experiments show some structural restraints Spheroidene from Rb. sphaeroides can be reconstituted into a complex with LHl polypeptides from Rhodospirillum rubrum, restoring spectral properties of native Rs. rubrum LHl and carotenoid-BChl energy transfer whereas spirilloxanthin is unable to incorporate into a reconstituted complex with LHl apoproteins from Rb. sphaeroides (Davis et al., 1995). [Pg.126]

Koyama Y, Takatsuka I, Kanaji M, Tomimoto K, Kito M, Shimamura T, Yamashita J, Saiki K and Tsukida K (1990) Configurations of carotenoids in the reaction center and the light-harvesting complex of Rhodospirillum rubrum. Natural selection of carotenoid configurations by pigment protein complexes. Photochem Photobiol 51 119-128 Koyama Y, Mukai Y and Kuki M (1992) Excited-state properties... [Pg.187]

Figure 5 Radiative properties of Chlamydomonas reinhardtii (ieft) and Rhodospirillum rubrum (right) obtained with the volume equivalent sphere approximation and a Lorentz-Mie code (gray color) and with a more accurate description of the shape and Schiff s approximation (black color) a prolate spheroid with elongation 1.2 (aspect ratio 0.837) for C. reinhardtii and a cylinder with elongation 3.8 (aspect ratio 0.263) for Rs. rubrum. These results were obtained by implementing the methodological chain presented in Section 2.1 for a log-normal size distribution pf, (reg =... Figure 5 Radiative properties of Chlamydomonas reinhardtii (ieft) and Rhodospirillum rubrum (right) obtained with the volume equivalent sphere approximation and a Lorentz-Mie code (gray color) and with a more accurate description of the shape and Schiff s approximation (black color) a prolate spheroid with elongation 1.2 (aspect ratio 0.837) for C. reinhardtii and a cylinder with elongation 3.8 (aspect ratio 0.263) for Rs. rubrum. These results were obtained by implementing the methodological chain presented in Section 2.1 for a log-normal size distribution pf, (reg =...
Since sc/-PHA are stiff and brittle, whereas mc/-PHA are more elastomeric and flexible, incorporation of both scl- and mcl-monomers results in a scl-mcl-copolymer which possesses the properties in between the two states. The resulting polymer has superior properties compared with scl- or wc/-PHA. According to Chen [13], scl-mcl-PHA are ideal to advance the ongoing development in various applications since they exhibit flexible mechanical properties. An attempt to produce this combination of copolymers was started in 1988 by Brandi and co-workers [14] who studied the ability of Rhodospirillum rubrum, a phototrophic bacterium, to produce various kinds of PHA. Among all the sc/-mc/-PHA produced, poly(3HB-co-3HHx) is one of the most successful polymers in this category and has been produced on an industrial scale [13]. [Pg.4]

Alternatively, it is possible to abolish cooperation by removing the catalytic subunit from its environment in the enzyme complex - providing that this can be accomplished while maintaining the subunit in an active conformation. This approach has been successful in the case of the p subunit fix)m the F, of Rhodospirillum rubrum [4]. We show here that the P subunit of chloroplast Fj can also be isolated pure in a form capable of ATP hydrolysis. The hydrolysis rate observed is of the same order as other estimates of unisite ATP hydrolysis. Properties of this isolated subunit are described. [Pg.1939]

The genes for the catalytic part of the F F -ATPase from two different phototrophic bacteria have been sequenced Rhodospirillum rubrum (1) and Rhodopseudomonas blastica (2). The sequence of the genes for the F of R. rubrum is also known (3). The atp1-operon of the latter bacteria encodes the five subunits found in the preparations of the enzyme (Walker, J. E., Falk, G., and Strid, A., unpublished results) as judged by N-terminaT analysis. The atp-operon of Rps. blastica also contains a sixth gene, termed X. The F--protein has not previously been prepared from Rps. blas-tica. Some characteristic properties of a pure preparation of the enzyme is compared to the properties of the R. rubrum F. ... [Pg.2079]

F. Parak, E. N. Frolov, A. A. Kononenko, R. L. Mssbauer, V. I. Goldanskii, A. B. Rubin, Evidence for a correlation between the photoinduced electron transfer and dynamic properties of the chromatophore membranes from Rhodospirillum rubrum, FEBS Lett. 117 (1980) 368-372. [Pg.288]

The paper by Hunyh et al. (1978) on the Mossbauer effect of low-spin Fe " in cytochrome c from Rhodospirillum rubrum highlights the value of analyses that search out fundamental properties of the system. While measurements of the sign of the product QxQyQz can be made using ESR with circularly polarized radiation (see Section 2.2.3), the measurements and analysis by Hunyh et al (1978) provides a valuable alternative. They noted that in Mossbauer spectroscopy under weak magnetic field conditions. [Pg.107]

Philosoph S, Binder A and Gromet-Elhanan Z (1977) Coupling factor ATPase complex of Rhodospirillum rubrum. Purification and properties of a recon-stitutively active single subunit, J. Biol. Chem. 252, 8747-8752. [Pg.598]


See other pages where Rhodospirillum rubrum properties is mentioned: [Pg.539]    [Pg.67]    [Pg.236]    [Pg.254]    [Pg.77]    [Pg.669]    [Pg.8]    [Pg.18]    [Pg.170]    [Pg.1764]    [Pg.77]    [Pg.236]   
See also in sourсe #XX -- [ Pg.500 , Pg.505 ]




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