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Rhodobacter capsulatus

Kirmaier C and Holten D 1988 Subpicosecond spectroscopy of charge separation in Rhodobacter capsulatus reaction centers Isr. J. Chem. 28 79-85... [Pg.1999]

The first x-ray structure of a porin was determined by the group of Georg Schulz and Wolfram Welte at Ereiburg University, Germany, who succeeded in growing crystals of a porin from Rhodobacter capsulatus that diffracted to 1.8 A resolution. Since then the x-ray structures of several other porin molecules have been determined and found to be very similar to the R. capsulatus porin despite having no significant sequence identity. [Pg.229]

Figure 12.7 Ribbon diagram of one subunit of potin from Rhodobacter capsulatus viewed from witbin tbe plane of tbe membrane. Sixteen p strands form an antiparallel p barrel tbat traverses tbe membrane. Tbe loops at tbe top of tbe picture are extracellular whereas tbe short turns at tbe bottom face the periplasm. The long loop between p strands 5 and 6 (red) constricts the channel of the barrel. Two calcium atoms are shown as orange circles. (Adapted from S.W. Cowan, Curr. Opin. Struct. Biol. 3 501-507, 1993.)... Figure 12.7 Ribbon diagram of one subunit of potin from Rhodobacter capsulatus viewed from witbin tbe plane of tbe membrane. Sixteen p strands form an antiparallel p barrel tbat traverses tbe membrane. Tbe loops at tbe top of tbe picture are extracellular whereas tbe short turns at tbe bottom face the periplasm. The long loop between p strands 5 and 6 (red) constricts the channel of the barrel. Two calcium atoms are shown as orange circles. (Adapted from S.W. Cowan, Curr. Opin. Struct. Biol. 3 501-507, 1993.)...
Early mutational studies of the Rieske protein from 6ci complexes have been performed with the intention of identifying the ligands of the Rieske cluster. These studies have shown that the four conserved cysteine residues as well as the two conserved histidine residues are essential for the insertion of the [2Fe-2S] cluster (44, 45). Small amounts of a Rieske cluster with altered properties were obtained in Rhodobacter capsulatus when the second cysteine in the cluster binding loop II (Cys 155, corresponding to Cys 160 in the bovine ISF) was replaced by serine (45). The fact that all four cysteine residues are essential in Rieske clusters from be complexes, but that only two cysteines are conserved in Rieske-type clusters, led to the suggestion that the Rieske protein may contain a disulfide bridge the disulfide bridge was finally shown to exist in the X-ray structure (9). [Pg.109]

When the fully conserved residue Thr 140, which is packed against the Pro loop, was substituted by Gly, His, or Arg in Rhodobacter capsulatus, the midpoint potential of the Rieske cluster was decreased by 50-100 mV, the cluster interacted with the quinone pool and the bci complex had 10-24% residual activity but the Rieske cluster was rapidly destroyed upon exposure to oxygen (49). In contrast, the residual activity was <5%, the cluster showed no interaction with the quinone pool, and the interaction with the inhibitor stigmatellin... [Pg.111]

Fig. 14. Plot of the g values g,g ) and of the average g value g vs rhombicity (UJ of (a) wild type (open symbol) and variant forms (closed symbols) of the Rieske protein in yeast bci complex where the residues Ser 183 and Tyr 185 forming hydrogen bonds into the cluster have been replaced by site-directed mutagenesis [Denke et al. (35) Merbitz-Zahradnik, T. Link, T. A., manuscript in preparation] and of (b) the Rieske cluster in membranes of Rhodobacter capsulatus in different redox states of the quinone pool and with inhibitors added [data from Ding et al. (79)]. The solid lines represent linear fits to the data points the dashed lines reproduce the fits to the g values of all Rieske and Rieske-type proteins shown in Fig. 13. Fig. 14. Plot of the g values g,g ) and of the average g value g vs rhombicity (UJ of (a) wild type (open symbol) and variant forms (closed symbols) of the Rieske protein in yeast bci complex where the residues Ser 183 and Tyr 185 forming hydrogen bonds into the cluster have been replaced by site-directed mutagenesis [Denke et al. (35) Merbitz-Zahradnik, T. Link, T. A., manuscript in preparation] and of (b) the Rieske cluster in membranes of Rhodobacter capsulatus in different redox states of the quinone pool and with inhibitors added [data from Ding et al. (79)]. The solid lines represent linear fits to the data points the dashed lines reproduce the fits to the g values of all Rieske and Rieske-type proteins shown in Fig. 13.
ENDOR and ESEEM studies of phthalate dioxygenase (PDO) (7, 84), benzene dioxygenase (85), 2-halobenzoate 1,2-dioxygenase (86), 2,4,5-trichlorophenoxyacetate monooxygenase (86a), spinach bef complex (8), and the bci complexes from Rhodobacter capsulatus (7, 84) and in bovine mitochondrial membranes (87) (Fig. 16) have identified two nitrogen nuclei coupled to the [2Fe-2S] cluster with isotropic N... [Pg.132]

Bartley, G.E. et al.. Carotenoid desaturases from Rhodobacter capsulatus and Neu-rospora crassa are structurally and functionally conserved and contain domains homologous to flavoprotein disulfide oxidoreductases, J. Biol. Chem. 265, 16020, 1990. [Pg.392]

Xanthine dehydrogenase that mediates the conversion of hypoxanthine into xanthine and uric acid has been studied extensively since it is readily available from cow s milk. It has also been studied (Leimkiihler et al. 2004) in the anaerobic phototroph Rhodobacter capsulatus, and the crystal structures of both enzymes have been solved. Xanthine dehydrogenase is a complex flavoprotein containing Mo, FAD, and [2Fe-2S] redox centers, and the reactions may be rationalized (Hille and Sprecher 1987) ... [Pg.130]

Leimkiihler S, AL Stockert, K Igarashi, T Nishino, R Hille (2004) The role of active site glutamate residues in catalysis of Rhodobacter capsulatus xanthine dehydrogenase. J Biol Chem 279 40437-40444. [Pg.141]

The aerobic and anaerobic degradation of acetone is initiated by carboxylation to acetoac-etate. The involvement of manganese has been examined in photoheterotrophically grown Rhodobacter capsulatus strain BIO and the presence of Mn verified from the X-band EPR spectrum (Boyd et al. 2004). [Pg.181]

Reduction of dimethyl sulfoxide and trimethylamine-fV-oxide by Rhodobacter capsulatus (Rhodopseudomonas capsulata) (King et al. 1987)... [Pg.286]

King GF, DJ Richardson, JB Jackson, SJ Ferguson (1987) Dimethyl sulfoxide and trimethylamine-A-oxide as bacterial electron acceptors use of nuclear magnetic resonance to assay and characterise the reductase system in Rhodobacter capsulatus. Arch Microbiol 149 47-51. [Pg.292]

Hagedoorn, P.-L., Hagen, W.R., Stewart, L.J., Docrat, A., Bailey, S., and Garner, C.D. 2003. Redox characteristics of the tungsten DMSO reductase of Rhodobacter capsulatus. FEBS Letters 555 606-610. [Pg.234]

S. Elsen, A. Colbeau, J. Chabert, P. M. Vignais (1996) The hupTUV operon is involved in the negative control of hydrogenase synthesis in Rhodobacter capsulatus. J. Bacteriol., 178 5174-5181... [Pg.30]

N. A. Worin, T. Lissolo, A. Colbeau, P. M. Vignais (1996) Increased hydrogen photoproduction by Rhodobacter capsulatus strains deficient in uptake hydrogenase, J. Mar. Biotechnol., 4 28-33... [Pg.54]

Rhodobacter capsulatus B10 Chemostat wih ammonium limitation, lactate, continuous argon flow (100 ml/min), light saturation 88 0.115 97 Tsygankov et al., 1998... [Pg.61]

H. Koku, I. Eroglu, U. Gunduz, M. Yucel, L. Turker (2002) Aspects of the metabolism of hydrogen production by Rhodobacter capsulatus. Int. J. Hydr. Energy., 27 1315-1329... [Pg.69]

A. A. Tsygankov, A S. Fedorov, T. V. Laurinavichene, I. N. Gogotov, K. K. Rao, D. O. Hall (1998) Actual and potential rates of hydrogen photoproduction by continuous culture of the purple non-sulfur bacterium Rhodobacter capsulatus. Appl. Microbiol. Biotechnol.,49 ... [Pg.70]

A. A. Tsygankov, T. Laurinavichene, I. Gogotov, Y. Asada, J. Miyake (1996) Switching over from light limitation to ammonium limitation of chemostat cultures of Rhodobacter capsulatus grown in different types of photobioreactors. J. Marine Biotechnol., 4 43-46... [Pg.70]

A. A. Tsygankov, T. V. Laurinavichene (1996) Influence of the degree and mode of ligth limitation on growth characteristics of the Rhodobacter capsulatus continuous culture, 51 605-612... [Pg.70]

Forward, J. A., Behrendt, M. C., Wyborn, N. R., Cross, R. and Kelly, D. J. (1997). TRAP transporters a new family of periplasmic solute transport systems encoded by the dctPQM genes of Rhodobacter capsulatus and by homologs in diverse gram-negative bacteria, J. Bacteriol., 179, 5482-5493. [Pg.329]

Fig. 7.—Chemical structure of lipid A of Rhodobacter capsulatus. Dashed lines indicate nonstoichiometric substitution. The anomeric a configuration of phosphates and the configuration (Zor ) of the double bond in A5-12 1 are assigned only tentatively (89). For substituents of the phosphates see Table I. [Pg.233]


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