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Photosynthetic metabolism of propionate in Rhodospirillum rubrum

Archiv f�r Mikrobiologie, 1957
As in the case of oxidative metabolism, the photosynthetic metabolism of propionate in Rhodospirillum rubrum begins with a carboxylation yielding succinate. This conclusion is based on experiments in which radioactive propionate (1-C14 and 2-C14) is administered in the presence of “carrier” lactate, pyruvate, succinate, and acrylate, and on studies of ...
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Characterization of the pet operon of Rhodospirillum rubrum

Photosynthesis Research, 1992
The three genes of the pet operon, coding, respectively, for the Rieske iron-sulfur protein, cytochrome b and cytochrome c 1 components of the cytochrome bc 1 complex in the photosynthetic bacterium Rhodospirillum rubrum have been sequenced. The amino acid sequences deduced for these three peptides from the nucleotide sequences of the genes have been ...
S, Chankor   +7 more
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Location of Chlorophyll in Rhodospirillum rubrum

Journal of Bacteriology, 1965
Holt, Stanley C. (University of California, Davis), and Allen G. Marr . Location of chlorophyll in Rhodospirillum rubrum . J. Bacteriol. 89: 1402–1412.
S C, HOLT, A G, MARR
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Light-activated hydrogenase in Rhodospirillum rubrum

Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects, 1964
Abstract Reduction of 37.5 mM potassium ferricyanide by hydrogen with washed suspensions of Rhodospirillum rubrum cells in phosphate buffer requires light when calcium is added. Washed cells have little hydrogenase activity in Tris buffer, but they are activated by divalent metal-complexing anions, cadmium, zinc, and detergents. Light activation of
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Ornithine-containing lipid in Rhodospirillum rubrum

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1967
Abstract An ornithine-containing lipid that lacks phosphorus has been observed in Rhodospirillum rubrum . [ 14 C]Omithine is incorporated into lipid during growth. Formation of ornithine lipid does not seem to be related to the synthesis of bacteriochlorophyll. Arginine repressed the formation of the ornithine lipid, but at the same concentration it
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Glutathione reductase from Rhodospirillum rubrum

Archiv f�r Mikrobiologie, 1969
Glutathione reductase (NADPH1: glutathione oxidoreductase (EC 1.6.4.2) was purified 70 fold from Rhodospirillum rubrum by ammonium sulfate fractionation, gelfiltration with Sephadex and chromatography on DEAE-cellulose. The optimum pH of the reaction is 7.5–8.2 Kmvalues of 8.4×10−6 M for NADPH and 5.8×10−5 M for GSSG were determined.
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The acetate-activating enzyme of Rhodospirillum rubrum

Biochimica et Biophysica Acta, 1955
Abstract A relatively stable purified enzyme preparation has been obtained from Rhodospirillum rubrum which catalyzes the formation of acetyl coenzyme A form ATP, acetate and CoA. AMP and pyrophosphate were shown to be end products of the reaction and also inhibitors of the reaction.
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Binding site on Rhodospirillum rubrum cytochrome c2 for the Rhodospirillum rubrum cytochrome bc1 complex

Biochemistry, 1987
Cytochrome c/sub 2/ and the detergent-solubilized cytochrome bc/sub 1/ complex, both from Rhodospirillum rubrum, form a tight complex at a low ionic strength that can be isolated by gel permeation chromatography. The dissociation constant of the complex is estimated to be 10/sup -6/ M or less.
Hans Rudolf Bosshard   +2 more
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Regulation of photoreduction in Rhodospirillum rubrum by ammonia

Archiv f�r Mikrobiologie, 1971
Rhodospirillum rubrum was grown in a malate medium without bound nitrogen anaerobically under N2. 1. Resting cells of these cultures showed a gradual decrease in photoreducing activity (light-induced consumption of CO2 with H2). Small amounts of ammonium chloride immediately restored the initial activity. 2.
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Glycolate excretion by Rhodospirillum rubrum

Archives of Microbiology, 1981
Glycolate can be measured in the supernatant fraction after incubation of butyrate-grown cells of Rhodospirillum rubrum either colorimetrically by the Calkins method or enzymatically using glycolate oxidase. Under optimal conditions, half-maximal excretion occurs at 11% O2 and the maximal rate is 6.9 nmol of glycolate min-1 mg protein-1 at 30°C. The pH
Ivar Storr�, A. McFadden
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