Search results for "Rhodospirillum"

Isolation and partial characterization of a cytochrome-o complex from chromatophores of the photosynthetic bacterium Rhodospirillum rubrum FR1.

1989

A cytochrome-o complex was isolated from chromatophores of photoheterotrophically grown Rhodospirillum rubrum FR1. The enzyme was extracted with the non-denaturating detergent taurodeoxycholate and subsequently purified by sucrose-density-gradient centrifugation and gel-permeation HPLC. The complex contains two types of cytochromes, one of them cytochrome o, and two copper atoms. It catalyzes the reduction of molecular oxygen, when N,N,N',N'-tetramethyl-p-phenylenediamine or ubiquinol 10 are offered as electron donors. The oxidase activity is inhibited by cyanide, carbon monoxide and 2-heptyl-2-hydroxyquinoline N-oxide. The molecular mass of the protein is 136 +/- 15 kDa. The subunit analys…

Conversion of the Ca2+-ATPase from Rhodospirillum rubrum into a Mg2+-dependent enzyme by 1,N6-etheno ATP

1980

Nucleoside triphosphate hydrolysis of R.rubrum ATPase complexes can be changed from Ca2+-dependence to Mg2+-dependence by replacing ATP with 1,N6-etheno ATP. Four ATPase complexes which have been prepared by different procedures hydrolyze ATP and 1,N6-etheno ATP at different rates in dependence on the added metal ions. These differences allow an easy distinction of the various enzyme forms.

Incorporation of ATP synthetase into long-term stable liposomes of a polymerizable synthetic sulfolipid

1981

Purification, subunit structure, and kinetics of the chloroform-released F1ATPase complex from Rhodospirillum rubrum and its comparison with F1ATPase…

1979

Abstract A stable and homogeneous adenosine-5ʹ-triphosphatase (ATPase, EC 3.6.1.3) has been solubilized from Rhodospirillum rubrum (R . rubrum) chromatophores by chloroform extraction. Purification of the Ca2+-dependent ATPase activity was 200-fold. Ca2+ can be replaced by Mg2+, Cd2+, and Mn2+ .The Km for Ca-ATP (0.17 mᴍ) is increased about 5-fold during solubilization of the enzyme, whereas the Km values for Mg-ATP (0.029 mᴍ) and Cd-ATP (0.014 mᴍ) are not affected. The chloroform-released ATPase has a molecular weight of 400,000 ± 30,000 and consists of the following subunits (molecular weights in parenthesis): α (58,000), β (53,500), γ (39,000), δ (18,500), and ε (14,000). The amino acid …

Reconstitution and Pigment Exchange

2007

Properties of the F0F1 ATPase Complex from Rhodospirillum rubrum Chromatophores, Solubilized by Triton X-100

1979

1. A cold-stable oligomycin-sensitive F0F1 ATPase complex from chromatophores of Rhodospirillum rubrum FR 1 was solubilized by Triton X-100 and purified by gel filtration. 2. The F0F1 complex is resolved by sodium dodecyl sulfate electrophoresis into 14 polypeptides with approximate molecular weights in the range of 58000--6800; five of these polypeptides are derived from the F1 moiety of the complex which carries the catalytic centers of the enzyme. 3. The purified F0F1 complex is homogeneous according to analytical ultracentrifugation and isoelectric focusing. 4. The molecular weight as determined by gel filtration is about 480 000 +/- 30 000. S020,w is 1.45 +/- 0.1 S and the pI is 5.4. 5…

Coreconstitution of bacterial ATP synthase with monomeric bacteriorhodopsin into liposomes. A comparison between the efficiency of monomeric bacterio…

1987

The conditions for coreconstitution of a bacterial ATP synthase and bacteriorhodopsin into lecithin liposomes and for light driven ATP synthesis have been optimized. A rate of maximally 280 nmol ATP min-1 mg ATP synthase-1 was achieved with monomerized bacteriorhodopsin compared with a rate of up to 45 nmol ATP min-1 mg-1 found for proteoliposomes containing bacteriorhodopsin in the form of purple membrane patches. The different rates are explained by the finding that monomeric bacteriorhodopsin is more homogeneously distributed among the liposomes than the purple membrane patches. The final activities depended on both the purification method for the two proteins and the coreconstitution pr…

Solubilization of an oligomycin-sensitive ATPase complex fromRhodospirillum rubrumchromatophores and its inhibition by various antibiotics

1978

New waves underneath the purple strain.

2016

Summary Successful merging of chemical and biotechnological operations is essential to achieve cost‐efficient industrialization of bio‐based processes. The demonstration of the use of syngas, derived from microwave assisted pyrolysis of municipal solid waste, for the improved growth and poly‐3‐hydroxybutyrate production in Rhodospirillium rubrum, stands out as an example of the synergistic contribution of chemical engineering and applied microbiology to sustainable biomaterial manufacturing, paving the way to similar applications for other syngas derived bioproducts.

Energy-Linked Reactions Catalyzed by the Purified ATPase Complex (F0F1) from Rhodospirillum rubrum Chromatophores

1980

1. The isolation of the F0F1-ATPase complex from Rhodospirillum rubrum chromatophores by the use of taurodeoxycholate is described. 2. The enzyme preparation contains about 12 polypeptides; five are subunits of the F1 moiety. 3. The ATPase activity of the purified enzyme is dependent on the addition of phospholipids. 4. Km-vales for Mg2+-ATP and Ca2+-ATP are similar to the values obtained for the membrane-bound enzyme. 5. The F0F1-ATPase complex is more than 70% inhibited by oligomycin and N,N′-dicyclohexyl-carbodiimide. 6. The F0F1-ATPase complex was integrated into liposomes. The reconstituted proteoliposomes catalyzed energy transduction as shown by ATP-dependent quenching of acridine dy…