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Wednesday, May 20, 2020 | History

2 edition of Rhodospirillum rubrum adenosine triphosphatase. found in the catalog.

Rhodospirillum rubrum adenosine triphosphatase.

Geoffrey David Webster

Rhodospirillum rubrum adenosine triphosphatase.

by Geoffrey David Webster

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  • 33 Currently reading

Published by University of Birmingham in Birmingham .
Written in English


Edition Notes

Thesis (Ph.D.)- University of Birmingham, Dept. of Biochemistry.

ID Numbers
Open LibraryOL20230833M

COUPLING FACTOR ADENOSINE TRIPHOSPHATASE-COMPLEX OF RHODOSPIRILL UM R UBR UM In Rhodospirillum rubrum was observed and its activity was inhibited by oligomycin [4]. Attempts to separate the ATPase from R. rubrum membranes were carried out by several groups. Johansson et al. [S] purified a Ca2+-. I86 BIOCHIMICA ET BIOPHYSlCA ACTA VOL. 5 (o) ON THE ROLE OF THE CAROTENOIDS IN PHOTOSYNTHESIS IN RHODOSPIRILLUM RUBRUM by J, B. THOMAS" Biophysical Research Group under the Direction o/ A. J. ]'{LUYVER, Delft, and of J. M. W. MILATZ, Utrecht (Netherlands) INTRODUCTION.

  Affinity chromatography of H+-translocating adenosine triphosphatase isolated by chloroform extraction of Rhodospirillum rubrum chromatophores. Modification of binding affinity by divalent cations and activating anions. Webster GD, Jackson JB. 1. ATPase isolated from Rhodospirillum rubrum by chloroform extraction and purified by gel filtration Cited by: The Rhodospirillaceae are a family of majority are purple nonsulfur bacteria, producing energy through photosynthesis; originally all purple nonsulfur bacteria were included here.. They are often found in anaerobic aquatic environments, such as mud and stagnant water, although they are able to survive in air.. This family also includes Magnetospirillum, which contains tiny Class: Alphaproteobacteria.

Abstract. Characteristics of inorganic pyrophosphate synthesis from inorganic orthophosphate were examined in chromatophores of Rhodospirillum application of an ADP-glucose pyrophosphorylase-trapping system has shown in an unequivocal fashion that pyrophosphate is a product of a light-dependent reaction utilizing P i as the substrate. Only very limited pyrophosphate synthesis Cited by: Webster, G. D., Jackson, F. B.: Affinity chromatography of H +-translocating adenosine triphosphatase isolated by chloroform extraction of Rhodospirillum rubrum chromatophores. Modification of binding affinity by divalent cations and activating : Norma L. Pucheu, Oscar Romero, Augusto F. García.


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Rhodospirillum rubrum adenosine triphosphatase by Geoffrey David Webster Download PDF EPUB FB2

The control of the adenosine triphosphatase of Rhodospirillum rubrum chromatophores by divalent cations and the membrane high energy state. Edwards PA, Jackson JB. The rate of ATP hydrolysis, catalysed by Rhodospirilum rubrum chromatophores is accelerated by low concentrations and inhibited by high concentrations of uncoupling agent.

by: Rhodospirillum Rubrum Adenosine Triphosphatase. Author: Webster, G. ISNI: Awarding Body: University of Birmingham Current Institution: University of Birmingham Date of Award: Availability of Full Text: Access from EThOS.

Rhodospirillum rubrum (Typical Spirillum), w.m. Microscope Slide Price: $ + $ shipping. The control of the adenosine triphosphatase of Rhodospirillum rubrum chromatophores by divalent cations and the membrane high energy state. (PMID) PMIDCited by: 1. The ATP content of intact cells of Rhodospirillum rubrum and Rhodopseudomonas spheroides was measured under different conditions using the sensitive luciferin-luciferase method.

The rate of decrease in ATP in the intact bacteria in the dark in the absence of O 2 is low; ATP formation following illumination or oxygenation is extremely rapid and the initial rates are similar with the two. 1. Chromatophores from Rhodospirillum rubrum hydrolyze ATP into ADP and P 1 either in the light or in darkness; this activity is called ATPase activity.

The ATPase activity in some, though not all, cases is inhibited by light. The light appears to be a competitive inhibitor against by: Coupling factor adenosine triphosphatase-complex of Rhodospirillum rubrum Vol number 1 FEBS LETTERS July COUPLING FACTOR ADENOSINE TRIPHOSPHATASE-COMPLEX OF RHODOSPIRILL UM R UBR UM Isolation of an oligomycin-sensitive Ca 1% Mgt+-ATPase R.

OREN and Z. GROMET-ELHANAN Biochemistry Department, Weizmann Institute of Science, Rehovot Cited by:   The nucleotide sequence was determined of a base-pair region of DNA cloned from the photosynthetic non-sulphur bacterium Rhodospirillum rubrum. It contains a cluster of five genes encoding F1-ATPase subunits.

The genes are arranged in the same order Cited by: Rhodospirillum rubrum (R. rubrum) is a Gram-negative, pink-coloured Proteobacterium, with a size of to is a facultative anaerobe, thus capable of using oxygen for aerobic respiration under aerobic conditions, or an alternative terminal electron acceptor for anaerobic respiration under anaerobic ative terminal electron acceptors for R.

rubrum include Family: Rhodospirillaceae. Due to the fact that Rhodospirillum rubrum can grow both aerobically and anaerobically, it is capable of inhabiting a wide variety of conditions.R. rubrum is found in many natural aquatic environments such as ponds, lakes, streams, and standing water (Reslewic et.

al, ).R. rubrum is also often found in mud and sewage (Brock et al, ). Studies have shown that R. rubrum. (EC ) and adenosine 5 ’ -triphosphatase (EC ) We have developed a method for obtaining a highly purified membrane-bound PPase from R. rubrum chromatophore [lo]. This pure membrane- bound PPase, incorporated into phospholipid vesicles in the presence of PPi and Mg’+, can func.

The mitochondrial adenosine triphosphatase (ATPase) of Acanthamoeba castellanii is Mg2+-requiring (optimum cation: ATP ratio of ) and has two pH optima of activity (at pH and ). The chromatophore-bound adenosine triphosphatase and inorganic pyrophosphatase of Rhodospirillum rubrum are inactivated by treatment with phospholipase A.

Parallel to the inactivation of these enzymes, the ability of the chromatophores to catalyze photophosphorylation of ADP and the ATP-P i exchange reaction is lost. The loss of the enzymatic activities involved in the energy-conversion Cited by: Cation Flux Across Biomembranes documents the proceedings of a symposium on ""Cation Flux across Biomembranes"" sponsored by the Japan Bioenergetics Group, held Septemberat the Inter-University Seminar House of Kansai in Kobe, Japan.

Preparation and characterisation of an αβ heterodimer from the ATP synthase of Rhodospirillum rubrum. Biochimica et Biophysica Acta (BBA) - Bioenergetics(1), DOI: /(93) Zippora by: Bengis-Garber C, Gromet-Elhanan Z.

Purification of the energy-transducing adenosine triphosphatase complex from Rhodospirillum rubrum. Biochemistry. Aug 7; 18 (16)– Bibb MJ, Van Etten RA, Wright CT, Walberg MW, Clayton DA.

Sequence and gene organization of mouse mitochondrial DNA. Cell. Oct; 26 (2 Pt 2)–Cited by: 1. ATPase isolated from Rhodospirillum rubrum by chloroform extraction and purified by gel filtration or affinity chromatography shows three bands (α, Cited by: Rhodospirillum rubrum is a purple non-sulfur bacteria.

It most easily is found in marine environments, which may range from ponds, to brackish ditches and even sewage.

Membrane-bound phosphate as driving force for ATP synthesis in chromatophores ofRhodospirillum rubrum Walter Beyeler, Hans U. Lutz, Reinhard Bachofen Pages OriginalPaper. Anaerobic suspensions of Rhodospirillum rubrum cells which had been grown in the dark under low oxygen tension showed only a small increase of their ATP content when illuminated for 30 s.

The same suspensions failed to start immediate growth in the light. Both high light-induced ATP levels and immediate phototrophic growth were elicited by small amounts of oxygen which were insufficient Cited by:.

Rhodospirillum rubrum, have been reported (). During the course of our investigations, Abrams, McNamara, and Johnson published results describing an adenosine triphosphatase found in cell membranes of Streptococcus fuecalis (6). EXPERIMENTAL PROCEDURE Preparation of Enzymically Active Cell FractionsB.

mega.We use cookies to make interactions with our website easy and meaningful, to better understand the use of our services, and to tailor advertising. Koenings, A. W. T., Guillory, R.

J.: Resolution of enzymes catalyzing energy-linked transhydrogenation. IV. Reconstitution of adenosine triphosphate-driven transhydrogenation in depleted chromatophores of Rhodospirillum rubrum by the transhydrogenase factor and a soluble oligomycin insensitive Mg 2+-adenosine triphosphatase.

by: 9.