Importance of Rhodospirillum rubrum H + -Pyrophosphatase under Low-Energy Conditions
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چکیده
منابع مشابه
The H(+)-pyrophosphatase of Rhodospirillum rubrum is predominantly located in polyphosphate-rich acidocalcisomes.
Acidocalcisomes are acidic, calcium storage compartments with a H(+) pump located in their membrane that have been described in several unicellular eukaryotes, including trypanosomatid and apicomplexan parasites, algae, and slime molds, and have also been found in the bacterium Agrobacterium tumefaciens. In this work, we report that the H(+)-pyrophosphatase (H(+)-PPase) of Rhodospirillum rubrum...
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Glutamate synthase, a key enzyme in ammonia assimilation, has been purified from the photosynthetic bacterium Rhodospirillum rubrum. The purification procedure involves ion-exchange chromatography, affinity chromatography and gel filtration. The recovery in the procedure is high (62%) and the specific activity is 21 mumol of NADPH oxidized/min per mg. The enzyme is specific for its substrates, ...
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Ribulose 1,5-diphosphate carboxylase has been isolated from autotrophically cultured Rhoclospirillum rubrum. The molecular weight is 120,000. The K, for ribulose 1,5diphosphate is 83 mM, and for CO2 is 59 mM. The enzyme is inhibited by three important metabolites: citrate, an intermediate of the tricarboxylic acid cycle; inorganic phosphate; and 3-phosphoglyceric acid, the product of the reacti...
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In the previous paper of this series (l), some characteristics of the photoreducing system of Rhodospirillum rubrum chromatophores were presented. In one of the experiments described, it appeared that methylene blue was being oxidized in the illuminated reaction mixture. Since such a photooxidation would be an expression of the photooxidizing system of the chromatophore, this reaction was inves...
متن کاملRegulation of nitrogen fixation in Rhodospirillum rubrum grown under dark, fermentative conditions.
Rhodospirillum rubrum was shown to grow fermentatively on fructose with N2 as a nitrogen source. The nitrogenase activity of these cells was regulated by the NH4+ switch-off/switch-on mechanism in a manner identical to that for photosynthetically grown cells. In vitro, the inactive nitrogenase Fe protein from fermenting cells was reactivated by an endogenous membrane-bound, Mn2+-dependent activ...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 2004
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.186.19.6651-6655.2004