Reconstitution of highly purified proton-translocating pyrophosphatase from Rhodospirillum rubrum
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چکیده
منابع مشابه
Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum.
Transhydrogenase is a proton pump found in the membranes of bacteria and animal mitochondria. The solution structure of the expressed, 21.5 kDa, NADP(H)-binding component (dIII) of transhydrogenase from Rhodospirillum rubrum has been solved by NMR methods. This is the first description of the structure of dIII from a bacterial source. The protein adopts a Rossmann fold: an open, twisted, parall...
متن کاملRegulatory properties of an inorganic pyrophosphatase from the photosynthic bacterium Rhodospirillum rubrum.
In Rhodospirillum rubrum, inorganic pyrophosphatase activity is observed in both the cytoplasmic and membrane fractions. The soluble enzyme accounts for about 80% of the total activity in crude extracts, and is the subject of this report. Zn(2+) is required for both activity and stability of the enzyme, which has a molecular weight of approximately 90,000 (gel-filtration determinations). The su...
متن کاملPhotosynthesis in Rhodospirillum rubrum
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...
متن کاملThe 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...
متن کاملCarbon monoxide dehydrogenase from Rhodospirillum rubrum.
The carbon monoxide dehydrogenase from the photosynthetic bacterium Rhodospirillum rubrum was purified over 600-fold by DEAE-cellulose chromatography, heat treatment, hydroxylapatite chromatography, and preparative scale gel electrophoresis. In vitro, this enzyme catalyzed a two-electron oxidation of CO to form CO2 as the product. The reaction was dependent on the addition of an electron accept...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1982
ISSN: 0014-5793
DOI: 10.1016/0014-5793(82)80730-8