Photosynthesis in Rhodospirillum rubrum. II. Photoheterotrophic Carbon Dioxide Fixation
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چکیده
منابع مشابه
Photosynthesis in Rhodospirillum rubrum. II. Photoheterotrophic carbon dioxide fixation.
The contribution of the reductive pentose phosphate cycle to the photometabolism of carbon dioxide and to carbon metabolism in Rhodospirillum rubrum grown photoheterotrophically with l-malate as the carbon source is nil, unlike autotrophically grown R. rubrum. Glycolic acid appears to be the first stable product of CO(2) fixation in R. rubrum cultured photoheterotrophically on l-malate. The res...
متن کاملPhotosynthesis in Rhodospirillum rubrum. I. Autotrophic carbon dioxide fixation.
The incorporation and distribution of activity from (14)CO(2) was investigated under autotrophic conditions in the facultative photoautotroph, Rhodospirillum rubrum, with cells cultured on hydrogen, carbon dioxide, and ammonium sulfate. In 1 second (14)CO(2) fixation experiments essentially all of the activity was found in 3-phosphoglyceric acid: plotted against time percent incorporation into ...
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 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 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: Plant Physiology
سال: 1967
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.42.4.491