Characterization of a CO-responsive Transcriptional Activator from Rhodospirillum rubrum
نویسندگان
چکیده
منابع مشابه
Redox-dependent activation of CO dehydrogenase from Rhodospirillum rubrum.
Studies of initial activities of carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum show that CODH is mostly inactive at redox potentials higher than -300 mV. Initial activities measured at a wide range of redox potentials (0--500 mV) fit a function corresponding to the Nernst equation with a midpoint potential of -316 mV. Previously, extensive EPR studies of CODH have suggested th...
متن کاملCooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein.
Biological sensing of small molecules such as NO, O2, and CO is an important area of research; however, little is know about how CO is sensed biologically. The photosynthetic bacterium Rhodospirillum rubrum responds to CO by activating transcription of two operons that encode a CO-oxidizing system. A protein, CooA, has been identified as necessary for this response. CooA is a member of a family...
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...
متن کاملThe succinic dehydrogenase from Rhodospirillum rubrum.
Succinic dehydrogenase has usually been associated with a macromolecular intracellular unit (mitochondria) whenever the enzyme has been isolated. In an ultracentrifugal analysis of the composition of extracts of various organisms, Schachman et al. (1952) found that Rhodospirillum rubrum yielded particles with a wide range of sedimentation constants. Succinic dehydrogenase has been demonstrated ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.1.120