Protein phosphorylation in the photosynthetic bacterium Rhodospirillum rubrum

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High-level production of the industrial product lycopene by the photosynthetic bacterium Rhodospirillum rubrum.

The biosynthesis of the major carotenoid spirilloxanthin by the purple nonsulfur bacterium Rhodospirillum rubrum is thought to occur via a linear pathway proceeding through phytoene and, later, lycopene as intermediates. This assumption is based solely on early chemical evidence (B. H. Davies, Biochem. J. 116:93-99, 1970). In most purple bacteria, the desaturation of phytoene, catalyzed by the ...

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Oxidative phosphorylation in extracts of Rhodospirillum rubrum.

The purple photosynthetic bacterium, Rhodospirillum rubrum, grows anaerobically only when illuminated with light of appropriate wave lengths. Extracts prepared from cells grown in this manner catalyze an anaerobic light-dependent phosphorylation of adenosine diphosphate to adenosine triphosphate (1). However, R. rubrum also can be grown heterotrophically in darkness if oxygen is provided (2). U...

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Purification and properties of dinitrogenase reductase ADP-ribosyltransferase from the photosynthetic bacterium Rhodospirillum rubrum.

The enzyme that catalyzes the ADP-ribosylation and concomitant inactivation of dinitrogenase reductase in Rhodospirillum rubrum has been purified greater than 19,000-fold to near homogeneity. We propose dinitrogenase reductase ADP-ribosyltransferase (DRAT) as the working name for the enzyme. DRAT activity is stabilized by NaCl and ADP. The enzyme is a monomer with a molecular mass of 30 kDa and...

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Amino acid sequence of cytochrome c' from the purple photosynthetic bacterium Rhodospirillum rubrum S1.

The amino acid sequence of cytochrome c' from the purple photosynthetic bacterium Rhodospirillum rubrum S1 has been determined and is consistent with homology to cytochrome c' from the nonphotosynthetic bacterium Alcaligenes sp. NCIB 11015. There is 29% identity in the chosen alignment of these two proteins. R. rubrum cytochrome c' is composed of a single peptide chain of 126 amino acid residu...

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Amino Acid Sequence of Cytochrome c’ from the Purple Photosynthetic Bacterium Rhodospirillum rubrum Sl*

The amino acid sequence of cytochrome c’ from the purple photosynthetic bacterium Rhodospirillum rubrum Sl has been determined and is consistent with homology to cytochrome c’ from the nonphotosynthetic bacterium Alcaligenes sp. NCIB 11015. There is 29% identity in the chosen alignment of these two proteins. R. rubrum cytochrome c’ is composed of a single peptide chain of 126 amino acid residue...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 1985

ISSN: 0014-5793

DOI: 10.1016/0014-5793(85)81122-4