Ferredoxin Excreted from Photosynthetic Bacterium, Rhodospirillum rubrum: Purification and Properties1
نویسندگان
چکیده
منابع مشابه
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...
متن کاملPurification and properties of the activating enzyme for iron protein of nitrogenase from the photosynthetic bacterium Rhodospirillum rubrum.
The oxygen-labile, activating enzyme for iron protein from the photosynthetic bacterium, Rhodospirillum rubrum, was purified 11,800-fold using a combination of chromatophore washing, DE52-cellulose chromatography, hydroxylapatite chromatography, reactive red-120 cross-linked agarose chromatography, reactive red-120 cross-linked agarose chromatography, and Sephadex G-75 gel filtration. Activatin...
متن کاملPrimary structure of a high potential, four-iron-sulfur ferredoxin from the photosynthetic bacterium Rhodospirillum tenue.
The amino acid sequence of a high oxidation-reduction potential iron-sulfur protein (HiPIP) isolated from the purple photosynthetic bacterium Rhodospirillum tenue has been determined. This is the smallest of the HiPIP's, containing 63 residues, with only 3 residues apparently conserved in addition to the 4 cluster-binding cysteines. A minimum of four internal genetic gaps is postulated to align...
متن کاملAmino 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...
متن کاملAmino 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...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: The Journal of Biochemistry
سال: 1981
ISSN: 1756-2651,0021-924X
DOI: 10.1093/oxfordjournals.jbchem.a133378