Borate inhibits activation of inactive dinitrogenase reductase from Rhodospirillum rubrum
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چکیده
منابع مشابه
Removal of an adenine-like molecule during activation of dinitrogenase reductase from Rhodospirillum rubrum.
During the activation of the inactive dinitrogenase reductase from Rhodospirillum rubrum, an adenine-like molecules is lost and phosphate is found on both active and inactive forms of the protein. ATP and divalent metals are required for activation of the reduced protein, but ATP is not required for activation of phenazine methosulfate-oxidized dinitrogenase reductase. Snake venom diesterase an...
متن کاملEffects of specific amino acid substitutions on activities of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum.
Site-directed mutagenesis of the draG gene was used to generate altered forms of dinitrogenase reductase-activating glycohydrolase (DRAG) with D123A, H142L, H158N, D243G, and E279R substitutions. The amino acid residues H142 and E279 are not required either for the coordination to the metal center or for catalysis since the variants H142L and E279R retained both catalytic and electron paramagne...
متن کاملDinitrogenase reductase-activating glycohydrolase can be released from chromatophores of Rhodospirillum rubrum by treatment with MgGDP.
Dinitrogenase reductase-activating glycohydrolase (DRAG), involved in the regulation of nitrogenase activity in Rhodospirillum rubrum, is associated with chromatophore membranes in cell extracts. We show that DRAG can be specifically released by treatment with MgGDP; other nucleotides studied had no effect. The DRAG activity released corresponds to the release of DRAG protein.
متن کاملPurification 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 کاملEffect of P(II) and its homolog GlnK on reversible ADP-ribosylation of dinitrogenase reductase by heterologous expression of the Rhodospirillum rubrum dinitrogenase reductase ADP-ribosyl transferase-dinitrogenase reductase-activating glycohydrolase regulatory system in Klebsiella pneumoniae.
Reversible ADP-ribosylation of dinitrogenase reductase, catalyzed by the dinitrogenase reductase ADP-ribosyl transferase-dinitrogenase reductase-activating glycohydrolase (DRAT-DRAG) regulatory system, has been characterized in Rhodospirillum rubrum and other nitrogen-fixing bacteria. To investigate the mechanisms for the regulation of DRAT and DRAG activities, we studied the heterologous expre...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1981
ISSN: 0264-6021
DOI: 10.1042/bj1970503