scholarly journals Comparison studies of dinitrogenase reductase ADP-ribosyl transferase/dinitrogenase reductase activating glycohydrolase regulatory systems in Rhodospirillum rubrum and Azospirillum brasilense.

1995 ◽  
Vol 177 (9) ◽  
pp. 2354-2359 ◽  
Author(s):  
Y Zhang ◽  
R H Burris ◽  
P W Ludden ◽  
G P Roberts
Keyword(s):  
Azospirillum Brasilense ◽  
Rhodospirillum Rubrum ◽  
Regulatory Systems ◽  
Dinitrogenase Reductase

scholarly journals Borate inhibits activation of inactive dinitrogenase reductase from Rhodospirillum rubrum

1981 ◽  
Vol 197 (2) ◽  
pp. 503-505 ◽  
Author(s):  
Paul W. Ludden
Keyword(s):  
Rhodospirillum Rubrum ◽  
Ph Dependence ◽  
Active Form ◽  
Aminophenylboronic Acid ◽  
Dinitrogenase Reductase ◽  
Hydroxy Groups

Borate and aminophenylboronic acid were tested as inhibitors of activation of inactive dinitrogenase reductase from Rhodospirillum rubrum. Inhibition was specific for activation because activity of the active form of the enzyme was not inhibited. Inhibition showed the pH-dependence expected if borate inhibits by binding to cis-hydroxy groups of the modifying group found on the inactive enzyme.

scholarly journals Correlation of Activity Regulation and Substrate Recognition of the ADP-Ribosyltransferase That Regulates Nitrogenase Activity in Rhodospirillum rubrum

1999 ◽  
Vol 181 (5) ◽  
pp. 1698-1702 ◽  
Author(s):  
Kitai Kim ◽  
Yaoping Zhang ◽  
Gary P. Roberts
Keyword(s):  
Rhodospirillum Rubrum ◽  
Nitrogenase Activity ◽  
Substrate Recognition ◽  
Posttranslational Regulation ◽  
Activity Regulation ◽  
Adp Ribosylation ◽  
Dinitrogenase Reductase ◽  
Adp Ribosyltransferase

ABSTRACT In Rhodospirillum rubrum, nitrogenase activity is regulated posttranslationally through the ADP-ribosylation of dinitrogenase reductase by dinitrogenase reductase ADP-ribosyltransferase (DRAT). Several DRAT variants that are altered both in the posttranslational regulation of DRAT activity and in the ability to recognize variants of dinitrogenase reductase have been found. This correlation suggests that these two properties are biochemically connected.

scholarly journals Purification and characterization of an oxygen-stable form of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum

1994 ◽  
Vol 302 (3) ◽  
pp. 801-806 ◽  
Author(s):  
G M Nielsen ◽  
Y Bao ◽  
G P Roberts ◽  
P W Ludden
Keyword(s):  
Fluorescence Spectra ◽  
Rhodospirillum Rubrum ◽  
Sodium Dithionite ◽  
Stable Form ◽  
Purification And Characterization ◽  
Dinitrogenase Reductase ◽  
Bivalent Metals ◽  
Overexpressing Strain ◽  
Ribose Moiety

Dinitrogenase reductase-activating glycohydrolase (DRAG) is responsible for removing the ADP-ribose moiety from post-translationally inactivated nitrogenase of Rhodospirillum rubrum. Using DRAG purified from an overexpressing strain (UR276), further properties of this enzyme were studied, including its u.v.-visible and fluorescence spectra and its stability in air. DRAG appears to require no covalently bound inorganic cofactors for its activity or regulation. Previously, purified DRAG was found to be rapidly inactivated in air. The air-catalysed lability originated with the presence of sodium dithionite and Mn2+ throughout the purification of the enzyme. This lability can be mimicked using H2O2, which is known to oxidatively inactivate proteins containing bivalent metals. Implications for the regulation of nitrogenase are discussed with respect to the lack of sensitivity to air of the regulatory enzyme, DRAG.

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