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Science 22 October 1976:
Vol. 194. no. 4263, pp. 424 - 426
DOI: 10.1126/science.824729

Articles

Science, Vol 194, Issue 4263, 424-426
Copyright © 1976 by American Association for the Advancement of Science


articles

Activating factor for the iron protein of nitrogenase from Rhodospirillum rubrum

PW Ludden and RH Burris

As isolated from Rhodospirillum rubrum, the iron protein of nitrogenase has little or no activity. It can be activated by incubating it with a trypsin-sensitive, oxygen-labile component (activating factor) plus adenosine triphosphate and a divalent metal ion. After activation, the iron protein retains its nitrogenase activity when the activating factor is removed.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Effects of Specific Amino Acid Substitutions on Activities of Dinitrogenase Reductase-Activating Glycohydrolase from Rhodospirillum rubrum.
B. S. Antharavally, R. R. Poyner, Y. Zhang, G. P. Roberts, and P. W. Ludden (2001)
J. Bacteriol. 183, 5743-5746
   Abstract »    Full Text »    PDF »
Effects of Perturbations of the Nitrogenase Electron Transfer Chain on Reversible ADP-Ribosylation of Nitrogenase Fe Protein in Klebsiella pneumoniae Strains Bearing the Rhodospirillum rubrum dra Operon.
C. M. Halbleib, Y. Zhang, G. P. Roberts, and P. W. Ludden (2000)
J. Bacteriol. 182, 3681-3687
   Abstract »    Full Text »
Regulation of Dinitrogenase Reductase ADP-ribosyltransferase and Dinitrogenase Reductase-activating Glycohydrolase by a Redox-dependent Conformational Change of Nitrogenase Fe Protein.
C. M. Halbleib, Y. Zhang, and P. W. Ludden (2000)
J. Biol. Chem. 275, 3493-3500
   Abstract »    Full Text »    PDF »
Cell-Free Nitrogenase and Hydrogenase from Actinorhizal Root Nodules.
D. R. BENSON, D. J. ARP, and R. H. BURRIS (1979)
Science 205, 688-689
   Abstract »    PDF »



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