Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1988 Apr 15;251(2):609–612. doi: 10.1042/bj2510609

ADP-ribosylation of dinitrogenase reductase from Clostridium pasteurianum prevents its inhibition of nitrogenase from Azotobacter vinelandii.

S A Murrell 1, R G Lowery 1, P W Ludden 1
PMCID: PMC1149044  PMID: 3135803

Abstract

The effect of ADP-ribosylation of dinitrogenase reductase on its binding to dinitrogenase was investigated. Dinitrogenase reductase from Clostridium pasteurianum (Cp2) was a substrate for the ADP-ribosyltransferase and the dinitrogenase-reductase-activating glycohydrolase from Rhodospirillum rubrum. ADP-ribosylation inactivated Cp2 and prevented its formation of a tight complex with dinitrogenase from Azotobacter vinelandii (Av1). The complex between Cp2 and Av1 could not be ADP-ribosylated once it formed.

Full text

PDF
609

Images in this article

610Fig. 1.
on p.610
611Fig. 2.
on p.611

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Emerich D. W., Burris R. H. Interactions of heterologous nitrogenase components that generate catalytically inactive complexes. Proc Natl Acad Sci U S A. 1976 Dec;73(12):4369–4373. doi: 10.1073/pnas.73.12.4369. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Emerich D. W., Ljones T., Burris R. H. Nitrogenase: properties of the catalytically inactive complex between the Azotobacter vinelandii MoFe protein and the Clostridium pasteurianum Fe protein. Biochim Biophys Acta. 1978 Dec 8;527(2):359–369. doi: 10.1016/0005-2744(78)90350-9. [DOI] [PubMed] [Google Scholar]
  3. Erbes D. L., Burris R. H. The kinetics of methyl viologen oxidation and reduction by the hydrogenase from Clostridium pasteurianum. Biochim Biophys Acta. 1978 Jul 7;525(1):45–54. doi: 10.1016/0005-2744(78)90198-5. [DOI] [PubMed] [Google Scholar]
  4. GOA J. A micro biuret method for protein determination; determination of total protein in cerebrospinal fluid. Scand J Clin Lab Invest. 1953;5(3):218–222. doi: 10.3109/00365515309094189. [DOI] [PubMed] [Google Scholar]
  5. Lowery R. G., Saari L. L., Ludden P. W. Reversible regulation of the nitrogenase iron protein from Rhodospirillum rubrum by ADP-ribosylation in vitro. J Bacteriol. 1986 May;166(2):513–518. doi: 10.1128/jb.166.2.513-518.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Ludden P. W., Burris R. H. Activating factor for the iron protein of nitrogenase from Rhodospirillum rubrum. Science. 1976 Oct 22;194(4263):424–426. doi: 10.1126/science.824729. [DOI] [PubMed] [Google Scholar]
  7. Nordlund S., Eriksson U., Baltscheffsky H. Necessity of a membrane component for nitrogenase activity in Rhodospirillum rubrum. Biochim Biophys Acta. 1977 Oct 12;462(1):187–195. doi: 10.1016/0005-2728(77)90201-8. [DOI] [PubMed] [Google Scholar]
  8. Pope M. R., Murrell S. A., Ludden P. W. Covalent modification of the iron protein of nitrogenase from Rhodospirillum rubrum by adenosine diphosphoribosylation of a specific arginine residue. Proc Natl Acad Sci U S A. 1985 May;82(10):3173–3177. doi: 10.1073/pnas.82.10.3173. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Saari L. L., Triplett E. W., Ludden P. W. Purification and properties of the activating enzyme for iron protein of nitrogenase from the photosynthetic bacterium Rhodospirillum rubrum. J Biol Chem. 1984 Dec 25;259(24):15502–15508. [PubMed] [Google Scholar]
  10. Shah V. K., Brill W. J. Nitrogenase. IV. Simple method of purification to homogeneity of nitrogenase components from Azotobacter vinelandii. Biochim Biophys Acta. 1973 May 30;305(2):445–454. doi: 10.1016/0005-2728(73)90190-4. [DOI] [PubMed] [Google Scholar]
  11. Stewart W. D., Fitzgerald G. P., Burris R. H. Acetylene reduction by nitrogen-fixing blue-green algae. Arch Mikrobiol. 1968;62(4):336–348. doi: 10.1007/BF00425639. [DOI] [PubMed] [Google Scholar]
  12. Tanaka M., Haniu M., Yasunobu K. T. The amino acid sequence of Clostridium pasteurianum iron protein, a component of nitrogenase. III. The NH2-terminal and COOH-terminal sequences, tryptic peptides of large cyanogen bromide peptides, and the complete sequence. J Biol Chem. 1977 Oct 25;252(20):7093–7100. [PubMed] [Google Scholar]
  13. Tso M. Y., Ljones T., Burris R. H. Purification of the nitrogenase proteins from Clostridium pasteurianum. Biochim Biophys Acta. 1972 Jun 23;267(3):600–604. doi: 10.1016/0005-2728(72)90193-4. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES