Article
Ionic interactions in the nitrogenase complex. Properties of Fe-protein containing substitutions for Arg-100.
The Journal of biological chemistry - 25 Feb 1992
Wolle D, Kim C, Dean D, Howard J B
Abstract excerpt
A series of Azotobacter vinelandii strains have been constructed in which the nitrogenase Fe-protein (Av2) was altered by substitutions for Arg-100. This invariant residue is a likely partner in a salt bridge with the MoFe-protein and, in some species, is the site of reversible regulation by ADP-ribosylation (Pope, M. R., Murrell, S. A., and Ludden, P. W. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 3173-3177)....
Topics
- Acetylene
- Adenosine Triphosphate
- Arginine
- Azotobacter vinelandii
- Catalysis
- Genes, Bacterial
- Ions
- Klebsiella pneumoniae
- Mutation
- Nitrogenase
- Oxidation-Reduction