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Azotobacter vinelandii is diazotroph that can fix nitrogen while grown aerobically. It is a genetically tractable system that is used to study nitrogen fixation. These bacteria are easily cultured and grown.
The nitrogenase holoenzyme of Azotobacter vinelandii has been characterised via x-ray crystallography in both ADP tetrafluoroaluminate-bound and MgATP-bound states. The enzyme possesses molybdenum iron-sulfido cluster cofactors (FeMoCo) as active sites, each bearing 2 pseudo-cubic iron-sulfido structures.
- William A. Noyes, ed. (1904). Review of American Chemical Research 10. p. 75.
- Schindelin, H., Kisker, C., Schlessman, J.L., Howard, J.B., Rees, D.C. (1997) Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction. Nature 387: 370-376
- Chiu, H., Peters, J.W., Lanzilotta, W.N., Ryle, M.J., Seefeldt, L.C., Howard, J.B., Rees, D.C. (2001) MgATP-Bound and nucleotide-free structures of a nitrogenase protein complex between the Leu 127 Delta-Fe-protein and the MoFe-protein. Biochemistry 40: 641-650
- Azotobacter vinelandii Genome Project
- Current research on Azotobacter vinelandii at the Norwich Research Park
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