The alternative nitrogenase of Azotobacter chroococcum is a vanadium enzyme

@article{Robson1986TheAN,
  title={The alternative nitrogenase of Azotobacter chroococcum is a vanadium enzyme},
  author={R. Robson and R. Eady and T. Richardson and Richard W. Miller and M. Hawkins and J. Postgate},
  journal={Nature},
  year={1986},
  volume={322},
  pages={388-390}
}
The requirement for molybdenum in biological dinitrogen fixation, first reported by Bortels1, is due to its involvement at or near the site of reduction of N2 in conventional nitrogenase. To date, all nitrogenases which have been purified to homogeneity consist of an iron protein (component 2) and a molybdoprotein (component 1)2. Azotobacter vinelandii, an obligately aerobic diazotrophic bacterium, has two systems for nitrogen fixation: a conventional nitrogenase involving molybdenum and an… Expand
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References

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Nitrogenase from vanadium-grown Azotobacter: isolation, characteristics, and mechanistic implications.
The nitrogenase system from Azotobacter: two-enzyme requirement for N2 reduction, ATP-dependent H2 evolution, and ATP hydrolysis.
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Advances in Nitrogen Fixation Research
A vanadium containing nitrogenase preparation: implications for the role of molybdenum in nitrogen fixation.
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