Comparative biochemical characterization of the iron-only nitrogenase and the molybdenum nitrogenase from Rhodobacter capsulatus.

@article{Schneider1997ComparativeBC,
  title={Comparative biochemical characterization of the iron-only nitrogenase and the molybdenum nitrogenase from Rhodobacter capsulatus.},
  author={Korbinian M H Schneider and U. Gollan and Melanie Dr{\"o}ttboom and S. Selsemeier-Voigt and Anika M{\"u}ller},
  journal={European journal of biochemistry},
  year={1997},
  volume={244 3},
  pages={789-800}
}
The component proteins of the iron-only nitrogenase were isolated from Rhodobacter capsulatus (delta nifHDK, delta modABCD strain) and purified in a one-day procedure that included only one column-chromatography step (DEAE-Sephacel). This procedure yielded component 1 (FeFe protein, Rc1Fe), which was more than 95% pure, and an approximately 80% pure component 2 (Fe protein, Rc2Fe). The highest specific activities, which were achieved at an Rc2Fe/Rc1Fe molar ratio of 40:1, were 260 (C2H4 from… CONTINUE READING

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