Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum.

@article{Schlessman1998ConformationalVI,
  title={Conformational variability in structures of the nitrogenase iron proteins from Azotobacter vinelandii and Clostridium pasteurianum.},
  author={Jamie L. Schlessman and Denise K Woo and Leemor Joshua-Tor and James W. Howard and Douglas C Rees},
  journal={Journal of molecular biology},
  year={1998},
  volume={280 4},
  pages={669-85}
}
The nitrogenase iron (Fe) protein performs multiple functions during biological nitrogen fixation, including mediating the mechanistically essential coupling between ATP hydrolysis and electron transfer to the nitrogenase molybdenum iron (MoFe) protein during substrate reduction, and participating in the biosynthesis and insertion of the FeMo-cofactor into the MoFe-protein. To establish a structural framework for addressing the diverse functions of Fe-protein, crystal structures of the Fe… CONTINUE READING