Mössbauer and Integer-Spin EPR Studies and Spin-Coupling Analysis of the [ 4 Fe-4 S ] 0 Cluster of the Fe Protein from Azotobacter V inelandii Nitrogenase

@inproceedings{Yoo1999MssbauerAI,
  title={M{\"o}ssbauer and Integer-Spin EPR Studies and Spin-Coupling Analysis of the [ 4 Fe-4 S ] 0 Cluster of the Fe Protein from Azotobacter V inelandii Nitrogenase},
  author={Sun Jae Yoo and Hayley C. Angove and Barbara K. Burgess and Michael P Hendrich and Eckard Mu},
  year={1999}
}
We have previously shown that the [4Fe-4S] cluster of the Fe protein of nitrogenase from Azotobacter Vinelandii can be reduced to the all-ferrous state, [4Fe-4S] 0. We have studied here this state with integer-spin EPR and Mo ̈ssbauer spectroscopy, and analyzed the exchange couplings that give rise to a ground state with cluster spinS ) 4. The results are as follows: The cluster contains four high-spin ( Si ) 2) ferrous sites with isomer shiftδ ) 0.68 mm/s. One site, Fe A, has∆EQ ) 3.08 mm/s… CONTINUE READING