Structural models for the metal centers in the nitrogenase molybdenum-iron protein.

@article{Kim1992StructuralMF,
  title={Structural models for the metal centers in the nitrogenase molybdenum-iron protein.},
  author={Jongmin Kim and Douglas C Rees},
  journal={Science},
  year={1992},
  volume={257 5077},
  pages={1677-82}
}
Structural models for the nitrogenase FeMo-cofactor and P-clusters are proposed based on crystallographic analysis of the nitrogenase molybdenum-iron (MoFe)-protein from Azotobacter vinelandii at 2.7 angstrom resolution. Each center consists of two bridged clusters; the FeMo-cofactor has 4Fe:3S and 1Mo:3Fe:3S clusters bridged by three non-protein ligands, and the P-clusters contain two 4Fe:4S clusters bridged by two cysteine thiol ligands. Six of the seven Fe sites in the FeMo-cofactor appear… CONTINUE READING

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