Structural factors governing azide and cyanide binding to mammalian metmyoglobins.

@article{Brancaccio1994StructuralFG,
  title={Structural factors governing azide and cyanide binding to mammalian metmyoglobins.},
  author={Andrea Brancaccio and Francesca Cutruzzol{\`a} and C T Allocatelli and Maurizio Brunori and Stephen J. Smerdon and Anthony James Wilkinson and Y C Dou and Deborah Keenan and Masao Ikeda-Saito and R E Brantley},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 19},
  pages={13843-53}
}
The structural factors governing azide and cyanide binding have been examined by measuring the effects of 46 mutations at key topological positions in the distal pocket in sperm whale, pig, and human myoglobin. Replacement of His64 (E7) with smaller amino acids results in dramatic increases in the association rate constant for azide binding primarily due to relief of steric hindrance imposed by the imidazole side chain. Gln64 and His64 (native) metmyoglobins have abnormally low rate constants… CONTINUE READING
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