Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect.

@article{Vidakovic1998UnderstandingTR,
  title={Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect.},
  author={Marijana Vidakovic and Stephen G Sligar and Huiying Li and Thomas L Poulos},
  journal={Biochemistry},
  year={1998},
  volume={37 26},
  pages={9211-9}
}
Proton transfer in cytochromes P450 is a critical step in the activation of molecular oxygen. Extensive study of the P450cam active site has identified several residues that play a central role in dioxygen bond scission. A highly conserved carboxylate, aspartate-251 in P450cam in the distal helix I, participates in a series of hydrogen-bond/ion pairs near the molecular surface and has been implicated in the catalytic mechanism. Mutation of Asp251 is known to lower activity by 2 orders of… CONTINUE READING

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