Covalent linkage of prosthetic heme to CYP4 family P450 enzymes.

@article{Henne2001CovalentLO,
  title={Covalent linkage of prosthetic heme to CYP4 family P450 enzymes.},
  author={Kirk R. Henne and Kent L. Kunze and Yi-min Zheng and Peter Christmas and Roy J. Soberman and Allan E Rettie},
  journal={Biochemistry},
  year={2001},
  volume={40 43},
  pages={
          12925-31
        }
}
An extensive body of research on the structural properties of cytochrome P450 enzymes has established that these proteins possess a b-type heme prosthetic group which is noncovalently bound at the active site. Coordinate, electrostatic, and hydrogen bond interactions between the protein backbone and heme functional groups are readily overcome upon mild acid treatment of the enzyme, which releases free heme from the protein. In the present study, we have used a combination of HPLC, LC/ESI-MS… CONTINUE READING

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