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Area of Science:

  • Biochemistry
  • Computational Chemistry
  • Spectroscopy

Background:

  • Cytochrome P450 enzymes are crucial for biological oxidation reactions.
  • The active state of P450 enzymes, the ferryl species, plays a key role in catalysis.
  • Understanding the protonation state of the ferryl species is essential for elucidating enzyme mechanisms.

Purpose of the Study:

  • To determine the protonation state of the ferryl forms of P450(BM3) and P450cam at physiological pH.
  • To investigate the impact of protonation on the Mössbauer parameters of ferryl species.
  • To provide insights into the electronic structure of heme active sites in P450 enzymes.

Main Methods:

  • Mössbauer spectroscopy was employed to experimentally measure the parameters of the ferryl species.
  • Density functional calculations were performed on large active-site models.
  • Theoretical Mössbauer parameters were calculated for both protonated and unprotonated ferryl species.

Main Results:

  • Calculations revealed a significant increase in the quadrupole splitting parameter upon protonation of the ferryl unit.
  • Experimental quadrupole splitting values for P450(BM3) and P450cam closely matched the calculated values for the protonated ferryl forms.
  • The ferryl forms of P450(BM3) and P450cam are determined to be protonated at physiological pH.

Conclusions:

  • The ferryl forms of P450(BM3) and P450cam are protonated under physiological conditions.
  • Protonation of the ferryl unit leads to a distinct enlargement of the quadrupole splitting parameter.
  • These findings suggest that protonated ferryls are a common feature of thiolate-ligated hemes in P450 enzymes.