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Salt-link stability in cytochrome P450cam
The strengths of all salt-links relative to mutation to their hydrophobic isosteres were computed by numerical solution of the finite-difference Poisson-Boltzmann equation (Lounnas & Wade, in preparation). A continuum model of the solvent was used and the protein was treated as a continuous dielectric medium with partial atomic charges embedded in it. The distribution of the computed salt-link electrostatic free energies is shown in the histogram below. The computed free energy of each salt-link is given relative to its apolar uncharged isostere (hydrophobic isostere). Thus negative values indicate salt-links which are more stable than their hydrophobic isosteres. Of the four most stable salt-links, two are made to the heme propionate groups and two are to Asp251. Thus, it appears that cytochrome P450cam has evolved stable salt-links to perform important functional roles: keeping the heme cofactor in place and regulating substrate access to the active site.
Figure 5. Distribution of the computed electrostatic free energies of the salt-links in cytochrome P450cam
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Wade et al. (1996) Fundamentals of Enzyme-Ligand Interactions in
Cytochrome P450cam
POPE5 Conference Proceedings
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