Abstract
Shakespeare recognized centuries ago the value of a foil for highlighting similarities and differences between characters. Comparative analysis is also an effective mechanism for studying related proteins to better understand the structural basis of their functions. Indeed, there are many similarities between peroxidases and cytochromes P450 (P450s) in terms of prosthetic group and catalytic mechanism. However, there are also important differences in three-dimensional structure, reactions catalyzed, and interactions with other proteins. As a result, these two classes of oxidizing enzymes evolved to fulfill very different functions. Peroxidases and P450s are hemeproteins; both react with peroxides to generate higher oxidation states; and both catalyze oxidation and oxygenation reactions that involve electron transfer from the substrate to the higher oxidation states. The major differences between peroxidases and P450s include the ability of P450s to accept electrons from a reductase; the redox potentials of the higher oxidation states; and the ability of P450s to generate the equivalent of a metal-bound peroxide by reduction of O2 at the heme center during catalytic turnover.
Osric: You are not ignorant of what excellence Laertes is—
Hamlet: I dare not confess that, lest I should compare with him in excellence; but to know a man well were to know himself.
William Shakespeare,
The Tragedy of Hamlet, Prince of Denmark
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Marnett, L.J., Kennedy, T.A. (1995). Comparison of the Peroxidase Activity of Hemoproteins and Cytochrome P450. In: de Montellano, P.R.O. (eds) Cytochrome P450. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-2391-5_2
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