Rapid Freeze-Quench ENDOR Study of Chloroperoxidase Compound I: The Site of the Radical
journal contributionposted on 03.05.2006, 00:00 by Sun Hee Kim, Roshan Perera, Lowell P. Hager, John H. Dawson, Brian M. Hoffman
The classical heme-monooxygenase active intermediate, compound I (Cpd-I), incorporates a heme which is oxidized by two equivalents above the resting ferric state, one equivalent associated with a ferryl center, [FeO]2+ (FeS = 1), and the other with an active-site radical (RS = 1/2). Theoretical calculations on models of a Cpd-I with a thiolato axial ligand have presented divergent views about its electronic structure. In one picture, the radical is on the porphyrin; in the other, it is on the sulfur. In this report, ENDOR spectroscopy answers the question, does Cpd-I of the enzyme chloroperoxidase contain a porphyrin π-cation radical or an iron-bound cysteinyl radical: the radical is predominantly on the porphyrin, with spin density on sulfur having an upper bound, ρS ≤ ρSmax ≈ 0.23. We further suggest that the same answer applies to Cpd-I of cytochromes P450.