. 2014 Jun 5;53(23):3781–3789. doi: 10.1021/bi500353p

Table 1. Assignments of the Sites for the Two Primary Tyr^• Intermediates in Cytochrome c Peroxidase (CcP) and the Reaction with the Guaiacol Substrate, Based on the EPR Characterization of the Designed CcP Variants Shown in Panels A and B of Figures 1 and 4.

graphic file with name bi-2014-00353p_0005.jpg

The colors highlight the four different Tyr radical signals that correspond to those in Figures 1 and 4.

The percentage of Tyr radical(s) yield for the variants was estimated by comparison of the signal intensity with that of the wild-type CcP with H₂O₂ (considered the 100% yield).

Tyr sites that contribute to the Tyr^• EPR signal in each sample.

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The underlined residues are those inducing EPR spectral changes, consistent with suppression of the primary Tyr radical sites. The W51F variant indirectly impeded the formation of Tyr₇₁^• by the disruption of the long-range electron transfer pathway, while the F89L variant destabilized radical formation on Tyr₇₁ by inducing steric effects on its microenvironment (see the text).

Table 1. Assignments of the Sites for the Two Primary Tyr• Intermediates in Cytochrome c Peroxidase (CcP) and the Reaction with the Guaiacol Substrate, Based on the EPR Characterization of the Designed CcP Variants Shown in Panels A and B of Figures 1 and 4.

Table 1. Assignments of the Sites for the Two Primary Tyr^• Intermediates in Cytochrome c Peroxidase (CcP) and the Reaction with the Guaiacol Substrate, Based on the EPR Characterization of the Designed CcP Variants Shown in Panels A and B of Figures 1 and 4.