Peroxygenase activity of cytochrome c peroxidase and three apolar distal heme pocket mutants: hydroxylation of 1-methoxynaphthalene
Department of Chemistry and Biochemistry, Northern Illinois University, DeKalb, IL 60115, USA
BMC Biochemistry 2013, 14:19 doi:10.1186/1471-2091-14-19Published: 30 July 2013
Additional file 1:
The additional file provided with this paper contains 8 figures and 1 table.Figure SA.1. Spectrum of Russig’s blue in organic and aqueous solution. Figure SA.2, Figure SA.2, and Figure SA.3. Spectral scans CcP(triLeu)-, CcP(triVal)-, and rCcP-catalyzed formation of Russig’s blue, respectively. Figure SA.5. Dependence of the initial velocity for CcP(triAla)-catalyzed formation of Russig’s blue on the concentration of 1-methoxynaphthalene. Figure SA.6. Dependence of the initial velocity for CcP(triAla)-catalyzed formation of Russig’s blue on the concentration of hydrogen peroxide. Figure SA.7. Histogram of the peroxygenase activity of rCcP, 20 CcP mutants, and selected other heme proteins. Figure SA.8. Percent heme degradation during the peroxygenase reaction for the heme proteins included in Figure SA.7. Table SA.1. Peroxygenase activity of rCcP, 20 CcP mutants, and selected other heme proteins.
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