Significantly shorter Fe–S bond in cytochrome P450-I is consistent with greater reactivity relative to chloroperoxidase
http://www.nature.com/nchem/journal/vaop/ncurrent/pdf/nchem.2306.pdf
Nature Chemistry. doi:10.1038/nchem.2306
Authors: Courtney M. Krest, Alexey Silakov, Jonathan Rittle, Timothy H. Yosca, Elizabeth L. Onderko, Julio C. Calixto & Michael T. Green
Cytochrome P450 (P450) and chloroperoxidase (CPO) are both thiolate-ligated haem proteins that form a ferryl radical species called compound I. P450-I is, however, significantly more reactive than CPO-I. Variable-temperature Mössbauer and X-ray absorption measurements have now shown that increased electron donation from the axial thiolate ligand in P450-I may explain its greater propensity for C–H bond activation.
Nature Chemistry. doi:10.1038/nchem.2306
Authors: Courtney M. Krest, Alexey Silakov, Jonathan Rittle, Timothy H. Yosca, Elizabeth L. Onderko, Julio C. Calixto & Michael T. Green
Cytochrome P450 (P450) and chloroperoxidase (CPO) are both thiolate-ligated haem proteins that form a ferryl radical species called compound I. P450-I is, however, significantly more reactive than CPO-I. Variable-temperature Mössbauer and X-ray absorption measurements have now shown that increased electron donation from the axial thiolate ligand in P450-I may explain its greater propensity for C–H bond activation.
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