A new look at the role of thiolate ligation in cytochrome P450
Protonated ferryl (or iron(IV)hydroxide) intermediates have been characterized in several thiolate-ligated heme proteins that are known to catalyze C–H bond activation. The basicity of the ferryl intermediates in these species has been proposed to play a critical role in facilitating this chemistry,...
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| Veröffentlicht in: | Journal of biological inorganic chemistry 2017-04, Vol.22 (2-3), p.209-220 |
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| container_title | Journal of biological inorganic chemistry |
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| creator | Yosca, Timothy H. Ledray, Aaron P. Ngo, Joanna Green, Michael T. |
| description | Protonated ferryl (or iron(IV)hydroxide) intermediates have been characterized in several thiolate-ligated heme proteins that are known to catalyze C–H bond activation. The basicity of the ferryl intermediates in these species has been proposed to play a critical role in facilitating this chemistry, allowing hydrogen abstraction at reduction potentials below those that would otherwise lead to oxidative degradation of the enzyme. In this contribution, we discuss the events that led to the assignment and characterization of the unusual iron(IV)hydroxide species, highlighting experiments that provided a quantitative measure of the ferryl basicity, the iron(IV)hydroxide pKa. We then turn to the importance of the iron(IV)hydroxide state, presenting a new way of looking at the role of thiolate ligation in these systems.
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| doi_str_mv | 10.1007/s00775-016-1430-3 |
| format | Article |
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The basicity of the ferryl intermediates in these species has been proposed to play a critical role in facilitating this chemistry, allowing hydrogen abstraction at reduction potentials below those that would otherwise lead to oxidative degradation of the enzyme. In this contribution, we discuss the events that led to the assignment and characterization of the unusual iron(IV)hydroxide species, highlighting experiments that provided a quantitative measure of the ferryl basicity, the iron(IV)hydroxide pKa. We then turn to the importance of the iron(IV)hydroxide state, presenting a new way of looking at the role of thiolate ligation in these systems.
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| subjects | 60 Years of Oxygen Activation Biochemistry Biomedical and Life Sciences Commentary Cytochrome P-450 Enzyme System - chemistry Cytochrome P-450 Enzyme System - metabolism Cytochrome P450 Ferric Compounds - chemistry Ferric Compounds - metabolism Heme proteins Inorganic chemistry Intermediates Iron Life Sciences Microbiology Sulfhydryl Compounds - chemistry Sulfhydryl Compounds - metabolism |
| title | A new look at the role of thiolate ligation in cytochrome P450 |
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