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Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Proceedings of the National Academy of Sciences, 112, 2015, 12, S. 3686-3691 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
|
| Schlagwörter: |
| author_facet |
Wang, Xiaoshi Ullrich, René Hofrichter, Martin Groves, John T. Wang, Xiaoshi Ullrich, René Hofrichter, Martin Groves, John T. |
|---|---|
| author |
Wang, Xiaoshi Ullrich, René Hofrichter, Martin Groves, John T. |
| spellingShingle |
Wang, Xiaoshi Ullrich, René Hofrichter, Martin Groves, John T. Proceedings of the National Academy of Sciences Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive Multidisciplinary |
| author_sort |
wang, xiaoshi |
| spelling |
Wang, Xiaoshi Ullrich, René Hofrichter, Martin Groves, John T. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1503340112 <jats:title>Significance</jats:title> <jats:p> The heme-thiolate peroxygenase of <jats:italic>Agrocybe aegerita</jats:italic> is a remarkably capable biocatalyst and a mechanistic analog of cytochrome P450. The stability of this fungal protein has provided a rare opportunity to study P450-like C−H hydroxylation in a novel and unrelated enzyme. Both APO-I and APO-II have been generated, and their redox potentials have been determined. The ferryl species Cys−S−Fe <jats:sup>IV</jats:sup> −OH (APO-II) has been generated cleanly via reduction of the corresponding APO-I and a basic p <jats:italic>K</jats:italic> <jats:sub>a</jats:sub> revealed for the Cys−S−Fe <jats:sup>IV</jats:sup> −OH ⇄ Cys−S−Fe <jats:sup>IV</jats:sup> =O equilibrium. Most significantly, APO-II displays surprisingly high reactivity toward benzylic C−H (bond-dissociation energy 80−86 kcal/mol) and phenolic substrates with rate constants orders of magnitude larger than those of typical peroxidases or model compounds due to the basic ferryl. </jats:p> Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive Proceedings of the National Academy of Sciences |
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| title |
Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive |
| title_unstemmed |
Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive |
| title_full |
Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive |
| title_fullStr |
Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive |
| title_full_unstemmed |
Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive |
| title_short |
Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive |
| title_sort |
heme-thiolate ferryl of aromatic peroxygenase is basic and reactive |
| topic |
Multidisciplinary |
| url |
http://dx.doi.org/10.1073/pnas.1503340112 |
| publishDate |
2015 |
| physical |
3686-3691 |
| description |
<jats:title>Significance</jats:title>
<jats:p>
The heme-thiolate peroxygenase of
<jats:italic>Agrocybe aegerita</jats:italic>
is a remarkably capable biocatalyst and a mechanistic analog of cytochrome P450. The stability of this fungal protein has provided a rare opportunity to study P450-like C−H hydroxylation in a novel and unrelated enzyme. Both APO-I and APO-II have been generated, and their redox potentials have been determined. The ferryl species Cys−S−Fe
<jats:sup>IV</jats:sup>
−OH (APO-II) has been generated cleanly via reduction of the corresponding APO-I and a basic p
<jats:italic>K</jats:italic>
<jats:sub>a</jats:sub>
revealed for the Cys−S−Fe
<jats:sup>IV</jats:sup>
−OH ⇄ Cys−S−Fe
<jats:sup>IV</jats:sup>
=O equilibrium. Most significantly, APO-II displays surprisingly high reactivity toward benzylic C−H (bond-dissociation energy 80−86 kcal/mol) and phenolic substrates with rate constants orders of magnitude larger than those of typical peroxidases or model compounds due to the basic ferryl.
</jats:p> |
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| author | Wang, Xiaoshi, Ullrich, René, Hofrichter, Martin, Groves, John T. |
| author_facet | Wang, Xiaoshi, Ullrich, René, Hofrichter, Martin, Groves, John T., Wang, Xiaoshi, Ullrich, René, Hofrichter, Martin, Groves, John T. |
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| description | <jats:title>Significance</jats:title> <jats:p> The heme-thiolate peroxygenase of <jats:italic>Agrocybe aegerita</jats:italic> is a remarkably capable biocatalyst and a mechanistic analog of cytochrome P450. The stability of this fungal protein has provided a rare opportunity to study P450-like C−H hydroxylation in a novel and unrelated enzyme. Both APO-I and APO-II have been generated, and their redox potentials have been determined. The ferryl species Cys−S−Fe <jats:sup>IV</jats:sup> −OH (APO-II) has been generated cleanly via reduction of the corresponding APO-I and a basic p <jats:italic>K</jats:italic> <jats:sub>a</jats:sub> revealed for the Cys−S−Fe <jats:sup>IV</jats:sup> −OH ⇄ Cys−S−Fe <jats:sup>IV</jats:sup> =O equilibrium. Most significantly, APO-II displays surprisingly high reactivity toward benzylic C−H (bond-dissociation energy 80−86 kcal/mol) and phenolic substrates with rate constants orders of magnitude larger than those of typical peroxidases or model compounds due to the basic ferryl. </jats:p> |
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| imprint | Proceedings of the National Academy of Sciences, 2015 |
| imprint_str_mv | Proceedings of the National Academy of Sciences, 2015 |
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| spelling | Wang, Xiaoshi Ullrich, René Hofrichter, Martin Groves, John T. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1503340112 <jats:title>Significance</jats:title> <jats:p> The heme-thiolate peroxygenase of <jats:italic>Agrocybe aegerita</jats:italic> is a remarkably capable biocatalyst and a mechanistic analog of cytochrome P450. The stability of this fungal protein has provided a rare opportunity to study P450-like C−H hydroxylation in a novel and unrelated enzyme. Both APO-I and APO-II have been generated, and their redox potentials have been determined. The ferryl species Cys−S−Fe <jats:sup>IV</jats:sup> −OH (APO-II) has been generated cleanly via reduction of the corresponding APO-I and a basic p <jats:italic>K</jats:italic> <jats:sub>a</jats:sub> revealed for the Cys−S−Fe <jats:sup>IV</jats:sup> −OH ⇄ Cys−S−Fe <jats:sup>IV</jats:sup> =O equilibrium. Most significantly, APO-II displays surprisingly high reactivity toward benzylic C−H (bond-dissociation energy 80−86 kcal/mol) and phenolic substrates with rate constants orders of magnitude larger than those of typical peroxidases or model compounds due to the basic ferryl. </jats:p> Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive Proceedings of the National Academy of Sciences |
| spellingShingle | Wang, Xiaoshi, Ullrich, René, Hofrichter, Martin, Groves, John T., Proceedings of the National Academy of Sciences, Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive, Multidisciplinary |
| title | Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive |
| title_full | Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive |
| title_fullStr | Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive |
| title_full_unstemmed | Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive |
| title_short | Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive |
| title_sort | heme-thiolate ferryl of aromatic peroxygenase is basic and reactive |
| title_unstemmed | Heme-thiolate ferryl of aromatic peroxygenase is basic and reactive |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.1503340112 |