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H(2)O(2)-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin
The O(2)-binding carboxylate-bridged diiron site in DcrH-Hr was engineered in an effort to perform the H(2)O(2)-dependent oxidation of external substrates. A His residue was introduced near the diiron site in place of a conserved residue, Ile119. The I119H variant promotes the oxidation of guaiacol...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Royal Society of Chemistry
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3947700/ https://www.ncbi.nlm.nih.gov/pubmed/24400317 http://dx.doi.org/10.1039/c3cc48108e |
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author | Okamoto, Yasunori Onoda, Akira Sugimoto, Hiroshi Takano, Yu Hirota, Shun Kurtz, Donald M. Shiro, Yoshitsugu Hayashi, Takashi |
author_facet | Okamoto, Yasunori Onoda, Akira Sugimoto, Hiroshi Takano, Yu Hirota, Shun Kurtz, Donald M. Shiro, Yoshitsugu Hayashi, Takashi |
author_sort | Okamoto, Yasunori |
collection | PubMed |
description | The O(2)-binding carboxylate-bridged diiron site in DcrH-Hr was engineered in an effort to perform the H(2)O(2)-dependent oxidation of external substrates. A His residue was introduced near the diiron site in place of a conserved residue, Ile119. The I119H variant promotes the oxidation of guaiacol and 1,4-cyclohexadiene upon addition of H(2)O(2). |
format | Online Article Text |
id | pubmed-3947700 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-39477002014-11-05 H(2)O(2)-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin Okamoto, Yasunori Onoda, Akira Sugimoto, Hiroshi Takano, Yu Hirota, Shun Kurtz, Donald M. Shiro, Yoshitsugu Hayashi, Takashi Chem Commun (Camb) Chemistry The O(2)-binding carboxylate-bridged diiron site in DcrH-Hr was engineered in an effort to perform the H(2)O(2)-dependent oxidation of external substrates. A His residue was introduced near the diiron site in place of a conserved residue, Ile119. The I119H variant promotes the oxidation of guaiacol and 1,4-cyclohexadiene upon addition of H(2)O(2). Royal Society of Chemistry 2014-04-04 2014-01-08 /pmc/articles/PMC3947700/ /pubmed/24400317 http://dx.doi.org/10.1039/c3cc48108e Text en This journal is © The Royal Society of Chemistry 2014 https://creativecommons.org/licenses/by/3.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution 3.0 Unported License (http://creativecommons.org/licenses/by/3.0/ (https://creativecommons.org/licenses/by/3.0/) ) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Chemistry Okamoto, Yasunori Onoda, Akira Sugimoto, Hiroshi Takano, Yu Hirota, Shun Kurtz, Donald M. Shiro, Yoshitsugu Hayashi, Takashi H(2)O(2)-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin |
title | H(2)O(2)-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin
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title_full | H(2)O(2)-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin
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title_fullStr | H(2)O(2)-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin
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title_full_unstemmed | H(2)O(2)-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin
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title_short | H(2)O(2)-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin
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title_sort | h(2)o(2)-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3947700/ https://www.ncbi.nlm.nih.gov/pubmed/24400317 http://dx.doi.org/10.1039/c3cc48108e |
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