<?xml version="1.0" encoding="utf-8"?>
<export-example>
  <doc>
    <id>11652</id>
    <completedYear/>
    <publishedYear>2011</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>673</pageFirst>
    <pageLast>679</pageLast>
    <pageNumber/>
    <edition/>
    <issue>5</issue>
    <volume>65</volume>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2014-08-21</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Oxidative cleavage of non-phenolic b-O-4 lignin model dimers by an extracellular aromatic peroxygenase</title>
    <abstract language="eng">The extracellular aromatic peroxygenase of the agaric fungus Agrocybe aegerita catalyzed the H2O2-dependent cleavage of non-phenolic arylglycerol-b-aryl ethers (b-O-4 ethers). For instance 1-(3,4-dimethoxyphenyl)-2-(2-methoxy-phenoxy)pro- pane-1,3-diol, a recalcitrant dimeric lignin model compound that represents the major non-phenolic substructure in lignin, was selectively O-demethylated at the para-methoxy group to give formaldehyde and 1-(4-hydroxy-3-methoxyphenyl)- 2-(2-methoxyphenoxy)propane-1,3-diol. The phenol moiety of the latter compound was then enzymatically oxidized into phenoxy radicals and a quinoid cation, which initiated the autocatalytic cleavage of the dimer and the formation of monomers such as 2-methoxy-1,4-benzoquinone and phenoxyl-substituted propionic acid. The introduction of 18O from H218O2 and H218O at different positions into the products provided information about the routes of ether cleavage. Studies with a 14C-labeled lignin model dimer showed that more than 70% of the intermediates formed were further coupled to form polymers with molecular masses above 10 kDa. The results indicate that fungal aromatic peroxyge- nases may be involved in the bioconversion of methoxylated plant ingredients originating from lignin or other sources.</abstract>
    <parentTitle language="deu">Holzforschung</parentTitle>
    <identifier type="doi">10.1515/HF.2011.057</identifier>
    <identifier type="issn">1437-434X</identifier>
    <enrichment key="BTU">nicht an der BTU erstellt / not created at BTU</enrichment>
    <author>
      <firstName>Matthias</firstName>
      <lastName>Kinne</lastName>
    </author>
    <submitter>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </submitter>
    <author>
      <firstName>Marzena</firstName>
      <lastName>Poraj-Kobielska</lastName>
    </author>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Paula</firstName>
      <lastName>Nousiainen</lastName>
    </author>
    <author>
      <firstName>Jussi</firstName>
      <lastName>Sipilä</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>Kenneth E.</firstName>
      <lastName>Hammel</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Agrocybe aegerita</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>hydroxylation</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>lignin model compound</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>0-dealkylation</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>peroxidase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>peroxygenase</value>
    </subject>
    <collection role="old_institute" number="06010">Prof. Enzymtechnologie</collection>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
  <doc>
    <id>11654</id>
    <completedYear/>
    <publishedYear>2011</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>789</pageFirst>
    <pageLast>796</pageLast>
    <pageNumber/>
    <edition/>
    <issue>7</issue>
    <volume>82</volume>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2014-08-21</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Preparation of human drug metabolites using fungal peroxygenases</title>
    <abstract language="eng">The synthesis of hydroxylated and O- or N-dealkylated human drug metabolites (HDMs) via selective monooxygenation remains a challenging task for synthetic organic chemists. Here we report that aromatic peroxygenases (APOs; EC 1.11.2.1) secreted by the agaric fungi Agrocybe aegerita and Coprinellus radians catalyzed the H₂O₂-dependent selective monooxygenation of diverse drugs, including acetanilide, dextrorphan, ibuprofen, naproxen, phenacetin, sildenafil and tolbutamide. Reactions included the hydroxylation of aromatic rings and aliphatic side chains, as well as O- and N-dealkylations and exhibited different regioselectivities depending on the particular APO used. At best, desired HDMs were obtained in yields greater than 80% and with isomeric purities up to 99%. Oxidations of tolbutamide, acetanilide and carbamazepine in the presence of H₂¹⁸O₂ resulted in almost complete incorporation of ¹⁸O into the corresponding products, thus establishing that these reactions are peroxygenations. The deethylation of phenacetin-d₁ showed an observed intramolecular deuterium isotope effect [(k(H)/k(D))(obs)] of 3.1±0.2, which is consistent with the existence of a cytochrome P450-like intermediate in the reaction cycle of APOs. Our results indicate that fungal peroxygenases may be useful biocatalytic tools to prepare pharmacologically relevant drug metabolites.</abstract>
    <parentTitle language="eng">Biochemical Pharmacology</parentTitle>
    <identifier type="doi">10.1016/j.bcp.2011.06.020</identifier>
    <identifier type="url">http://www.sciencedirect.com/science/article/pii/S0006295211004035</identifier>
    <identifier type="issn">1873-2968</identifier>
    <enrichment key="BTU">nicht an der BTU erstellt / not created at BTU</enrichment>
    <author>
      <firstName>Marzena</firstName>
      <lastName>Poraj-Kobielska</lastName>
    </author>
    <submitter>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </submitter>
    <author>
      <firstName>Matthias</firstName>
      <lastName>Kinne</lastName>
    </author>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>Gernot</firstName>
      <lastName>Kayser</lastName>
    </author>
    <author>
      <firstName>Kenneth E.</firstName>
      <lastName>Hammel</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxidase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxygenation</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Hydroxylation</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>O-Dealkylation</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>N-Dealkylation</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Cytochrome P450</value>
    </subject>
    <collection role="old_institute" number="06010">Prof. Enzymtechnologie</collection>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
  <doc>
    <id>11658</id>
    <completedYear/>
    <publishedYear>2009</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>3085</pageFirst>
    <pageLast>3087</pageLast>
    <pageNumber/>
    <edition/>
    <issue>11</issue>
    <volume>19</volume>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2014-08-21</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Regioselective preparation of 5-hydroxypropranolol and 4′-hydroxydiclofenac with a fungal peroxygenase</title>
    <abstract language="eng">An extracellular peroxygenase of Agrocybe aegerita catalyzed the H2O2-dependent hydroxylation of the multi-function beta-adrenergic blocker propranolol (1-naphthalen-1-yloxy-3-(propan-2-ylamino)propan-2-ol) and the non-steroidal anti-inflammatory drug diclofenac (2-[2-[(2,6-dichlorophenyl)amino]phenyl]acetic acid) to give the human drug metabolites 5-hydroxypropranolol (5-OHP) and 4′-hydroxydiclofenac (4′-OHD). The reactions proceeded regioselectively with high isomeric purity and gave the desired 5-OHP and 4′-OHD in yields up to 20% and 65%, respectively. 18O-labeling experiments showed that the phenolic hydroxyl groups in 5-OHP and 4′-OHD originated from H2O2, which establishes that the reaction is mechanistically a peroxygenation. Our results raise the possibility that fungal peroxygenases may be useful for versatile, cost-effective, and scalable syntheses of drug metabolites.</abstract>
    <parentTitle language="eng">Bioorganic &amp; Medicinal Chemistry Letters</parentTitle>
    <identifier type="doi">10.1016/j.bmcl.2009.04.015</identifier>
    <identifier type="url">http://www.sciencedirect.com/science/article/pii/S0960894X09005071</identifier>
    <identifier type="issn">1464-3405</identifier>
    <enrichment key="BTU">nicht an der BTU erstellt / not created at BTU</enrichment>
    <author>
      <firstName>Matthias</firstName>
      <lastName>Kinne</lastName>
    </author>
    <submitter>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </submitter>
    <author>
      <firstName>Marzena</firstName>
      <lastName>Poraj-Kobielska</lastName>
    </author>
    <author>
      <firstName>Elisabet</firstName>
      <lastName>Aranda</lastName>
    </author>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Kenneth E.</firstName>
      <lastName>Hammel</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxidase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxygenase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Oxygenase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Cytochrome P450</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Hydroxylation</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>5-Hydroxypropranolol</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Propranolol</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>4′-Hydroxydiclofenac</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Diclofenac</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Ascorbic acid</value>
    </subject>
    <collection role="old_institute" number="06010">Prof. Enzymtechnologie</collection>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
  <doc>
    <id>11660</id>
    <completedYear/>
    <publishedYear>2008</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>5950</pageFirst>
    <pageLast>5953</pageLast>
    <pageNumber/>
    <edition/>
    <issue>41</issue>
    <volume>49</volume>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2014-08-21</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Regioselective preparation of (R)-2-(4-Hydroxyphenoxy)propionic acid with a fungal peroxygenase</title>
    <abstract language="eng">The extracellular heme-thiolate peroxygenase of Agrocybe aegerita catalyzed the H2O2-dependent hydroxylation of 2-phenoxypropionic acid (POPA) to give the herbicide precursor 2-(4-hydroxyphenoxy)propionic acid (HPOPA). The reaction proceeded regioselectively with an isomeric purity near 98%, and yielded the desired R-isomer of HPOPA with an enantiomeric excess of 60%. 18O-labeling experiments showed that the phenolic hydroxyl in HPOPA originated from H2O2, which establishes that the reaction is mechanistically a peroxygenation. Our results raise the possibility that fungal peroxygenases may be useful for a variety of organic oxidations.</abstract>
    <parentTitle language="eng">Tetrahedron Letters</parentTitle>
    <identifier type="doi">10.1016/j.tetlet.2008.07.152</identifier>
    <identifier type="url">http://www.sciencedirect.com/science/article/pii/S0040403908014421</identifier>
    <identifier type="issn">1873-3581</identifier>
    <enrichment key="BTU">nicht an der BTU erstellt / not created at BTU</enrichment>
    <author>
      <firstName>Matthias</firstName>
      <lastName>Kinne</lastName>
    </author>
    <submitter>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </submitter>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Kenneth E.</firstName>
      <lastName>Hammel</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxidase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxygenase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Oxygenase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Cytochrome P450</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Hydroxylation</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>2-(4-Hydroxyphenoxy)propionic acid</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Ascorbic acid</value>
    </subject>
    <collection role="old_institute" number="06010">Prof. Enzymtechnologie</collection>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
</export-example>
