<?xml version="1.0" encoding="utf-8"?>
<export-example>
  <doc>
    <id>11644</id>
    <completedYear/>
    <publishedYear>2014</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>47</pageFirst>
    <pageLast>51</pageLast>
    <pageNumber/>
    <edition/>
    <issue>103</issue>
    <volume/>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2014-08-21</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Enzymatic one-pot conversion of cyclohexane into cyclohexanone: Comparison of four fungal peroxygenases</title>
    <abstract language="eng">Unspecific peroxygenases (UPO; EC 1.11.2.1) represent a group of secreted heme-thiolate proteins that are capable of catalyzing the mono-oxygenation of diverse organic compounds, using only H2O2 as a co-substrate. Here we show that the four peroxygenases AaeUPO, MroUPO, rCciUPO and rNOVO catalyze the stepwise hydroxylation of cyclohexane to cyclohexanol and cyclohexanone. The catalytic efficiencies (kcat/Km) for the initial hydroxylation were in the same order of magnitude for all four peroxygenases (∼104 M−1 s−1), whereas they differed in the second step. The conversion of cyclohexanol by AaeUPO and rCciUPO was 1–2 orders of magnitude less efficient (∼102 M−1 s−1) than by MroUPO and rNOVO (∼104 M−1 s−1). The highest conversion rate in terms of H2O2 utilization was accomplished by MroUPO under repeated addition of the peroxide (87% in relation to the total products formed). Using the latter UPO, we successfully established a micro-mixing reaction device (SIMM-V2) for the oxidation of cyclohexane. As cyclohexanone is a chemical of high relevance, for example, as starting material for polymer syntheses or as organic solvent, new enzymatic production pathways for this compound are of interest to complement existing chemical and biotechnological approaches. Stable and versatile peroxygenases, as those presented here, may form a promising biocatalytic platform for the development of such enzyme-based processes.</abstract>
    <parentTitle language="eng">Journal of Molecular Catalysis : B, Enzymatic</parentTitle>
    <identifier type="doi">10.1016/j.molcatb.2013.09.016</identifier>
    <identifier type="url">http://www.sciencedirect.com/science/article/pii/S138111771300266X</identifier>
    <enrichment key="BTU">an der BTU erstellt / created at BTU</enrichment>
    <author>
      <firstName>Sebastian</firstName>
      <lastName>Peter</lastName>
    </author>
    <submitter>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </submitter>
    <author>
      <firstName>Alexander</firstName>
      <lastName>Karich</lastName>
    </author>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</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>cyclohexane</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>cyclohexanol</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>cyclohexanone</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>UPO</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>11638</id>
    <completedYear/>
    <publishedYear>2011</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst/>
    <pageLast/>
    <pageNumber/>
    <edition/>
    <issue/>
    <volume/>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2014-08-19</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">High-yield production of aromatic peroxygenase by the agaric fungus Marasmius rotula</title>
    <abstract language="eng">An extracellular peroxygenase from Marasmius rotula was produced in liquid culture, chromatographically purified and partially characterized. This is the third aromatic peroxygenase (APO) that has been characterized in detail and the first one that can be produced in high yields. The highest enzyme levels of about 41,000 U l-1 (corresponding to appr. 445 mg l-1 APO protein) exceeded the hitherto reported levels more than 40-fold and were detected in carbon- and nitrogen-rich complex media. The enzyme was purified by FPLC to apparent homogeneity (SDS-PAGE) with a molecular mass of 32 kDa (27 kDa after deglycosylation) and isoelectric points between 4.97 and 5.27. The UV-visible spectrum of the native enzyme showed a characteristic maximum (Soret band) at 418 nm that shifted after reduction with sodium dithionite and flushing with carbon monoxide to 443 nm. The pH optimum of the M. rotula enzyme was found to vary between pH 5 and 6 for most reactions studied. The apparent Km-values for 2,6-dimethoxyphenol, benzyl alcohol, veratryl alcohol, naphthalene and H2O2 were 0.133, 0.118, 0.279, 0.791 and 3.14 mM, respectively. M. rotula APO was found to be highly stable in a pH range from 5 to 10 as well as in the presence of organic solvents (50% vol/vol) such as methanol, acetonitrile and N,N-dimethylformamide. Unlike other APOs, the peroxygenase of M. rotula showed neither brominating nor chlorinating activities.</abstract>
    <parentTitle language="eng">AMB Express</parentTitle>
    <identifier type="url">http://www.amb-express.com/content/1/1/31</identifier>
    <identifier type="issn">2191-0855</identifier>
    <enrichment key="BTU">nicht an der BTU erstellt / not created at BTU</enrichment>
    <author>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </author>
    <submitter>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </submitter>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Marek J.</firstName>
      <lastName>Pecyna</lastName>
    </author>
    <author>
      <firstName>Danuta</firstName>
      <lastName>Kapturska</lastName>
    </author>
    <author>
      <firstName>Stephanie</firstName>
      <lastName>Friedrich</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxygenase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxidase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Basidiomycota</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Cytochrome P450</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Bioreactor</value>
    </subject>
    <collection role="old_institute" number="06010">Prof. Enzymtechnologie</collection>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
  <doc>
    <id>18617</id>
    <completedYear/>
    <publishedYear>2015</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>4130</pageFirst>
    <pageLast>4142</pageLast>
    <pageNumber/>
    <edition/>
    <issue>12</issue>
    <volume>81</volume>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2017-02-14</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Steroid hydroxylation by basidiomycete peroxygenases: A combined experimental and computational study</title>
    <abstract language="eng">The goal of this study is the selective oxyfunctionalization of steroids under mild and environmentally-friendly conditions using fungal enzymes. With this purpose, peroxygenases from three basidiomycete species were tested for hydroxylation of a variety of steroidal compounds, using H2O2 as the only cosubstrate. Two of them are wild-type enzymes from Agrocybe aegerita and Marasmius rotula, and the third one is a recombinant enzyme from Coprinopsis cinerea. The enzymatic reactions on free and esterified sterols, and steroid hydrocarbons and ketones were followed by gas chromatography, and the products were identified by mass spectrometry. Hydroxylation at the side chain over the steroidal rings was preferred, with the 25-hydroxyderivatives predominating (interestingly antiviral and other biological activities of 25-hydroxycholesterol have been recently reported). However, hydroxylation in the ring moiety and terminal hydroxylation at the side-chain was also observed in some steroids, the former favored by the absence of oxygenated groups at C3 and by the presence of conjugated double bonds in the rings. To understand the yield and selectivity differences between the different steroids, a computational study was performed using Protein Energy Landscape Exploration (PELE) software for dynamic ligand diffusion. These simulations showed that the active site geometry and hydrophobicity favors the entrance of the steroid side-chain, while the entrance of the ring is energetically penalized. Also, a direct correlation between the conversion rate and the side-chain entrance ratio could be established, that explains the varying reaction yields observed.</abstract>
    <parentTitle language="eng">Applied and Environmental Microbiology</parentTitle>
    <identifier type="doi">10.1128/AEM.00660-15</identifier>
    <identifier type="url">http://aem.asm.org/content/early/2015/04/08/AEM.00660-15</identifier>
    <identifier type="issn">0099-2240</identifier>
    <identifier type="issn">1098-5336</identifier>
    <enrichment key="BTU">an der BTU erstellt / created at BTU</enrichment>
    <author>
      <firstName>Esteban D.</firstName>
      <lastName>Babot</lastName>
    </author>
    <submitter>
      <firstName>Kai-Uwe</firstName>
      <lastName>Schmidtke</lastName>
    </submitter>
    <author>
      <firstName>José C. del</firstName>
      <lastName>Río</lastName>
    </author>
    <author>
      <firstName>Marina</firstName>
      <lastName>Cañellas</lastName>
    </author>
    <author>
      <firstName>Ferran</firstName>
      <lastName>Sancho</lastName>
    </author>
    <author>
      <firstName>Fátima</firstName>
      <lastName>Lucas</lastName>
    </author>
    <author>
      <firstName>Víctor</firstName>
      <lastName>Guallar</lastName>
    </author>
    <author>
      <firstName>Lisbeth</firstName>
      <lastName>Kalum</lastName>
    </author>
    <author>
      <firstName>Henrik</firstName>
      <lastName>Lund</lastName>
    </author>
    <author>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <author>
      <firstName>Angel T.</firstName>
      <lastName>Martínez</lastName>
    </author>
    <author>
      <firstName>Ana</firstName>
      <lastName>Gutiérrez</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Peroxyenase</value>
    </subject>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
  <doc>
    <id>11645</id>
    <completedYear/>
    <publishedYear>2013</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>34767</pageFirst>
    <pageLast>34776</pageLast>
    <pageNumber/>
    <edition/>
    <issue>288</issue>
    <volume/>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2014-08-21</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Structural basis of substrate conversion in a new aromatic peroxygenase: cytochrome P450 functionality with benefits</title>
    <abstract language="eng">Aromatic peroxygenases (APOs) represent a unique oxidoreductase sub-subclass of heme proteins with peroxygenase and peroxidase activity and were thus recently assigned a distinct EC classification (EC 1.11.2.1). They catalyze, inter alia, oxyfunctionalization reactions of aromatic and aliphatic hydrocarbons with remarkable regio- and stereoselectivities. When compared with cytochrome P450, APOs appear to be the choice enzymes for oxyfunctionalizations in organic synthesis due to their independence from a cellular environment and their greater chemical versatility. Here, the first two crystal structures of a heavily glycosylated fungal aromatic peroxygenase (AaeAPO) are described. They reveal different pH-dependent ligand binding modes. We model the fitting of various substrates in AaeAPO, illustrating the way the enzyme oxygenates polycyclic aromatic hydrocarbons. Spatial restrictions by a phenylalanine pentad in the active-site environment govern substrate specificity in AaeAPO.</abstract>
    <parentTitle language="eng">The Journal of Biological Chemistry</parentTitle>
    <identifier type="doi">10.1074/jbc.M113.514521</identifier>
    <identifier type="issn">1083-351X</identifier>
    <enrichment key="BTU">an der BTU erstellt / created at BTU</enrichment>
    <author>
      <firstName>Klaus</firstName>
      <lastName>Piontek</lastName>
    </author>
    <submitter>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </submitter>
    <author>
      <firstName>Eric</firstName>
      <lastName>Strittmatter</lastName>
    </author>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </author>
    <author>
      <firstName>Marek J.</firstName>
      <lastName>Pecyna</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Kluge</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <author>
      <firstName>Dietmar A.</firstName>
      <lastName>Plattner</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Cytochrome P450</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Fungi; Glycoprotein</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Oxyfunctionalization</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Polycyclic Aromatic Hydrocarbons</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>11642</id>
    <completedYear/>
    <publishedYear>2012</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>405</pageFirst>
    <pageLast>412</pageLast>
    <pageNumber/>
    <edition/>
    <issue>1</issue>
    <volume>402</volume>
    <type>articler</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2014-08-21</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">The aromatic peroxygenase from Marasmius rutola—a new enzyme for biosensor applications</title>
    <abstract language="eng">The aromatic peroxygenase (APO; EC 1.11.2.1) from the agraric basidomycete Marasmius rotula (MroAPO) immobilized at the chitosan-capped gold-nanoparticle-modified glassy carbon electrode displayed a pair of redox peaks with a midpoint potential of −278.5 mV vs. AgCl/AgCl (1 M KCl) for the Fe2+/Fe3+ redox couple of the heme-thiolate-containing protein. MroAPO oxidizes aromatic substrates such as aniline, p-aminophenol, hydroquinone, resorcinol, catechol, and paracetamol by means of hydrogen peroxide. The substrate spectrum overlaps with those of cytochrome P450s and plant peroxidases which are relevant in environmental analysis and drug monitoring. In M. rotula peroxygenase-based enzyme electrodes, the signal is generated by the reduction of electrode-active reaction products (e.g., p-benzoquinone and p-quinoneimine) with electro-enzymatic recycling of the analyte. In these enzyme electrodes, the signal reflects the conversion of all substrates thus representing an overall parameter in complex media. The performance of these sensors and their further development are discussed.</abstract>
    <parentTitle language="eng">Analytical and Bioanalytical Chemistry</parentTitle>
    <identifier type="doi">10.1007/s00216-011-5497-y</identifier>
    <identifier type="url">http://link.springer.com/article/10.1007%2Fs00216-011-5497-y</identifier>
    <identifier type="issn">1618-2650</identifier>
    <enrichment key="BTU">nicht an der BTU erstellt / not created at BTU</enrichment>
    <author>
      <firstName>Aysu</firstName>
      <lastName>Yarman</lastName>
    </author>
    <submitter>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </submitter>
    <author>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </author>
    <author>
      <firstName>Bettina</firstName>
      <lastName>Neumann</lastName>
    </author>
    <author>
      <firstName>Mathias</firstName>
      <lastName>Kinne</lastName>
    </author>
    <author>
      <firstName>Nenad</firstName>
      <lastName>Gajovic-Eichelmann</lastName>
    </author>
    <author>
      <firstName>Ulla</firstName>
      <lastName>Wollenberger</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>Frieder W.</firstName>
      <lastName>Scheller</lastName>
    </author>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Unspecific peroxygenase</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Biosensors</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Cytochrome P450</value>
    </subject>
    <subject>
      <language>eng</language>
      <type>uncontrolled</type>
      <value>Phenolic substances</value>
    </subject>
    <collection role="old_institute" number="06010">Prof. Enzymtechnologie</collection>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
  <doc>
    <id>11722</id>
    <completedYear/>
    <publishedYear>2014</publishedYear>
    <thesisYearAccepted/>
    <language>deu</language>
    <pageFirst/>
    <pageLast/>
    <pageNumber/>
    <edition/>
    <issue/>
    <volume/>
    <type>patent</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>2014-09-26</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="deu">Verfahren zur Deacylierung von Corticoiden</title>
    <enrichment key="Patentnr">AKZ 10 2014 005 371.7</enrichment>
    <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>Katrin</firstName>
      <lastName>Scheibner</lastName>
    </author>
    <author>
      <firstName>Glenn</firstName>
      <lastName>Gröbe</lastName>
    </author>
    <author>
      <firstName>Jan</firstName>
      <lastName>Kiebist</lastName>
    </author>
    <author>
      <firstName>Manfred</firstName>
      <lastName>Grün</lastName>
    </author>
    <author>
      <firstName>René</firstName>
      <lastName>Ullrich</lastName>
    </author>
    <author>
      <firstName>Martin</firstName>
      <lastName>Hofrichter</lastName>
    </author>
    <collection role="institutes" number="2111">FG Enzymtechnologie</collection>
  </doc>
</export-example>
