René Ullrich

ORCID: 0000-0002-9165-6341
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About
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Research Areas
  • Enzyme-mediated dye degradation
  • Metal-Catalyzed Oxygenation Mechanisms
  • Microbial Metabolism and Applications
  • Microbial bioremediation and biosurfactants
  • Biochemical and biochemical processes
  • Fungal Biology and Applications
  • Enzyme Catalysis and Immobilization
  • Microbial Natural Products and Biosynthesis
  • Pharmacogenetics and Drug Metabolism
  • Electrochemical sensors and biosensors
  • bioluminescence and chemiluminescence research
  • Oxidative Organic Chemistry Reactions
  • Mycorrhizal Fungi and Plant Interactions
  • Pesticide and Herbicide Environmental Studies
  • Biocrusts and Microbial Ecology
  • Biofuel production and bioconversion
  • Microbial Metabolic Engineering and Bioproduction
  • Chromium effects and bioremediation
  • Plant Pathogens and Fungal Diseases
  • Lignin and Wood Chemistry
  • Steroid Chemistry and Biochemistry
  • Lichen and fungal ecology
  • Catalysis for Biomass Conversion
  • Neutrophil, Myeloperoxidase and Oxidative Mechanisms
  • Plant biochemistry and biosynthesis

International University Institute
2016-2025

TU Dresden
2013-2022

Vietnam Academy of Science and Technology
2020

International University
2011

Friedrich Schiller University Jena
1999-2004

Czech Academy of Sciences, Institute of Microbiology
2004

Technische Universität Berlin
1971-1972

Johannes Gutenberg University Mainz
1965-1966

ABSTRACT Unspecific peroxygenase (UPO) represents a new type of heme-thiolate enzyme with self-sufficient mono(per)oxygenase activity and many potential applications in organic synthesis. With view to taking advantage these properties, we subjected the Agrocybe aegerita UPO1-encoding gene directed evolution Saccharomyces cerevisiae . To promote functional expression, several different signal peptides were fused mature protein, resulting products tested. Over 9,000 clones screened using an ad...

10.1128/aem.00490-14 article EN Applied and Environmental Microbiology 2014-03-29

Agrocybe aegerita, a bark mulch- and wood-colonizing basidiomycete, was found to produce peroxidase (AaP) that oxidizes aryl alcohols, such as veratryl benzyl into the corresponding aldehydes then benzoic acids. The enzyme also catalyzed oxidation of typical substrates, 2,6-dimethoxyphenol (DMP) or 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonate) (ABTS). A. aegerita production depended on concentration organic nitrogen in medium, highest levels were detected presence soybean meal. Two...

10.1128/aem.70.8.4575-4581.2004 article EN Applied and Environmental Microbiology 2004-08-01

The degradation of lignocellulose and the secretion extracellular oxidoreductases were investigated in beech-wood (Fagus sylvatica) microcosms using 11 representative fungi four different ecophysiological taxonomic groups causing: (1) classic white rot wood (e.g. Phlebia radiata), (2) 'nonspecific' Agrocybe aegerita), (3) leaf litter (Stropharia rugosoannulata) or (4) soft Xylaria polymorpha). All strong rotters produced manganese-oxidizing peroxidases as key enzymes ligninolysis (75-2200 mU...

10.1111/j.1574-6941.2011.01144.x article EN FEMS Microbiology Ecology 2011-06-01

Oxidative conversion of 5‐hydroxymethylfurfural ( HMF ) is biotechnological interest for the production renewable (lignocellulose‐based) platform chemicals, such as 2,5‐furandicarboxylic acid FDCA ). To best our knowledge, ability fungal aryl‐alcohol oxidase AAO to oxidize reported here first time, resulting in almost complete into 2,5‐formylfurancarboxylic FFCA a few hours. The reaction starts with alcohol oxidation, yielding 2,5‐diformylfuran DFF ), which rapidly converted by carbonyl most...

10.1111/febs.13177 article EN cc-by-nc-nd FEBS Journal 2014-12-15

Abstract Peroxygenases catalyze a broad range of (stereo)selective oxyfunctionalization reactions. However, to access their full catalytic potential, peroxygenases need balanced provision hydrogen peroxide achieve high activity while minimizing oxidative inactivation. Herein, we report an enzymatic cascade process that employs methanol as sacrificial electron donor for the reductive activation molecular oxygen. Full oxidation is achieved, generating three equivalents can be used completely...

10.1002/anie.201507881 article EN Angewandte Chemie International Edition 2015-11-26

Turn a light on: Enantiospecific hydroxylation of nonactivated CH bonds as well epoxidations CC are reported using novel peroxidase from Agrocybe aegerita (AaeAPO). AaeAPO represents more active and versatile alternative to the current gold standard, chloroperoxidase. H2O2 was produced in situ by photocatalytic reduction O2 simple flavin adenine mononucleotide (FMN) catalysts. Detailed facts importance specialist readers published "Supporting Information". Such documents peer-reviewed, but...

10.1002/anie.201105308 article EN Angewandte Chemie International Edition 2011-09-16

Aromatic peroxygenases (APOs) represent a unique oxidoreductase sub-subclass of heme proteins with peroxygenase and peroxidase activity were thus recently assigned distinct EC classification (EC 1.11.2.1). They catalyze, inter alia, oxyfunctionalization reactions aromatic aliphatic hydrocarbons remarkable regio- stereoselectivities. When compared cytochrome P450, APOs appear to be the choice enzymes for oxyfunctionalizations in organic synthesis due their independence from cellular...

10.1074/jbc.m113.514521 article EN cc-by Journal of Biological Chemistry 2013-10-15

Here we report on the stereoselective benzylic hydroxylation and C1–C2 epoxidation of alkylbenzenes styrene derivatives, respectively, by a heme-thiolate peroxygenase (EC 1.11.2.1) from fungus Agrocybe aegerita. Benzylic led exclusively to (R)-1-phenylalkanols. For (R)-1-phenylethanol, (R)-1-phenylpropanol (R)-1-tetralol, ee reached >99%. longer chain lengths, enantiomeric excesses (ee) total turnover numbers (TTN) decreased while number by-products, e.g. 1-phenylketones, increased....

10.1039/c1gc16173c article EN Green Chemistry 2011-12-23

The mushroom Agrocybe aegerita secretes a peroxidase (AaP) that catalyzes halogenations and hydroxylations. Phenol was brominated to 2‐ 4‐bromophenol (ratio 1:4) chlorinated lesser extent 2‐chlorophenol. purified enzyme found oxidize toluene via benzyl alcohol benzaldehyde into benzoic acid. A second fraction of hydroxylated give p ‐cresol as well o methyl‐ ‐benzoquinone. UV–Vis absorption spectrum AaP showed high similarity resting state cytochrome P450 with the Soret band at 420 nm...

10.1016/j.febslet.2005.10.014 article EN FEBS Letters 2005-10-19

Coprophilous and litter-decomposing species (26 strains) of the genus Coprinus were screened for peroxidase activities by using selective agar plate tests complex media based on soybean meal. Two species, radians C. verticillatus, found to produce peroxidases, which oxidized aryl alcohols corresponding aldehydes at pH 7 (a reaction that is typical heme-thiolate haloperoxidases). The was purified homogeneity characterized. Three fractions enzyme, CrP I, II, III, with molecular masses 43 45...

10.1128/aem.00026-07 article EN Applied and Environmental Microbiology 2007-06-30

An extracellular peroxygenase from Marasmius rotula was produced in liquid culture, chromatographically purified and partially characterized. This is the third aromatic (APO) that has been characterized detail first one can be high yields. The highest enzyme levels of about 41,000 U l-1 (corresponding to appr. 445 mg APO protein) exceeded hitherto reported more than 40-fold were detected carbon- nitrogen-rich complex media. by FPLC apparent homogeneity (SDS-PAGE) with a molecular mass 32 kDa...

10.1186/2191-0855-1-31 article EN cc-by AMB Express 2011-01-01

Many litter-decay fungi secrete heme-thiolate peroxygenases that oxidize various organic chemicals, but little is known about the role or mechanism of these enzymes. We found extracellular peroxygenase Agrocybe aegerita catalyzed H2O2-dependent cleavage environmentally significant ethers, including methyl t-butyl ether, tetrahydrofuran, and 1,4-dioxane. Experiments with tetrahydrofuran showed reaction was a two-electron oxidation generated one aldehyde group alcohol group, yielding...

10.1074/jbc.m109.040857 article EN cc-by Journal of Biological Chemistry 2009-08-28

Dye-decolorizing peroxidases (DyPs) belong to the large group of heme peroxidases. They utilize hydrogen peroxide catalyze oxidations various organic compounds. AauDyPI from Auricularia auricula-judae (fungi) was crystallized, and its crystal structure determined at 2.1 Å resolution. The mostly helical also shows a β-sheet motif typical for DyPs Cld (chlorite dismutase)-related structures includes complete polypeptide chain. At distal side molecule, flexible aspartate residue (Asp-168) plays...

10.1074/jbc.m112.400176 article EN cc-by Journal of Biological Chemistry 2012-12-13
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