Fred Höfler

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Fred HГ¶fler CLAUDIA SOLAL & BENOÎT DELBECQ "Hopetown" Video

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Gayle Jacob Murphy — Wilson NEW — Furlong WBA , Ajayi WBA , Peroxygenases catalyze a broad range of stereo selective oxyfunctionalization reactions.

However, to access their full catalytic potential, peroxygenases need a balanced provision of hydrogen peroxide to achieve high catalytic activity while minimizing oxidative inactivation.

Herein, we report an enzymic cascade process that employs methanol as a sacrificial electron donor for the reductive activation of mol.

Full oxidn. Overall we propose and demonstrate an atom-efficient and easily applicable alternative to established hydrogen peroxide generation methods, which enables the efficient use of peroxygenases for oxyfunctionalization reactions.

H2 as a fuel for flavin- and H2O2-dependent biocatalytic reactions. Al-Shameri, Ammar; Willot, Sebastien J. Chemical Communications Cambridge, United Kingdom , 56 67 , CODEN: CHCOFS ; ISSN: The sol.

Reactions were expanded to aerobic conditions to supply H2O2 for peroxygenase-catalyzed hydroxylations.

H2O2 Production at Low Overpotentials for Electroenzymatic Halogenation Reactions. Bormann, Sebastian; van Schie, Morten M.

ChemSusChem , 12 21 , CODEN: CHEMIZ ; ISSN: Various enzymes utilize hydrogen peroxide as an oxidant. Such "peroxizymes" are potentially very attractive catalysts for a broad range of oxidn.

Most peroxizymes, however, are inactivated by an excess of H2O2. The electrochem. Using conventional electrode materials, however, also necessitates significant overpotentials, thereby reducing the energy efficiency of these systems.

This study concerns a method to coat a gas-diffusion electrode with oxidized carbon nanotubes oCNTs , thereby greatly reducing the overpotential needed to perform an electroenzymic halogenation reaction.

In comparison to the unmodified electrode, with the oCNTs-modified electrode the overpotential can be reduced by approx.

Electro-enzymatic hydroxylation of ethylbenzene by the evolved unspecific peroxygenase of Agrocybe aegerita.

B: Enzym. Enzymatic halogenation of the phenolic monoterpenes thymol and carvacrol with chloroperoxidase. Getrey, Laura; Krieg, Thomas; Hollmann, Frank; Schrader, Jens; Holtmann, Dirk.

Green Chemistry , 16 3 , CODEN: GRCHFJ ; ISSN: The conversion of the phenolic monoterpenes thymol and carvacrol into antimicrobials by electro -chemoenzymic halogenation was investigated using a chloroperoxidase CPO catalyzed process.

The CPO catalyzed process enables for the first time the biotechnol. First asymmetric electroenzymatic oxidation catalyzed by a peroxidase.

Electrochemistry Communications , 6 6 , CODEN: ECCMF9 ; ISSN: Elsevier Science B. Hydrogen peroxide is generated in situ by cathodic redn.

This is the first example of an asym. The reaction was carried out on mL scale with a productivity of 30 g L-1 d Piezobiocatalysis: Ultrasound-Driven Enzymatic Oxyfunctionalization of C-H Bonds.

Yoon, Jaeho; Kim, Jinhyun; Tieves, Florian; Zhang, Wuyuan; Alcalde, Miguel; Hollmann, Frank; Park, Chan Beum.

ACS Catalysis , 10 9 , CODEN: ACCACS ; ISSN: Peroxygenases have long inspired the selective oxyfunctionalization of various aliph. This study provides a proof-of-concept of piezobiocatalysis by demonstrating peroxygenase-catalyzed oxyfunctionalization reactions fueled by piezocatalytically generated H2O2.

Bismuth oxychloride BiOCl generated H2O2 in situ via an oxygen redn. Through the simple combination of water, ultrasound, recombinant, evolved unspecific peroxygenase from Agrocybe aegerita rAaeUPO , and BiOCl, the piezobiocatalytic platform accelerated selective hydroxylation of ethylbenzene to enantiopure R phenylethanol [total turnover no.

The BiOCl-rAaeUPO couple also catalyzed other representative substrates e. Overall, the BiOCl-rAaeUPO couple serves as a mech.

Selective aerobic oxidation reactions using a combination of photocatalytic water oxidation and enzymatic oxyfunctionalizations.

Zhang, Wuyuan; Fernandez-Fueyo, Elena; Ni, Yan; van Schie, Morten; Gacs, Jenoe; Renirie, Rokus; Wever, Ron; Mutti, Francesco G.

Nature Catalysis , 1 1 , CODEN: NCAACP ; ISSN: Nature Research. Peroxygenases offer an attractive means to address challenges in selective oxyfunctionalization chem.

Despite this, their application in synthetic chem. Often atom-inefficient peroxide generation systems are required, which show little potential for large-scale implementation.

Here, we show that visible-light-driven, catalytic water oxidn. In this way, the stereoselective oxyfunctionalization of hydrocarbons can be achieved by simply using the catalytic system, water and visible light.

Plasma-Driven in Situ Production of Hydrogen Peroxide for Biocatalysis. Yayci, Abdulkadir; Baraibar, Alvaro Gomez; Krewing, Marco; Fueyo, Elena Fernandez; Hollmann, Frank; Alcalde, Miguel; Kourist, Robert; Bandow, Julia E.

ChemSusChem , 13 8 , CODEN: CHEMIZ ; ISSN: Peroxidases and peroxygenases are promising classes of enzymes for biocatalysis because of their ability to carry out one-electron oxidn.

However, industrial application is limited, as the major drawback is the sensitivity toward the required peroxide substrates.

Herein, we report a novel biocatalysis approach to circumvent this shortcoming: in situ prodn. The discharge plasma can be controlled to produce hydrogen peroxide at desired rates, yielding desired concns.

Using horseradish peroxidase, it is demonstrated that hydrogen peroxide produced by plasma treatment can drive the enzymic oxidn. As direct treatment of the reaction soln.

Hydrogen peroxide kinetics in water radiolysis. Radiation Physics and Chemistry , , CODEN: RPCHDM ; ISSN: X. Escape yields of hydrogen peroxide on the microsecond time scale are easily measured with added radical scavengers even with substantial amts.

The dose necessary to reach that limiting hydrogen peroxide concn. The addn. Proton irradiations of solns. Radiation Physics and Chemistry , 77 9 , CODEN: RPCHDM ; ISSN: X.

Argon- or air-satd. Both the exptl. While the main prodn. As a result, the presence of a dissolved species, or a change in chem.

Over a wide range of conditions, there exist quant. The steady-state concns. However, raising pH above the pKa value of the acid-base equil.

This considerably increases the time for the irradiated system to reach a steady state, and is responsible for different impacts on [H2O2] and [H2] due to radically produced O2, compared to impacts due to initially dissolved O2.

Model sensitivity anal. Further validation of the water radiolysis model, particularly at higher pHs, is also discussed.

Novel haloperoxidase from the agaric basidiomycete Agrocybe aegerita oxidizes aryl alcohols and aldehydes.

Ullrich, Rene; Nueske, Joerg; Scheibner, Katrin; Spantzel, Joerg; Hofrichter, Martin. Applied and Environmental Microbiology , 70 8 , CODEN: AEMIDF ; ISSN: American Society for Microbiology.

Agrocybe aegerita, a bark mulch- and wood-colonizing basidiomycete, was found to produce a peroxidase AaP that oxidizes aryl alcs.

The enzyme also catalyzed the oxidn. Two fractions of the enzyme, AaP I and AaP II, which had identical mol. The optimum pH for the oxidn.

The apparent Km values for ABTS, DMP, benzyl alc. The N-terminal amino acid sequences of the main AaP II spots blotted after two-dimensional gel electrophoresis were almost identical and exhibited almost no homol.

This finding is consistent with the fact that AaP halogenates monochlorodimedone, the specific substrate of CPO. The existence of haloperoxidases in basidiomycetous fungi may be of general significance for the natural formation of chlorinated org.

Tandem-yeast expression system for engineering and producing unspecific peroxygenase. Enzyme Microb. Molina-Espeja, Patricia; Ma, Su; Mate, Diana M.

Enzyme and Microbial Technology , , CODEN: EMTED2 ; ISSN: Unspecific peroxygenase UPO is a highly efficient biocatalyst with a peroxide dependent monooxygenase activity and many biotechnol.

Recently, the UPO from Agrocybe aegerita was evolved for secretion and activity in Saccharomyces cerevisiae [8]. In the current work, we describe a tandem-yeast expression system for UPO engineering and large scale prodn.

By harnessing the directed evolution process in S. While secretion levels were found similar for both yeasts in flask fermn. The P.

Thus, this tandem-yeast expression system ensures the engineering of UPOs to use them in future industrial applications as well as large scale prodn.

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