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Date Created Description Birthdate: ; World War I service: Theme s Nazism. Subject s. National socialism. Ngankam — K.
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Kowalczyk — Hostikka Sobczyk , Jimenez C. Current Opinion in Biotechnology , 11 6 , CODEN: CUOBE3 ; ISSN: Elsevier Science Ltd.
A review with 65 refs. The synthetic and mechanistic aspects of the use of heme peroxidases as functional mimics of the cytochrome P monooxygenases in oxygen-transfer reactions have been described.
The chloroperoxidase from Caldariomyces fumago CPO is the catalyst of choice in sulfoxidn. Other heme peroxidases were less active by orders of magnitude; protein engineering has resulted in impressive improvements but even the most active mutant was still at least an order of magnitude less active than CPO.
The "oxygen-rebound" mechanisms of oxygen transfer mediated by heme enzymes - as originally conceived - have proved to be untenable. Formate oxidase FOx from Aspergillus oryzae: one catalyst to promote H 2 O 2 -dependent biocatalytic oxidation reactions.
Tieves, Florian; Willot, Sebastien Jean-Paul; van Schie, Morten Martinus Cornelis Harald; Rauch, Marine Charlene Renee; Younes, Sabry Hamdy Hamed; Zhang, Wuyuan; Dong, JiaJia; Gomez de Santos, Patricia; Robbins, John Mick; Bommarius, Bettina; Alcalde, Miguel; Bommarius, Andreas Sebastian; Hollmann, Frank.
Angewandte Chemie, International Edition , 58 23 , CODEN: ACIEF5 ; ISSN: An increasing no. The poor robustness of most enzymes towards H2O2, however, necessitates more efficient systems for in situ H2O2 generation.
In analogy to the well-known formate dehydrogenase to promote NADH-dependent reactions, we here propose employing formate oxidase FOx to promote H2O2-dependent enzymic oxidn.
Even under non-optimized conditions, high turnover nos. FOx News: Towards Methanol-driven Biocatalytic Oxyfunctionalisation Reactions.
Willot, Sebastien J. ChemCatChem , 12 10 , CODEN: CHEMK3 ; ISSN: The novel formate oxidase from Aspergillus oryzae AoFOx is a useful catalyst to promote H2O2-dependent oxyfunctionalisation reactions.
In this contribution we exploit the substrate promiscuity of AoFOx to fully oxidise methanol and formaldehyde to CO2 and drive peroxygenase-catalyzed stereoselective oxyfunctionalisation reactions.
The highly atom efficient H2O2 generation system also enabled high catalytic turnover of the peroxygenase prodn.
Selective activation of C-H bonds by cascading photochemistry with biocatalysis. Zhang, Wuyuan; Burek, Bastien O. Angewandte Chemie, International Edition , 56 48 , CODEN: ACIEF5 ; ISSN: Selective oxyfunctionalizations of inert C-H bonds can be achieved under mild conditions by using peroxygenases.
This approach, however, suffers from the poor robustness of these enzymes in the presence of hydrogen peroxide as the stoichiometric oxidant.
Herein, we demonstrate that inorg. Peroxygenase-catalyzed oxyfunctionalization reactions promoted by the complete oxidation of methanol.
Ni, Yan; Fernandez-Fueyo, Elena; Baraibar, Alvaro Gomez; Ullrich, Rene; Hofrichter, Martin; Yanase, Hideshi; Alcalde, Miguel; van Berkel, Willem J.
Angewandte Chemie, International Edition , 55 2 , CODEN: ACIEF5 ; ISSN: 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.
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