Searched for: author:"Paul, C.E."
(1 - 18 of 18)
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Kim, Jinhyun (author), Lee, Sahng Ha (author), Tieves, F. (author), Paul, C.E. (author), Hollmann, F. (author), Park, Chan Beum (author)
Nicotinamide adenine dinucleotide (NAD<sup>+</sup>) is a key redox compound in all living cells responsible for energy transduction, genomic integrity, life-span extension, and neuromodulation. Here, we report a new function of NAD<sup>+</sup> as a molecular photocatalyst in addition to the biological roles. Our spectroscopic and...
journal article 2019
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Josa-Culleré, Laia (author), Lahdenperä, Antti S.K. (author), Ribaucourt, Aubert (author), Höfler, G.T. (author), Gargiulo, S. (author), Liu, Yuan Yang (author), Paradisi, Francesca (author), Hollmann, F. (author), Paul, C.E. (author)
Redox reactions catalyzed by highly selective nicotinamide-dependent oxidoreductases are rising to prominence in industry. The cost of nicotinamide adenine dinucleotide coenzymes has led to the use of well-established elaborate regeneration systems and more recently alternative synthetic biomimetic cofactors. These biomimetics are highly...
journal article 2019
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Ismail, M.B.M. (author), Schroeder, Lea (author), Frese, Marcel (author), Kottke, Tilman (author), Hollmann, F. (author), Paul, C.E. (author), Sewald, Norbert (author)
Flavin-dependent halogenases are known to regioselectively introduce halide substituents into aromatic moieties, for example, the indole ring of tryptophan. The process requires halide salts and oxygen instead of molecular halogen in the chemical halogenation. However, the reduced cofactor flavin adenine dinucleotide (FADH<sub>2</sub>) has to...
journal article 2019
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van Schie, M.M.C.H. (author), Paul, C.E. (author), Arends, I.W.C.E. (author), Hollmann, F. (author)
Two-component-diffusible-flavomonooxygenases are versatile biocatalysts for selective epoxidation-, hydroxylation- or halogenation reactions. Their complicated molecular architecture can be simplified using photochemical regeneration of the catalytically active, reduced FADH <sub>2</sub> prosthetic group. In this contribution we provide the...
journal article 2019
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van Schie, M.M.C.H. (author), Zhang, W. (author), Tieves, F. (author), Choi, Da Som (author), Park, Chan Beum (author), Burek, Bastien O. (author), Bloh, Jonathan Z. (author), Arends, I.W.C.E. (author), Paul, C.E. (author), Alcalde, Miguel (author), Hollmann, F. (author)
Peroxygenases are very interesting catalysts for specific oxyfunctionalization chemistry. Instead of relying on complicated electron transport chains, they rely on simple hydrogen peroxide as the stoichiometric oxidant. Their poor robustness against H<sub>2</sub>O<sub>2</sub> can be addressed via in situ generation of H<sub>2</sub>O<sub>2<...
journal article 2019
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Rauch, M.C.R. (author), Tieves, F. (author), Paul, C.E. (author), Arends, I.W.C.E. (author), Alcalde, Miguel (author), Hollmann, F. (author)
Biocatalytic oxyfunctionalisation reactions are traditionally conducted in aqueous media limiting their production yield. Here we report the application of a peroxygenase in neat reaction conditions reaching product concentrations of up to 360 mM.
journal article 2019
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Gotor-Fernández, Vicente (author), Paul, C.E. (author)
Deep eutectic solvents (DES) are a class of neoteric solvents used in multiple applications amongst which biocatalytic processes. Due to its simple preparation, low cost and inherent biodegradable properties, its use as a non-volatile biocompatible co-solvent with both whole cells and isolated enzymes has displayed increased enzyme activity...
review 2019
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Guarneri, A. (author), van Berkel, Willem JH (author), Paul, C.E. (author)
Coenzymes are ubiquitous in Nature, assisting in enzyme-catalysed reactions. Several coenzymes, nicotinamides and flavins, have been known for close to a century, whereas variations of those organic molecules have more recently come to light. In general, the requirement of these coenzymes imposes certain constraints for in vitro enzyme use in...
review 2019
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Scholtissek, Anika (author), Gädke, Eric (author), Paul, C.E. (author), Westphal, Adrie H. (author), Van Berkel, Willem J.H. (author), Tischler, Dirk (author)
Class III old yellow enzymes (OYEs) contain a conserved cysteine in their active sites. To address the role of this cysteine in OYE-mediated asymmetric synthesis, we have studied the biocatalytic properties of OYERo2a from Rhodococcus opacus 1CP (WT) as well as its engineered variants C25A, C25S and C25G. OYERo2a in its redox resting state ...
journal article 2018
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van Schie, M.M.C.H. (author), Younes, S.H.H. (author), Rauch, M.C.R. (author), Pesic, M. (author), Paul, C.E. (author), Arends, I.W.C.E. (author), Hollmann, F. (author)
Deazaflavins are potentially useful redox mediators for the direct, nicotinamide-independent regeneration of oxidoreductases. Especially the O<sub>2</sub>-stability of their reduced forms have attracted significant interest for the regeneration of monooxygenases. In this contribution we further investigate the photochemical properties of...
journal article 2018
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Dong, J. (author), Fernandez Fueyo, E. (author), Hollmann, F. (author), Paul, C.E. (author), Pesic, M. (author), Schmidt, S. (author), Wang, Yonghua (author), Younes, S.H.H. (author), Zhang, W. (author)
Oxidation chemistry using enzymes is approaching maturity and practical applicability in organic synthesis. Oxidoreductases (enzymes catalysing redox reactions) enable chemists to perform highly selective and efficient transformations ranging from simple alcohol oxidations to stereoselective halogenations of non‐activated C−H bonds. For many of...
journal article 2018
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Kim, Jinhyun (author), Lee, S.H. (author), Tieves, F. (author), Choi, Da Som (author), Hollmann, F. (author), Paul, C.E. (author), Park, Chan Beum (author)
Light-driven activation of redox enzymes is an emerging route for sustainable chemical synthesis. Among redox enzymes, the family of Old Yellow Enzyme (OYE) dependent on the nicotinamide adenine dinucleotide cofactor (NADH) catalyzes the stereoselective reduction of α,β-unsaturated hydrocarbons. Here, we report OYE-catalyzed asymmetric...
journal article 2018
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Qi, Jingxian (author), Paul, C.E. (author), Hollmann, F. (author), Tischler, Dirk (author)
The oxygen-insensitive azoreductase AzoRo originating from Rhodococcus opacus 1CP was found to be most active at low pH (ca. 4) and high temperature (ca. 50 °C). AzoRo is not an efficient biocatalyst when used at low pH due to stability problems. To overcome this issue, we discovered that AzoRo accepts an alternative electron donor, 1-benzyl...
journal article 2017
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Scholtissek, Anika (author), Tischler, Dirk (author), Westphal, Adrie H. (author), van Berkel, Willem J.H. (author), Paul, C.E. (author)
Asymmetric hydrogenation of activated alkenes catalysed by ene-reductases from the old yellow enzyme family (OYEs) leading to chiral products is of potential interest for industrial processes. OYEs’ dependency on the pyridine nucleotide coenzyme can be circumvented through established artificial hydride donors such as nicotinamide coenzyme...
journal article 2017
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Lee, Sahng Ha (author), Choi, Da Som (author), Pesic, M. (author), Lee, Yang Woo (author), Paul, C.E. (author), Hollmann, F. (author), Park, Chan Beum (author)
Enoate reductases from the family of old yellow enzymes (OYEs) can catalyze stereoselective trans-hydrogenation of activated C=C bonds. Their application is limited by the necessity for a continuous supply of redox equivalents such as nicotinamide cofactors [NAD(P)H]. Visible light-driven activation of OYEs through NAD(P)H-free, direct...
journal article 2017
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Geddes, Alexander (author), Paul, C.E. (author), Hay, Sam (author), Hollmann, F. (author), Scrutton, Nigel S. (author)
Understanding the mechanisms of enzymatic hydride transfer with nicotinamide coenzyme biomimetics (NCBs) is critical to enhancing the performance of nicotinamide coenzyme-dependent biocatalysts. Here the temperature dependence of kinetic isotope effects (KIEs) for hydride transfer between "better than nature" NCBs and several ene reductase...
journal article 2016
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Paul, C.E. (author), Hollmann, F. (author)
Synthetic nicotinamide cofactors are analogues of the natural cofactors used by oxidoreductases as redox intermediates. Their ability to be fine-tuned makes these biomimetics an attractive alternative to the natural cofactors in terms of stability, reactivity, and cost. The following mini-review focuses on the current state of the art of...
journal article 2016
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Knaus, T (author), Paul, C.E. (author), Levy, CW (author), de Vries, S. (author), Mutti, FG (author), Hollmann, F. (author), Scrutton, NS (author)
The search for affordable, green biocatalytic processes is a challenge for chemicals manufacture. Redox biotransformations are potentially attractive, but they rely on<br/>unstable and expensive nicotinamide coenzymes that have prevented their widespread exploitation. Stoichiometric use of natural coenzymes is not viable economically, and the...
journal article 2016
Searched for: author:"Paul, C.E."
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