Peroxygenase-Catalysed Epoxidation of Styrene Derivatives in Neat Reaction Media.
Ontology highlight
ABSTRACT:
SUBMITTER: Rauch MCR
PROVIDER: S-EPMC6853256 | biostudies-literature | 2019 Sep
REPOSITORIES: biostudies-literature
Publications
Peroxygenase-Catalysed Epoxidation of Styrene Derivatives in Neat Reaction Media.
Rauch Marine C R MCR Tieves Florian F Paul Caroline E CE Arends Isabel W C E IWCE Alcalde Miguel M Hollmann Frank F
ChemCatChem 20190827 18
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. ...[more]
Similar Datasets
Project description:Oxyfunctionalisation reactions in neat substrate still pose a challenge for biocatalysis. Here, we report an alginate-confined peroxygenase-CLEA to catalyse the enantioselective epoxidation of cis-β-methylstyrene in a solvent-free reaction system achieving turnover numbers of 96 000 for the biocatalyst and epoxide concentrations of 48 mM.
| S-EPMC8191455 | biostudies-literature
Project description:Limonene is one of the most abundant naturally occurring cyclic monoterpenes and has recently emerged as a sustainable alternative to petroleum-based solvents as well as a chemical platform for the production of value-added compounds. The biocatalytic epoxidation of both enantiomers of limonene was carried out in the presence of a peroxygenase-containing preparation from oat (Avena sativa) flour. Different reaction profiles were observed depending on the starting enantiomer of limonene, but in both cases the 1,2-monoepoxide was obtained as the main product with excellent diastereoselectivity. Trans-1,2-monoepoxide and cis-1,2-monoepoxide were isolated from the reaction of (R)-limonene and (S)-limonene, respectively, and the reactions were scaled-up to 0.17 M substrate concentration. The process is valuable for operational simplicity, lack of toxic metal catalysts, and cost-effectiveness of the enzymatic source. Pure stereoisomers of 1,2-monoepoxides of limonene constitute a useful starting material for biorenewable polymers, but can be also converted into other chiral derivatives by epoxide ring opening with nucleophiles. As a proof of concept, a tandem protocol for the preparation of enantiopure (1S,2S,4R)-1,2-diol from (R)-limonene and (1R,2R,4S)-1,2-diol from (S)-limonene was developed.
| S-EPMC8469233 | biostudies-literature
Project description:In this study, we developed a new bienzymatic reaction to produce enantioenriched phenylethanols. In a first step, the recombinant, unspecific peroxygenase from Agrocybe aegerita (rAaeUPO) was used to oxidise ethylbenzene and its derivatives to the corresponding ketones (prochiral intermediates) followed by enantioselective reduction into the desired (R)- or (S)-phenylethanols using the (R)-selective alcohol dehydrogenase (ADH) from Lactobacillus kefir (LkADH) or the (S)-selective ADH from Rhodococcus ruber (ADH-A). In a one-pot two-step cascade, 11 ethylbenzene derivatives were converted into the corresponding chiral alcohols at acceptable yields and often excellent enantioselectivity.
| S-EPMC9306878 | biostudies-literature
Project description:Peroxygenases are heme-dependent enzymes that use peroxide-borne oxygen to catalyze a wide range of oxyfunctionalization reactions. Herein, we report the engineering of an unusual cofactor-independent peroxygenase based on a promiscuous tautomerase that accepts different hydroperoxides (t-BuOOH and H2 O2 ) to accomplish enantiocomplementary epoxidations of various α,β-unsaturated aldehydes (citral and substituted cinnamaldehydes), providing access to both enantiomers of the corresponding α,β-epoxy-aldehydes. High conversions (up to 98 %), high enantioselectivity (up to 98 % ee), and good product yields (50-80 %) were achieved. The reactions likely proceed via a reactive enzyme-bound iminium ion intermediate, allowing tweaking of the enzyme's activity and selectivity by protein engineering. Our results underscore the potential of catalytic promiscuity for the engineering of new cofactor-independent oxidative enzymes.
| S-EPMC7317984 | biostudies-literature
Project description:Sustainable and biobased surfactants are required for a wide range of everyday applications. Key drivers are cost, activity and efficiency of production. Polycondensation is an excellent route to build surfactant chains from bio-sourced monomers, but this typically requires high processing temperatures (≥200 °C) to remove the condensate and to lower viscosity of the polymer melt. In addition, high temperatures also increase the degree of branching and cause discolouration through the degradation of sensitive co-initiators and monomers. Here we report the synthesis of novel surface-active polymers from temperature sensitive renewable building blocks such as dicarboxylic acids, polyols (d-sorbitol) and fatty acids. We demonstrate that the products have the potential to be key components in renewable surfactant design, but only if the syntheses are optimised to ensure linear chains with hydrophilic character. The choice of catalyst is key to this control and we have assessed three different approaches. Additionally, we also demonstrate that use of supercritical carbon dioxide (scCO2) can dramatically improve conversion by reducing reaction viscosity, lowering reaction temperature, and driving condensate removal. We also evaluate the performance of the new biobased surfactants, focussing upon surface tension, and critical micelle concentration.
| S-EPMC8145305 | biostudies-literature
Project description:We have presented an efficient method to access gem-difluoro-2-trifluromethyl styrene derivatives via palladium catalysis. This method features mild reaction conditions, broad substrate scope and good product yields. Moreover, gram-scale reactions demonstrated the robustness and potential of this method. Control experiments revealed that the -CF3 group was essential to the success of this transformation. Finally, the practicality of this method was successfully proven by three synthetic applications.
| S-EPMC9049850 | biostudies-literature
Project description:The styrene monooxygenase (SMO) system from Pseudomonas sp. consists of two enzymes (StyA and StyB). StyB catalyses the reduction of FAD at the expense of NADH. After the transfer of FADH2 from StyB to StyA, reaction with O2 generates FAD-OOH, which is the epoxidising agent. The wastage of redox equivalents due to partial diffusive transfer of FADH2 , the insolubility of recombinant StyB and the impossibility of expressing StyA and StyB in a 1:1 molar ratio reduce the catalytic efficiency of the natural system. Herein we present a chimeric SMO (Fus-SMO) that was obtained by genetic fusion of StyA and StyB through a flexible linker. Thanks to a combination of: 1) balanced and improved expression levels of reductase and epoxidase units, and 2) intrinsically higher specific epoxidation activity of Fus-SMO in some cases, Escherichia coli cells expressing Fus-SMO possess about 50 % higher activity for the epoxidation of styrene derivatives than E. coli cells coexpressing StyA and StyB as discrete enzymes. The epoxidation activity of purified Fus-SMO was up to three times higher than that of the two-component StyA/StyB (1:1, molar ratio) system and up to 110 times higher than that of the natural fused SMO. Determination of coupling efficiency and study of the influence of O2 pressure were also performed. Finally, Fus-SMO and formate dehydrogenase were coexpressed in E. coli and applied as a self-sufficient biocatalytic system for epoxidation on greater than 500 mg scale.
| S-EPMC5900736 | biostudies-literature
Project description:Lytic polysaccharide monooxygenases (LPMOs) are a recently discovered class of monocopper enzymes broadly distributed across the tree of life. Recent reports indicate that LPMOs can use H2O2 as an oxidant and thus carry out a novel type of peroxygenase reaction involving unprecedented copper chemistry. Here, we present a combined computational and experimental analysis of the H2O2-mediated reaction mechanism. In silico studies, based on a model of the enzyme in complex with a crystalline substrate, suggest that a network of hydrogen bonds, involving both the enzyme and the substrate, brings H2O2 into a strained reactive conformation and guides a derived hydroxyl radical toward formation of a copper-oxyl intermediate. The initial cleavage of H2O2 and subsequent hydrogen atom abstraction from chitin by the copper-oxyl intermediate are the main energy barriers. Stopped-flow fluorimetry experiments demonstrated that the priming reduction of LPMO-Cu(II) to LPMO-Cu(I) is a fast process compared to the reoxidation reactions. Using conditions resulting in single oxidative events, we found that reoxidation of LPMO-Cu(I) is 2,000-fold faster with H2O2 than with O2, the latter being several orders of magnitude slower than rates reported for other monooxygenases. The presence of substrate accelerated reoxidation by H2O2, whereas reoxidation by O2 became slower, supporting the peroxygenase paradigm. These insights into the peroxygenase nature of LPMOs will aid in the development and application of enzymatic and synthetic copper catalysts and contribute to a further understanding of the roles of LPMOs in nature, varying from biomass conversion to chitinolytic pathogenesis-defense mechanisms.
| S-EPMC6983374 | biostudies-literature
Project description:Examination of the subcellular distribution of retinoic acid 5,6-epoxidase activity in rat liver and human liver homogenates showed that there is a prominent peak of activity in a high-density fraction. A corresponding peak was also detected in rat blood and human blood. Retinoic acid 5,6-epoxidation was catalysed by human blood cells but not by human plasma, and purified human haemoglobin also catalysed the epoxidation of retinoic acid to 5,6-epoxyretinoic acid. These results suggest that retinoic acid 5,6-epoxidase activity in human liver and rat liver homogenates is partially due to the presence of residual blood cells, and particularly haemoglobin, in the homogenates. In the retinoic acid 5,6-epoxidation catalysed by human haemoglobin, molecular O2 was required and its reaction was stimulated by Triton X-100. Boiling of haemoglobin solution resulted in an 94% decrease in the activity. NADPH (1 mM) and NADH (1 mM) completely [2-mercaptoethanol (5 mM) almost completely] inhibited the 5,6-epoxidation catalysed by haemoglobin, but catalase, superoxide dismutase and mannitol showed no inhibitory effect. CN- ion (100 mM) inhibited the reaction, but N3- ion (100 mM) did not.
| S-EPMC1152902 | biostudies-other
Project description:Membrane-bound styrene oxide isomerase (SOI) catalyses the Meinwald rearrangement-a Lewis-acid-catalysed isomerization of an epoxide to a carbonyl compound-and has been used in single and cascade reactions. However, the structural information that explains its reaction mechanism has remained elusive. Here we determine cryo-electron microscopy (cryo-EM) structures of SOI bound to a single-domain antibody with and without the competitive inhibitor benzylamine, and elucidate the catalytic mechanism using electron paramagnetic resonance spectroscopy, functional assays, biophysical methods and docking experiments. We find ferric haem b bound at the subunit interface of the trimeric enzyme through H58, where Fe(III) acts as the Lewis acid by binding to the epoxide oxygen. Y103 and N64 and a hydrophobic pocket binding the oxygen of the epoxide and the aryl group, respectively, position substrates in a manner that explains the high regio-selectivity and stereo-specificity of SOI. Our findings can support extending the range of epoxide substrates and be used to potentially repurpose SOI for the catalysis of new-to-nature Fe-based chemical reactions.
| S-EPMC11374702 | biostudies-literature