Journal ArticleDOI
Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes
Valentin Köhler,Yvonne M. Wilson,Marc Dürrenberger,Diego Ghislieri,Ekaterina Churakova,Tommaso Quinto,Livia Knörr,Daniel Häussinger,Frank Hollmann,Nicholas J. Turner,Thomas R. Ward +10 more
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An artificial transfer hydrogenase, based on the incorporation of a biotinylated iridium-piano-stool complex in streptavidin, is shown to be fully compatible with a range of biocatalysts and enables the concurrent interplay with oxidative enzymes.Abstract:
Enzymatic catalysis and homogeneous catalysis offer complementary means to address synthetic challenges, both in chemistry and in biology. Despite its attractiveness, the implementation of concurrent cascade reactions that combine an organometallic catalyst with an enzyme has proven challenging because of the mutual inactivation of both catalysts. To address this, we show that incorporation of a d(6)-piano stool complex within a host protein affords an artificial transfer hydrogenase (ATHase) that is fully compatible with and complementary to natural enzymes, thus enabling efficient concurrent tandem catalysis. To illustrate the generality of the approach, the ATHase was combined with various NADH-, FAD- and haem-dependent enzymes, resulting in orthogonal redox cascades. Up to three enzymes were integrated in the cascade and combined with the ATHase with a view to achieving (i) a double stereoselective amine deracemization, (ii) a horseradish peroxidase-coupled readout of the transfer hydrogenase activity towards its genetic optimization, (iii) the formation of L-pipecolic acid from L-lysine and (iv) regeneration of NADH to promote a monooxygenase-catalysed oxyfunctionalization reaction.read more
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Artificial Metalloenzymes and Metallopeptide Catalysts for Organic Synthesis
TL;DR: The potential practical benefits of catalysts that combine these properties and a desire to understand how the structure and reactivity of metal and peptide components affect each other have driven researchers to create hybrid metal-peptide catalysts since the 1970s as mentioned in this paper.
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Transfer hydrogenation catalysis in cells as a new approach to anticancer drug design
TL;DR: It is shown that ruthenium(II) sulfonamido ethyleneamine complexes towards human ovarian cancer cells is enhanced by up to 50 × in the presence of low non-toxic doses of formate, offering a new strategy for the design of safe metal-based anticancer drugs.
Journal ArticleDOI
Cooperative asymmetric reactions combining photocatalysis and enzymatic catalysis
TL;DR: A class of cooperative chemoenzymatic reaction that combines photocatalysts that isomerize alkenes with ene-reductases that reduce carbon–carbon double bonds to generate valuable enantioenriched products and provides a general strategy for converting stereoselective enzymatic reactions into stereoconvergent ones.
Journal ArticleDOI
Multistep One-Pot Reactions Combining Biocatalysts and Chemical Catalysts for Asymmetric Synthesis
TL;DR: Some of the most successful reports in developing one-pot chemoenzymatic processes that take full advantage of the chemo-, regio-, and stereoselectivity of biocatalysts and the productivity of chemical catalysts are presented.
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Combining the 'two worlds' of chemocatalysis and biocatalysis towards multi-step one-pot processes in aqueous media.
Harald Gröger,Werner Hummel +1 more
TL;DR: This review will focus on major contributions in this field, which also underline the compatibility of these two 'worlds' of catalysis with each other as well as the industrial potential of this one-pot approach.
References
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Improvement of enzyme activity, stability and selectivity via immobilization techniques
Cesar Mateo,Jose M. Palomo,Gloria Fernández-Lorente,Jose M. Guisan,Roberto Fernandez-Lafuente +4 more
TL;DR: In all cases, enzyme engineering via immobilization techniques is perfectly compatible with other chemical or biological approaches to improve enzyme functions and the final success depend on the availability of a wide battery of immobilization protocols.
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Concurrent tandem catalysis
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Synthetic protein scaffolds provide modular control over metabolic flux
John E. Dueber,Gabriel C. Wu,G Reza Malmirchegini,G Reza Malmirchegini,Tae Seok Moon,Christopher J. Petzold,Christopher J. Petzold,Adeeti Ullal,Kristala L. J. Prather,Jay D. Keasling +9 more
TL;DR: In this article, synthetic protein scaffolds bearing interaction domains from metazoan signaling proteins were used to spatially recruit metabolic enzymes in a designable manner, and the modularity of these domains enabled them to optimize the stoichiometry of three mevalonate biosynthetic enzymes recruited to a synthetic complex.
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Understanding enzyme immobilisation
TL;DR: This tutorial review focuses on the understanding of enzyme immobilisation, which can address the issue of enzymatic instability.
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Advances in enzyme immobilisation
TL;DR: Improvements in current strategies for carrier-based immobilisation have been developed using hetero-functionalised supports that enhance the binding efficacy and stability through multipoint attachment, and promise to enhance the roles of immobilisation enzymes in industry, while opening the door for novel applications.