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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TLDR
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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Tailoring D‐Amino Acid Oxidase from the Pig Kidney to R‐Stereoselective Amine Oxidase and its Use in the Deracemization of α‐Methylbenzylamine
TL;DR: The findings of this study indicate that further investigations on the structure-activity relationship of AOx are warranted and also provide a new method for biotransformations in organic synthesis.
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Opportunities for merging chemical and biological synthesis.
Stephen Wallace,Emily P. Balskus +1 more
TL;DR: This review will discuss approaches that combine chemical and biological synthesis for small molecule production, highlighting recent advances in combining enzymatic and non-enzymatic catalysis in vitro, and discussing the application of design principles from organic chemistry for engineering non-biological reactivity into enzymes.
Journal ArticleDOI
Positional assembly of hemin and gold nanoparticles in graphene-mesoporous silica nanohybrids for tandem catalysis.
TL;DR: A hybrid catalyst in which two different types of enzyme mimics are positioned in spatially separate domains within a graphene–mesoporous silica support is presented.
Journal ArticleDOI
An NAD(P)H-Dependent Artificial Transfer Hydrogenase for Multienzymatic Cascades.
TL;DR: It is shown that incorporation of a Cp*Ir cofactor possessing a biotin moiety and 4,7-dihydroxy-1,10-phenanthroline into streptavidin yields an NAD(P)H-dependent artificial transfer hydrogenase (ATHase), which catalyzes imine reduction and can be concurrently regenerated by a glucose dehydrogenase (GDH) using only 1.2 equiv of glucose.
Journal ArticleDOI
One-pot combination of enzyme and Pd nanoparticle catalysis for the synthesis of enantiomerically pure 1,2-amino alcohols
Joerg H. Schrittwieser,Francesca Coccia,Selin Kara,Barbara Grischek,Wolfgang Kroutil,Nicola d'Alessandro,Frank Hollmann +6 more
TL;DR: This work reports the one-pot combination of alcohol dehydrogenasecatalysed asymmetric reduction of 2-azido ketones and Pd nanoparticle-catalysed hydrogenation of the resulting azido alcohols, which gives access to both enantiomers of aromatic 1,2-amino alcohols in high yields and excellent optical purity.
References
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Cesar Mateo,Jose M. Palomo,Gloria Fernández-Lorente,Jose M. Guisan,Roberto Fernandez-Lafuente +4 more
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Concurrent tandem catalysis
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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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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.