Light-driven biocatalytic reduction of α,β-unsaturated compounds by ene reductases employing transition metal complexes as photosensitizers

Peers, Martyn K.; Toogood, Helen S.; Heyes, Derren J.; Mansell, David; Coe, Benjamin J.; Scrutton, Nigel S.

doi:10.1039/c5cy01642h

Cited by 55 publications

(59 citation statements)

References 49 publications

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“…The initial turnover frequency (TOF) of Ts OYE was calculated to be 256.1±4.9 h −1 , which was saturated with a RB concentration at over 100 μ m . The TOF value is comparable to those of previously reported methyl viologen‐mediated, Ru‐polypyridyl‐sensitized OYE reactions 17. The apparent saturation kinetics, which levels off at higher RB concentration, indicate a Michaelis–Menten‐type behavior of Ts OYE with RB as a co‐substrate, instead of NADH.…”

supporting

confidence: 85%

“…Herein, we have demonstrated a mediator‐free, visible‐light driven activation of OYEs through direct transfer of photoinduced electrons from molecular dyes to the prosthetic flavin moiety. Previous studies for light‐driven activation of OYEs often involved Ru‐based organometallic photosensitizers or CdSe quantum dots that necessitate a redox mediator, such as toxic methyl viologen, to shuttle the electrons between photosensitizer and the enzyme 17, 25. Overcoming this limitation, we established direct photoinduced electron transfer from RB and its derivatives to OYEs by eliminating the necessity for the supply of expensive nicotinamide cofactors and its regeneration, as well as harmful electron mediators.…”

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confidence: 99%

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Cofactor‐Free, Direct Photoactivation of Enoate Reductases for the Asymmetric Reduction of C=C Bonds

et al. 2017

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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 transfer of photoexcited electrons from xanthene dyes to the prosthetic flavin moiety is reported. Spectroscopic and electrochemical analyses verified spontaneous association of rose bengal and its derivatives with OYEs. Illumination of a white light‐emitting‐diode triggered photoreduction of OYEs by xanthene dyes, which facilitated the enantioselective reduction of C=C bonds in the absence of NADH. The photoenzymatic conversion of 2‐methylcyclohexenone resulted in enantiopure (ee>99 %) (R)‐2‐methylcyclohexanone with conversion yields as high as 80–90 %. The turnover frequency was significantly affected by the substitution of halogen atoms in xanthene dyes.

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confidence: 85%

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confidence: 99%

Cofactor‐Free, Direct Photoactivation of Enoate Reductases for the Asymmetric Reduction of C=C Bonds

et al. 2017

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“…Although NADPH is the preferred physiological coenzyme for OYE, the dependency on this commercially expensive compound can be circumvented by established recycling systems with dehydrogenases [12,18,[42][43][44][45], with alternative sources of hydride [46,47], or through a nicotinamide-independent disproportionation coupling reaction [48][49][50][51]. A highly promising and elegant alternative is the use of relatively inexpensive nicotinamide coenzyme biomimetics (NCBs) [52][53][54][55][56].…”

Section: Introductionmentioning

confidence: 99%

Old Yellow Enzyme-Catalysed Asymmetric Hydrogenation: Linking Family Roots with Improved Catalysis

et al. 2017

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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 biomimetics (NCBs). Several OYEs were found to exhibit higher reduction rates with NCBs. In this review, we describe a new classification of OYEs into three main classes by phylogenetic and structural analysis of characterized OYEs. The family roots are linked with their use as chiral catalysts and their mode of action with NCBs. The link between bioinformatics (sequence analysis), biochemistry (structure-function analysis), and biocatalysis (conversion, enantioselectivity and kinetics) can enable an early classification of a putative ene-reductase and therefore the indication of the binding mode of various activated alkenes.

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“…Most recently, Ru(II) and Ir(II) complexes were successfully applied as photosensitizers for regeneration of nicotinamide adenine dinucleotide phosphate (NADPH) in OYE catalytic cycles. However, those systems required an extra sacrificial electron donor, triethanolamine [75]. Instead of coupling with oxidation enzymes, photoredox catalysts, working as hydride transfer catalysts, have also been incorporated with reductases such as alcohol dehydrogenase [72] and glucose dehydrogenase [73] to prepare chiral alcohols and L-glutamate respectively.…”

Section: Artificial Metalloenzymes For Selective Transformationsmentioning

confidence: 99%

Section: Coupling Visible-light Photoredox Catalysis With Biocatalystsmentioning

confidence: 99%

Tandem Reactions Combining Biocatalysts and Chemical Catalysts for Asymmetric Synthesis

Wang

Zhao

2016

Catalysts

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Abstract:The application of biocatalysts in the synthesis of fine chemicals and medicinal compounds has grown significantly in recent years. Particularly, there is a growing interest in the development of one-pot tandem catalytic systems combining the reactivity of a chemical catalyst with the selectivity engendered by the active site of an enzyme. Such tandem catalytic systems can achieve levels of chemo-, regio-, and stereo-selectivities that are unattainable with a small molecule catalyst. In addition, artificial metalloenzymes widen the range of reactivities and catalyzed reactions that are potentially employable. This review highlights some of the recent examples in the past three years that combined transition metal catalysis with enzymatic catalysis. This field is still in its infancy. However, with recent advances in protein engineering, catalyst synthesis, artificial metalloenzymes and supramolecular assembly, there is great potential to develop more sophisticated tandem chemoenzymatic processes for the synthesis of structurally complex chemicals.

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Light-driven biocatalytic reduction of α,β-unsaturated compounds by ene reductases employing transition metal complexes as photosensitizers

Abstract: Efficient and cost effective nicotinamide cofactor regeneration is essential for industrial-scale bio-hydrogenations employing flavin-containing biocatalysts such as the Old Yellow Enzymes.

Cited by 55 publications

References 49 publications

Cofactor‐Free, Direct Photoactivation of Enoate Reductases for the Asymmetric Reduction of C=C Bonds

Cofactor‐Free, Direct Photoactivation of Enoate Reductases for the Asymmetric Reduction of C=C Bonds

Old Yellow Enzyme-Catalysed Asymmetric Hydrogenation: Linking Family Roots with Improved Catalysis

Tandem Reactions Combining Biocatalysts and Chemical Catalysts for Asymmetric Synthesis

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