Alternative Hydride Sources for Ene‐Reductases: Current Trends

Toogood, Helen S.; Knaus, Tanja; Scrutton, Nigel S.

doi:10.1002/cctc.201300911

Cited by 40 publications

(34 citation statements)

References 26 publications

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“…[21] Nevertheless,t he limitations identified in this contribution are the basis for further improvements,s uch as the design of CDs exhibiting enhanced efficiencies of charge separation and migration, and the structural modification of the hydride-transfer mediator to tune its redox potential. Furthermore,abroader applicability of the photobiocatalytic system was demonstrated by employing different substrates (e.g., 2-methyl-2cyclohexen-1-one, trans-cinnamaldehyde).…”

Section: Angewandte Chemiementioning

confidence: 99%

Biocatalytic C=C Bond Reduction through Carbon Nanodot‐Sensitized Regeneration of NADH Analogues

et al. 2018

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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 hydrogenation through light-driven regeneration of NADH and its analogues (mNADHs) by N-doped carbon nanodots (N-CDs), a zero-dimensional photocatalyst. Our spectroscopic and photoelectrochemical analyses verified the transfer of photo-induced electrons from N-CDs to an organometallic electron mediator (M) for highly regioselective regeneration of cofactors. Light triggered the reduction of NAD and mNAD s with the cooperation of N-CDs and M, and the reduction behaviors of cofactors were dependent on their own reduction peak potentials. The regenerated cofactors subsequently delivered hydrides to OYE for stereoselective conversions of a broad range of substrates with excellent biocatalytic efficiencies.

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Section: Angewandte Chemiementioning

confidence: 99%

Biocatalytic C=C Bond Reduction through Carbon Nanodot‐Sensitized Regeneration of NADH Analogues

et al. 2018

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“…One method is the coupling of an in situ recycling system, where NAD(P) + is continuously regenerated to NAD(P)H. Although only catalytic levels of NAD(P) + are needed, stoichiometric amounts of a cosubstrate are required to drive the recycling system to overcome thermodynamic limitations. Various systems have been adopted for ER-catalyzed biocatalytic reactions such as the (i) GDH/glucose, (ii) glucose-6-phosphate dehydrogenase/glucose-6-phosphate (G6PDH/G6P), (iii) formate dehydrogenase/formate (FDH/formate), and (iv) phosphite dehydrogenase/phosphite (PTDH/phosphite) system [54]. Unfortunately, the nature of the substrate has a high influence on the efficiency of the recycling system.…”

Section: Alternative Hydride Sourcesmentioning

confidence: 99%

Ene‐reductases and their Applications

2016

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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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Alternative Hydride Sources for Ene‐Reductases: Current Trends

Abstract: Hydride source: Commercially viable biocatalytic reductions must overcome the cost barrier of NAD(P)H requirements. Developments in overcoming the “hydride problem” are discussed in this Highlight.

Cited by 40 publications

References 26 publications

Biocatalytic C=C Bond Reduction through Carbon Nanodot‐Sensitized Regeneration of NADH Analogues

Biocatalytic C=C Bond Reduction through Carbon Nanodot‐Sensitized Regeneration of NADH Analogues

Ene‐reductases and their Applications

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

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