The flavoprotein-catalyzed reduction of aliphatic nitro-compounds represents a biocatalytic equivalent to the Nef-reaction

Durchschein, Katharina; Silva, Bianca Ferreira da; Wallner, Silvia; Macheroux, Peter; Kroutil, Wolfgang; Glueck, Silvia M.; Faber, Kurt

doi:10.1039/b922691e

Cited by 61 publications

(68 citation statements)

References 53 publications

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“…[105] As eries of flavin-dependent reductases has been tested using NADH or NADPH as reducing agents on different primary ands econdary nitroalkanes. [106] Under these conditions,s econdary nitroalkanes gave the corresponding ketones in am aximum yield of 17%, while reactionwith 1-nitroheptane was totally ineffective. Reaction of 2-phenyl-1-nitroprop-1-ene with xenobiotic reductase B-NADH gave as am ajor product 2-phenyl-1-nitropropane in 66% yield and am odest 21% ee in favor of the S enantiomer.…”

Section: B Iocatalytic Methodsmentioning

confidence: 99%

The Nitro to Carbonyl Conversion (Nef Reaction): New Perspectives for a Classical Transformation

2015

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This review article reports new procedures and practical application of the nitro to carbonyl conversion that appeared in the literature after our\ud comprehensive report published in 2004. Beside traditional and well explored reactant systems, new procedures including the utilization of molecular oxygen and photoredox catalysis have been introduced for the Nef reaction. Of notable interest is the utilizationof the nitro to carbonyl conversion in tandem and cascade processes aimed at the preparation of hetero and carbocyclic derivatives

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Section: B Iocatalytic Methodsmentioning

confidence: 99%

The Nitro to Carbonyl Conversion (Nef Reaction): New Perspectives for a Classical Transformation

2015

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“…[26,30] Xenobiotic reductases A (XenA) and B (XenB) from Pseudomonas putida and P. fluorescens, respectively, [27] glycerol trinitrate reductase NerA from Agrobacterium radiobacter and estrogen-binding protein (EBP1) from Candida albicans were obtained as recently published. [31] General Procedure for the Bioreduction of 1a-4a…”

Section: Methodsmentioning

confidence: 99%

Asymmetric Synthesis of (R)‐3‐Hydroxy‐2‐methylpropanoate (‘Roche Ester’) and Derivatives via Biocatalytic CC‐Bond Reduction

et al. 2010

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Enoate reductases from the old yellow enzyme family were employed for the asymmetric bioreduction of methyl 2-hydroxymethylacrylate and its O-allyl, O-benzyl and O-TBDMS derivatives to furnish (R)-configurated methyl 3-hydroxy-2-methylpropionate products in up to > 99% ee Variation of the O-protective group had little influence on the stereoselectivity, but a major impact on the reaction rate.Keywords: biocatalysis; C=C-bioreduction; enoate reductase; old yellow enzyme; substrate engineeringThe asymmetric reduction of C=C bonds creates (up to) two chiral carbon centres and is thus one of the most widely employed strategies for the production of chiral materials. The biocatalytic variant, which is applicable to activated alkenes bearing an electron-withdrawing substituent is catalysed by enoate reductases [EC 1.3.1.X], [1,2] which are members of the old yellow enzyme (OYE) family.[3] Over the past few years, increasing attention has been devoted to these flavoproteins [4] in view of their substrate scope, [5] encompassing a,b-unsaturated carbonyl compounds (such as enals and enones), as well as carboxylic acids and derivatives thereof (such as esters, cyclic imides, nitriles, lactones) and nitroalkenes. As a rule of thumb, the degree of activation of the C=C-bond exerted by the electron-withdrawing effect of the activating substituent goes hand in hand with the substrate acceptance, which ensures generally fast reaction rates for enals, enones and nitroalkenes, whereas (di)carboxylic acids and esters are transformed more slowly.To illustrate the importance of this enzyme class for asymmetric synthesis, we aimed at their applicability for an industrially relevant product, that is, (R)-3-hydroxy-2-methylpropanoate, which is commonly denoted as the Roche ester. The latter is a popular chiral building block for the synthesis of vitamins (e.g., a-tocopherol [6] ), fragrance components (e.g., muscone [7] ), and antibiotics (e.g., calcimycin, [8] palinurin, [9] rapamycin, [10] 13-deoxytedanolide, [11] dictyostatin [12] ) and natural products (e.g., spiculoic acid A [13] ). Classical methods for its preparation include the diastereoselective addition of non-racemic alcohols as chiral auxiliaries, [14] the transformation of a chiral homoallylic acetate [15] or involve aldol condensation [16] and -most prominent -the transition metal-catalysed asymmetric hydrogenation of acrylate esters using Rh [17] (ee up to 99%) or Ru [18] (ee up to 94%). For the biocatalytic synthesis of the Roche ester only few examples are reported: the stereoselective oxidation of 2-methyl-1,3-propanediol by Gluconobacter and Acetobacter spp. [19] (ee up to 97%), the asymmetric reduction of ethyl 4,4-dimethoxy-3-methylcrotonate using bakers yeast [20] and the stereoseletive (formal) b-hydroxylation of isobutyric acid using Pseudomonas putida (ATCC 21244).[21] All of these biotransformations were performed using whole (fermenting) microbial cells with several enzymes being involved. Only recently, was it shown that a non-flavin NADH-dependen...

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“…[%] bic [36] conditions resulted in the formation of significant quantities of by-products. To investigate this further, we ran a largerscale biotransformation of (E)-1 a with H181A and H184T mutants, which produced a significantly higher proportion of by-products.…”

Section: Oxime and Aldehyde By-product Formationmentioning

confidence: 99%

A Site‐Saturated Mutagenesis Study of Pentaerythritol Tetranitrate Reductase Reveals that Residues 181 and 184 Influence Ligand Binding, Stereochemistry and Reactivity

et al. 2011

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We have conducted a site-specific saturation mutagenesis study of H181 and H184 of flavoprotein pentaerythritol tetranitrate reductase (PETN reductase) to probe the role of these residues in substrate binding and catalysis with a variety of α,β-unsaturated alkenes. Single mutations at these residues were sufficient to dramatically increase the enantiopurity of products formed by reduction of 2-phenyl-1-nitropropene. In addition, many mutants exhibited a switch in reactivity to predominantly catalyse nitro reduction, as opposed to CC reduction. These mutants showed an enhancement in a minor side reaction and formed 2-phenylpropanal oxime from 2-phenyl-1-nitropropene. The multiple binding conformations of hydroxy substituted nitro-olefins in PETN reductase were examined by using both structural and catalytic techniques. These compounds were found to bind in both active and inhibitory complexes; this highlights the plasticity of the active site and the ability of the H181/H184 couple to coordinate with multiple functional groups. These properties demonstrate the potential to use PETN reductase as a scaffold in the development of industrially useful biocatalysts.

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The flavoprotein-catalyzed reduction of aliphatic nitro-compounds represents a biocatalytic equivalent to the Nef-reaction

Cited by 61 publications

References 53 publications

The Nitro to Carbonyl Conversion (Nef Reaction): New Perspectives for a Classical Transformation

The Nitro to Carbonyl Conversion (Nef Reaction): New Perspectives for a Classical Transformation

Asymmetric Synthesis of (R)‐3‐Hydroxy‐2‐methylpropanoate (‘Roche Ester’) and Derivatives via Biocatalytic CC‐Bond Reduction

A Site‐Saturated Mutagenesis Study of Pentaerythritol Tetranitrate Reductase Reveals that Residues 181 and 184 Influence Ligand Binding, Stereochemistry and Reactivity

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