Redox Enzymes Used in Chiral Syntheses Coupled to Coenzyme Regeneration

Leonida, Mihaela D.

doi:10.2174/0929867013373390

Cited by 82 publications

(32 citation statements)

References 229 publications

(286 reference statements)

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“…Different electrochemical and enzymatic procedures for in vitro cofactor regeneration are available (20,21,32,52,56), but these systems are currently lacking long-term stability. As a consequence, the practical application of flavoprotein monooxygenases is virtually restricted to in vivo systems in which cofactor regeneration is mediated by the metabolism of the expression host (45,49).…”

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confidence: 99%

Identification of a Novel Self-Sufficient Styrene Monooxygenase from Rhodococcus opacus 1CP

et al. 2009

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Sequence analysis of a 9-kb genomic fragment of the actinobacterium Rhodococcus opacus 1CP led to identification of an open reading frame encoding a novel fusion protein, StyA2B, with a putative function in styrene metabolism via styrene oxide and phenylacetic acid. Gene cluster analysis indicated that the highly related fusion proteins of Nocardia farcinica IFM10152 and Arthrobacter aurescens TC1 are involved in a similar physiological process. Whereas 413 amino acids of the N terminus of StyA2B are highly similar to those of the oxygenases of two-component styrene monooxygenases (SMOs) from pseudomonads, the residual 160 amino acids of the C terminus show significant homology to the flavin reductases of these systems. Cloning and functional expression of His 10 -StyA2B revealed for the first time that the fusion protein does in fact catalyze two separate reactions. Strictly NADH-dependent reduction of flavins and highly enantioselective oxygenation of styrene to (S)-styrene oxide were shown. Inhibition studies and photometric analysis of recombinant StyA2B indicated the absence of tightly bound heme and flavin cofactors in this self-sufficient monooxygenase. StyA2B oxygenates a spectrum of aromatic compounds similar to those of two-component SMOs. However, the specific activities of the flavin-reducing and styrene-oxidizing functions of StyA2B are one to two orders of magnitude lower than those of StyA/StyB from Pseudomonas sp. strain VLB120.The incorporation of one atom of oxygen during hydroxylation, epoxidation, sulfoxidation, or Baeyer-Villiger oxidation is a common initial step of the aerobic degradation of aromatic compounds by microorganisms. In bacteria, these reactions are most frequently catalyzed by inducible flavoprotein monooxygenases (EC 1.14.13 [57]). The majority of these enzymes (socalled single-component flavoprotein monooxygenases) utilize electrons from NAD(P)H, which are transferred to a noncovalently bound flavin adenine dinucleotide (FAD) in order to activate molecular oxygen as a flavin (hydro)peroxide. Depending on the protonation of this intermediate and the type of substrate, an oxygen atom is then incorporated by nucleophilic or electrophilic attack. More recently, different twocomponent flavoprotein monooxygenases have been characterized (57). These systems cover an NAD(P)H-dependent flavin reductase in order to generate reduced flavin and an oxygenase that utilizes this cofactor for the activation of oxygen.The exquisite regio-and stereoselectivities of oxygen insertion by flavoprotein monooxygenases favor these enzymes for biocatalytic applications (23,24,33). This is especially true because chemical synthesis approaches by hetero-or homogenic catalysis often do not yield a sufficiently high enantiomeric excess for the production of pharmaceuticals and their chiral building blocks. The use of oxygen as an inexpensive nontoxic oxidant and mild reaction conditions are additional advantages with the potential for increasing the environmental sustainability of oxygenase-catalyzed bio...

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confidence: 99%

Identification of a Novel Self-Sufficient Styrene Monooxygenase from Rhodococcus opacus 1CP

et al. 2009

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“…Nafion, used to immobilize different species on electrodes is a perfluorosulfonated polyanionic ionomer [28]. It is known to immobilize species either by electrostatic binding or by simple entrapment [29]. Besides immobilizing the LiDH, Nafion has an active role in the sensor with LDH.…”

Section: Resultsmentioning

confidence: 99%

Polymeric FAD used as enzyme-friendly mediator in lactate detection

Leonida

Starczynowski

Waldman

et al. 2003

Analytical and Bioanalytical Chemistry

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We present the fabrication and properties of lactate biosensors. The novel feature is the use of polymerized flavin adenine dinucleotide (FAD) as mediator for electron transfer. The biosensors were prepared using lactate dehydrogenase (LDH), lactate oxidase (LOX), or baker's yeast (BY) immobilized at the surface of the electrode. The sensors using purified enzymes showed good sensitivity, linearity, and stability. The sensitivity of the BY electrodes was slightly lower. The advantages of this type of sensors are discussed in connection with potential applications.

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“…[21] For instance, the regeneration reaction has to be thermodynamically favorable, enzymes and reagents of the secondary reaction should be inexpensive and…”

Section: Regeneration Of Reduced Nad(p)h In Biocatalytic Oxidationsmentioning

confidence: 99%

Recent Advances in Cofactor Regeneration Systems Applied to Biocatalyzed Oxidative Processes

Rodrı́guez¹,

Lavandera²,

Gotor

2012

COC

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Abstract. Nowadays, the design of sustainable processes applicable at industrial scale is highly desirable due to environmental reasons. The use of biocatalytic reactions to carry out oxidative transformations is one of the possible strategies framed in here due to the mildness and usually high selectivities achieved with these methods. Anyway, while implementing this type of system at industrial scale several drawbacks must be overcome in order to obtain efficient setups. Historically, one of the main issues has been the cofactor-dependency of these biocatalysts to be active. Herein, we will show the state-of-the-art concerning the recent efforts developed in the design of (potentially) efficient methods to regenerate the cofactor in oxidative transformations. Thus, the more studied enzymatic methods will be discussed to highlight some recent examples dealing with the co-expression of both oxidative and recycling enzymes in one host or the development of self-sufficient biocatalysts. Furthermore, novel applications of these systems to couple two productive synthetic reactions will also be reviewed. Subsequently, we will focus on some recent examples related with the employment of electrochemical, photochemical, and chemical strategies to carry out the nicotinamide coenzyme or the flavin/heme prosthetic group regeneration. In the case of biocatalysts that use NAD(P) as electron shuttle, these systems have also been employed to replace it, allowing the design of nicotinamide-free recycling setups. In all cases, the (dis)advantages that these methodologies present will be briefly discussed.

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Redox Enzymes Used in Chiral Syntheses Coupled to Coenzyme Regeneration

Cited by 82 publications

References 229 publications

Identification of a Novel Self-Sufficient Styrene Monooxygenase from Rhodococcus opacus 1CP

Identification of a Novel Self-Sufficient Styrene Monooxygenase from Rhodococcus opacus 1CP

Polymeric FAD used as enzyme-friendly mediator in lactate detection

Recent Advances in Cofactor Regeneration Systems Applied to Biocatalyzed Oxidative Processes

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