Bioinspired Approach to Multienzyme Cascade System Construction for Efficient Carbon Dioxide Reduction

Wang, Xiaoli; Li, Zheng; Shi, Jiafu; Wu, Hong; Jiang, Zhongyi; Zhang, Wenyan; Song, Xiaokai; Ai, Qinghong

doi:10.1021/cs401096c

Cited by 123 publications

(102 citation statements)

References 65 publications

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“…Several attractive materials and successful strategies have been proposed leading to the design of an arsenal of multienzyme systems for mimicking the natural metabolic pathways in vitro. Examples are the preparations of hydrogels, 15,22 hourglass shaped nanochannel reactor, 23 mesoporous silica nanoparticles, 18,24 formation of inorganic nanocrystal-protein complexes 25 and self-assembled crystals, 26 microbeads, 27,28 DNA nanostructures, 4,5,11,[29][30][31] polymersomes, 14,32 nanoparticles, 33 nanobers, 13,16,34 graphene, 9,35 and metal-organic frameworks (MOFs). 17,36,37 In contrast to other scaffolds, MOFs, which are formed by the self-assembly of metal ions and organic linkers, feature ultrahigh surface area and porosity, uniform pores with tunable sizes, surfaces with variable chemistries, and structural diversity.…”

Section: Introductionmentioning

confidence: 99%

Magnetic metal–organic frameworks as scaffolds for spatial co-location and positional assembly of multi-enzyme systems enabling enhanced cascade biocatalysis

et al. 2017

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Magnetic multi-enzyme nanosystems have been prepared via co-precipitation of enzymes and metalorganic framework HKUST-1 precursors in the presence of magnetic Fe 3 O 4 nanoparticles. The spatial co-localization of two enzymes was achieved using a layer-by-layer positional assembly strategy.Glucose oxidase (GOx) and horseradish peroxidase (HRP) were used as the model enzymes for cascade biocatalysis. By controlling the spatial positions of enzymes, three bienzyme nanosystems GOx@HRP@HKUST-1@Fe 3 O 4 , GOx-HRP@HKUST-1@Fe 3 O 4 and HRP@GOx@HKUST-1@Fe 3 O 4 were prepared in which GOx and HRP containing layers were in close proximity, either encapsulated in the HKUST-1 inner layer, or immobilized on the HKUST-1 outer shell, or randomly distributed in the two MOF layers. Their properties were characterized by transmission electron microscopy, energydispersive X-ray spectroscopy, Fourier transform infrared spectroscopy, X-ray diffraction, thermal gravimetric analysis, and zeta potential measurements. The highest activity was observed at pH ¼ 6 and a temperature of 20 C. Thanks to the favorable positioning of enzymes, the GOx@HRP@HKUST-

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Section: Introductionmentioning

confidence: 99%

Magnetic metal–organic frameworks as scaffolds for spatial co-location and positional assembly of multi-enzyme systems enabling enhanced cascade biocatalysis

et al. 2017

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“…[2][3][4][5] In this enzyme cascade, one molecule of methanol is produced at the cost of three equivalents of NADH. It is environmentally beneficial to convert CO 2 into useful biofuel by enzymatic reactions, but the high cost of stoichiometric NADH consumption makes this process impractical.…”

mentioning

confidence: 99%

“…1 It was reported that the combination of three NAD + -dependent dehydrogenases (formate dehydrogenase, formaldehyde dehydrogenase and alcohol dehydrogenase) is capable of generating methanol from CO 2 by reversing the original enzymatic reaction direction. [2][3][4][5] In this enzyme cascade, one molecule of methanol is produced at the cost of three equivalents of NADH. It is environmentally beneficial to convert CO 2 into useful biofuel by enzymatic reactions, but the high cost of stoichiometric NADH consumption makes this process impractical.…”

mentioning

confidence: 99%

Regeneration of the NADH Cofactor by a Rhodium Complex Immobilized on Multi-Walled Carbon Nanotubes

Tan

Hickey

Milton

et al. 2014

J. Electrochem. Soc.

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The regeneration of the enzymatic cofactor nicotinamide adenine dinucleotide (NADH) by rhodium-based catalysts such as [Rh(Cp * )(bpy)Cl] + (Cp * = pentamethylcyclopentadienyl, bpy = 2,2 -bipyridine) and derivatives have previously been studied extensively in solution. In this work, we report a synthetic route of a rhodium complex with a pyrene-substituted phenanthroline ligand (pyr-Rh). The immobilization of the pyr-Rh complex was accomplished on multi-walled carbon nanotubes (MWCNTs) via π-π stacking to obtain effective and durable indirect electrochemical regeneration of NADH. Cyclic voltammetry and amperometry were used to demonstrate the electrochemical activity of the surface-confined pyr-Rh complex. The loading quantity of the pyr-Rh complex was found to be 47 ± 2 nmol/mg of MWCNTs. The reusability of the electrodes modified with the pyr-Rh complex was investigated and an average turnover frequency of 3.6 ± 0.1 s −1 over ten cycles in the presence of 2 mM nicotinamide adenine dinucleotide (NAD + ) was observed. Lastly, malate dehydrogenase (MDH), a NADH-dependent enzyme, was evaluated in the presence of the immobilized pyr-Rh complex to confirm the catalyst's capability to regenerate biologically active NADH for biocatalysis. In biological systems, the cofactor nicotinamide adenine dinucleotide (NAD + ) and its reduced form (NADH) are of significance in assisting oxidoreductase enzymes to catalyze redox reactions.1 The efficient in situ regeneration of NADH from NAD + is valuable in biocatalysis due to the stoichiometric amount required for NADHdependent enzymes along with its relatively high cost.1 It was reported that the combination of three NAD + -dependent dehydrogenases (formate dehydrogenase, formaldehyde dehydrogenase and alcohol dehydrogenase) is capable of generating methanol from CO 2 by reversing the original enzymatic reaction direction. [2][3][4][5] In this enzyme cascade, one molecule of methanol is produced at the cost of three equivalents of NADH. It is environmentally beneficial to convert CO 2 into useful biofuel by enzymatic reactions, but the high cost of stoichiometric NADH consumption makes this process impractical. Therefore, a regeneration system is necessary. Galarneau and coworkers also investigated the application of this three NADH-dependent dehydrogenases cascade and the use of the enzymatic regeneration of NADH by phosphite dehydrogenase (PTDH). 6 In comparison to enzyme systems which do not incorporate a NADH regeneration system, their polyenzymatic system had a higher activity in generating methanol from carbon dioxide.6 Practical cofactor regeneration is necessary for maintaining stable concentrations of NAD + /NADH, which provides a driving force for the desired enzymatic reactions. The reduced NADH cofactor can be regenerated enzymatically, 7-9 chemically, 10 photochemically 11-13 and electrochemically. 14,15 Two methods are commonly used when electrochemically converting NAD + to NADH: direct and indirect regeneration. In the direct regeneration of NADH, the cofactor N...

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“…For example, Ober and Dave immobilized the three enzymes in silica sol-gel matrixes, confining and reducing the volume of the enzymes, in such a manner that the local concentration of reactants was enhanced [8]. Jiang followed a similar strategy, and was able to increase the yield of methanol up to 71.6% [24]. These studies also confirmed that breaking the unfavourable equilibrium by switching it to the right is a good manner to enhance the overall conversion.…”

Section: Entrymentioning

confidence: 81%

“…As a consequence, production of formaldehyde is prevented, as the second sequential reaction requires a threshold concentration of formic acid to be activated [24]. Both factors (unfavourable equilibrium rates and need of a minimum concentration threshold) make the first reaction of the sequence (the one studied here) to play a decisive role on conversion of CO2 to methanol.…”

Section: Multi-enzymatic Reaction Of Converting Co2 To Methanol In Bmmentioning

confidence: 99%

Ionic Liquids as Bifunctional Cosolvents Enhanced CO2 Conversion Catalysed by NADH-Dependent Formate Dehydrogenase

Zhang

Luo

et al. 2018

Catalysts

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Efficient CO 2 conversion by formate dehydrogenase is limited by the low CO 2 concentrations that can be reached in traditional buffers. The use of ionic liquids was proposed as a manner to increase CO 2 concentration in the reaction system. It has been found, however, that the required cofactor (NADH) heavily degraded during the enzymatic reaction and that acidity was the main reason. Acidity, indeed, resulted in reduction of the conversion of CO 2 into formic acid and contributed to overestimate the amount of formic acid produced when the progression of the reaction was followed by a decrease in NADH absorbance (method N). Stability of NADH and the mechanism of NADH degradation was investigated by UV, NMR and by DFT calculations. It was found that by selecting neutral-basic ionic liquids and by adjusting the concentration of the ionic liquid in the buffer, the concentration of NADH can be maintained in the reaction system with little loss. Conversion of CO 2 to methanol in BmimBF 4 (67.1%) was more than twice as compared with the conversion attained by the enzymatic reaction in phosphate buffer (24.3%).

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Bioinspired Approach to Multienzyme Cascade System Construction for Efficient Carbon Dioxide Reduction

Cited by 123 publications

References 65 publications

Magnetic metal–organic frameworks as scaffolds for spatial co-location and positional assembly of multi-enzyme systems enabling enhanced cascade biocatalysis

Magnetic metal–organic frameworks as scaffolds for spatial co-location and positional assembly of multi-enzyme systems enabling enhanced cascade biocatalysis

Regeneration of the NADH Cofactor by a Rhodium Complex Immobilized on Multi-Walled Carbon Nanotubes

Ionic Liquids as Bifunctional Cosolvents Enhanced CO2 Conversion Catalysed by NADH-Dependent Formate Dehydrogenase

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