Factors affecting the electrochemical regeneration of NADH by (2,2′-bipyridyl) (pentamethylcyclopentadienyl)-rhodium complexes: Impact on their immobilization onto electrode surfaces

Walcarius, Alain; Nasraoui, Rihab; Wang, Zhijie; Qu, Fengli; Urbanová, Veronika; Etienne, Mathieu; Göllü, Mehmet; Demir, Ayhan S.; Gajdzik, Janine; Hempelmann, Rolf

doi:10.1016/j.bioelechem.2011.05.002

Cited by 57 publications

(86 citation statements)

References 35 publications

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“…However, the instability of enzymes in a non‐biological environment and the high cost and consumption of cofactors greatly hinder the development of this technology. Therefore, enhancing enzymatic reactions by enzyme stabilization as well as cofactor regeneration with an economic source of energy (for example, electrochemical or photochemical) will provide a more sustainable technology to decrease atmospheric CO 2 levels …”

Section: Methodsmentioning

confidence: 99%

Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO₂

et al. 2019

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The efficient fixation of excess CO2 from the atmosphere to yield value‐added chemicals remains crucial in response to the increasing levels of carbon emission. Coupling enzymatic reactions with electrochemical regeneration of cofactors is a promising technique for fixing CO2, while producing biomass which can be further transformed into biofuels. Herein, a bioelectrocatalytic system was established by depositing crystallites of a mesoporous metal–organic framework (MOF), termed NU‐1006, containing formate dehydrogenase, on a fluorine‐doped tin oxide glass electrode modified with Cp*Rh(2,2′‐bipyridyl‐5,5′‐dicarboxylic acid)Cl2 complex. This system converts CO2 into formic acid at a rate of 79±3.4 mm h−1 with electrochemical regeneration of the nicotinamide adenine dinucleotide cofactor. The MOF–enzyme composite exhibited significantly higher catalyst stability when subjected to non‐native conditions compared to the free enzyme, doubling the formic acid yield.

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Section: Methodsmentioning

confidence: 99%

Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO₂

et al. 2019

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“…45 Ultraviolet-visible spectroscopy.-Ultraviolet-visible spectroscopy was carried out using a Thermo Scientific Evolution 260 Bio UV-Visible Spectrophotometer and disposable plastic cuvettes (1 cm path length). The experimental assays were performed in 100 mM sodium phosphate buffer (pH 7.4), which was reported to prevent NADH deactivation at room temperature (20)(21)(22)(23)(24)(25) • C). 15 NADH concentration was determined by measuring the absorbance at a wavelength of 340 nm (extinction coefficient 6220 M…”

Section: Methodsmentioning

confidence: 99%

“…The most successful catalyst [Rh(Cp * )(bpy)Cl] + described by Steckhan and co-workers has attracted much attention. 10,14,[22][23][24][25] The use of this water-soluble rhodium * Electrochemical Society Student Member. * * Electrochemical Society Fellow.…”

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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“…NAD(P)H) associated to dehydrogenase enzymes in aqueous solution [19][20][21][22]. It was pointed out that the electrocatalytic efficiency of the complex is strongly influenced by the experimental conditions such as pH, the presence of chloride ions, peptides or amino acids [19,20]. Interaction of [RhCp*(bpy)(H 2 O)] 2+ with bovine serum albumin and His, Cys, Trp and Met amino acids decreased the activity in formate-driven reduction of NAD + .…”

Section: Compounds Namely Imidazolium Trans-[tetrachlorido(dmso)(imimentioning

confidence: 99%

Comparative solution equilibrium studies on pentamethylcyclopentadienyl rhodium complexes of 2,2ʹ-bipyridine and ethylenediamine and their interaction with human serum albumin

Enyedy

Mészáros

Dömötör

et al. 2015

Journal of Inorganic Biochemistry

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Complex formation equilibrium processes of the (N,N) donor containing 2,2'-bipyridine (bpy) and ethylenediamine (en) with (η 5 -pentamethylcyclopentadienyl)rhodium(III) were investigated in aqueous solution via pH-potentiometry, 1 H NMR spectroscopy, and UV-Vis spectrophotometry in the absence and presence of chloride ions. 2+ , and formation of ternary HSA-RhCp*-ligand adducts was proved. In the case of the deferiprone complex, the RhCp* fragment is cleaved off when HSA is loaded with low equivalents of the compound.

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Factors affecting the electrochemical regeneration of NADH by (2,2′-bipyridyl) (pentamethylcyclopentadienyl)-rhodium complexes: Impact on their immobilization onto electrode surfaces

Cited by 57 publications

References 35 publications

Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO₂

Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO₂

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

Comparative solution equilibrium studies on pentamethylcyclopentadienyl rhodium complexes of 2,2ʹ-bipyridine and ethylenediamine and their interaction with human serum albumin

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Factors affecting the electrochemical regeneration of NADH by (2,2′-bipyridyl) (pentamethylcyclopentadienyl)-rhodium complexes: Impact on their immobilization onto electrode surfaces

Cited by 57 publications

References 35 publications

Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO2

Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO2

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

Comparative solution equilibrium studies on pentamethylcyclopentadienyl rhodium complexes of 2,2ʹ-bipyridine and ethylenediamine and their interaction with human serum albumin

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Product

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Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO₂

Stabilization of Formate Dehydrogenase in a Metal–Organic Framework for Bioelectrocatalytic Reduction of CO₂