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A biomimetic redox flow battery based on flavin mononucleotide.

ABSTRACT: The versatility in design of redox flow batteries makes them apt to efficiently store energy in large-scale applications at low cost. The discovery of inexpensive organic electroactive materials for use in aqueous flow battery electrolytes is highly attractive, but is thus far limited. Here we report on a flow battery using an aqueous electrolyte based on the sodium salt of flavin mononucleotide. Flavins are highly versatile electroactive molecules, which catalyse a multitude of redox reactions in biological systems. We use nicotinamide (vitamin B3) as a hydrotropic agent to enhance the water solubility of flavin mononucleotide. A redox flow battery using flavin mononucleotide negative and ferrocyanide positive electrolytes in strong base shows stable cycling performance, with over 99% capacity retention over the course of 100 cycles. We hypothesize that this is enabled due to the oxidized and reduced forms of FMN-Na being stabilized by resonance structures.

SUBMITTER: Orita A

PROVIDER: S-EPMC5078740 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature

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A biomimetic redox flow battery based on flavin mononucleotide.

Orita Akihiro A Verde Michael G MG Sakai Masanori M Meng Ying Shirley YS

Nature communications 20161021

The versatility in design of redox flow batteries makes them apt to efficiently store energy in large-scale applications at low cost. The discovery of inexpensive organic electroactive materials for use in aqueous flow battery electrolytes is highly attractive, but is thus far limited. Here we report on a flow battery using an aqueous electrolyte based on the sodium salt of flavin mononucleotide. Flavins are highly versatile electroactive molecules, which catalyse a multitude of redox reactions ...[more]

PMID: 27767026

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Project description:Soil bacteria can detoxify Cr(VI) ions by reduction. Within the last 2 decades, numerous reports of chromate reductase enzymes have been published. These reports describe catalytic reduction of chromate ions by specific enzymes. These enzymes each have sequence similarity to known redox-active flavoproteins. We investigated the enzyme NfoR from Staphylococcus aureus, which was reported to be upregulated in chromate-rich soils and to have chromate reductase activity (H. Han, Z. Ling, T. Zhou, R. Xu, et al., Sci Rep 7:15481, 2017, https://doi.org/10.1038/s41598-017-15588-y). We show that NfoR has structural similarity to known flavin mononucleotide (FMN) reductases and reduces FMN as a substrate. NfoR binds FMN with a dissociation constant of 0.4 μM. The enzyme then binds NADPH with a dissociation constant of 140 μM and reduces the flavin at a rate of 1,350 s-1 Turnover of the enzyme is apparently limited by the rate of product release that occurs, with a net rate constant of 0.45 s-1 The rate of product release limits the rate of observed chromate reduction, so the net rate of chromate reduction by NfoR is orders of magnitude lower than when this process occurs in solution. We propose that NfoR is an FMN reductase and that the criterion required to define chromate reduction as enzymatic has not been met. That NfoR expression is increased in the presence of chromate suggests that the survival adaption was to increase the net rate of chromate reduction by facile, adventitious redox processes.IMPORTANCE Chromate is a toxic by-product of multiple industrial processes. Chromate reduction is an important biological activity that ameliorates Cr(VI) toxicity. Numerous researchers have identified chromate reductase activity by observing chromate reduction. However, all identified chromate reductase enzymes have flavin as a cofactor or use a flavin as a substrate. We show here that NfoR, an enzyme claimed to be a chromate reductase, is in fact an FMN reductase. In addition, we show that reduction of a flavin is a viable way to transfer electrons to chromate but that it is unlikely to be the native function of enzymes. We propose that upregulation of a redox-active flavoprotein is a viable means to detoxify chromate that relies on adventitious reduction that is not catalyzed.

Project description:The surface properties of porous carbonaceous electrodes govern the performance, durability, and ultimately the cost of redox flow batteries (RFBs). State-of-the-art carbon fiber-based electrode interfaces suffer from limited kinetic activity and incomplete wettability, fundamentally limiting the performance. Surface treatments for electrodes such as thermal and acid activation are a common practice to make them more suitable for aqueous RFBs; however, these treatments offer limited control over the desired functional properties. Here, we propose, for the first time, electrografting as a facile, rapid, and versatile technique to enable task-specific functionalization of porous carbonaceous electrodes for use in RFBs. Electrografting allows covalent attachment of organic molecules on conductive substrates upon application of an electrochemical driving force, and the vast library of available organic molecules can unlock a broad range of desired functional properties. To showcase the potential of electrografting for RFBs, we elect to investigate taurine, an amine with a highly hydrophilic sulfonic acid tail. Oxidative electrografting with cyclic voltammetry allows covalent attachment of taurine through the amine group to the fiber surface, resulting in taurine-functionalized carbon cloth electrodes. In situ polarization and impedance spectroscopy in single-electrolyte flow cells reveal that taurine-treated cloth electrodes result in 40% lower charge transfer and 25% lower mass transfer resistances than off-the-shelf cloth electrodes. We find that taurine-treated electrode interfaces promote faster Fe3+ reduction reaction kinetics as the electrochemical surface area normalized current densities are 2-fold and 4-fold higher than oxidized and untreated glassy carbon surfaces, respectively. Improved mass transfer of taurine-treated electrodes is attributed to their superior wettability, as revealed by operando neutron radiography within a flow cell setup. Through demonstrating promising results for aqueous systems with the model molecule taurine, this work aims to bring forth electrografting as a facile technique to tailor electrode surfaces for other RFB chemistries and electrochemical technologies.

Dataset Information

A biomimetic redox flow battery based on flavin mononucleotide.

Publications

A biomimetic redox flow battery based on flavin mononucleotide.

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