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Rational Design of Synergistic Structure Between Single-Atoms and Nanoparticles for CO₂ Hydrogenation to Formate Under Ambient Conditions.

ABSTRACT: Single-atom catalysts (SACs) as the new frontier in heterogeneous catalysis have attracted increasing attention. However, the rational design of SACs with high catalytic activities for specified reactions still remains challenging. Herein, we report the rational design of a Pd₁-Pd_NPs synergistic structure on 2,6-pyridinedicarbonitrile-derived covalent triazine framework (CTF) as an efficient active site for CO₂ hydrogenation to formate under ambient conditions. Compared with the catalysts mainly comprising Pd₁ and Pd_NPs, this hybrid catalyst presented significantly improved catalytic activity. By regulating the ratio of Pd₁ to Pd_NPs, we obtained the optimal catalytic activity with a formate formation rate of 3.66 mol_HCOOM·mol_Pd ^-1·h^-1 under ambient conditions (30°C, 0.1 MPa). Moreover, as a heterogeneous catalyst, this hybrid catalyst is easily recovered and exhibits about a 20% decrease in the catalytic activity after five cycles. These findings are significant in elucidating new rational design principles for CO₂ hydrogenation catalysts with superior activity and may open up the possibilities of converting CO₂ under ambient conditions.

SUBMITTER: Zhai S

PROVIDER: S-EPMC9343707 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature

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Rational Design of Synergistic Structure Between Single-Atoms and Nanoparticles for CO2 Hydrogenation to Formate Under Ambient Conditions.

Zhai Shengliang S Zhang Ling L Sun Jikai J Sun Lei L Jiang Shuchao S Yu Tie T Zhai Dong D Liu Chengcheng C Li Zhen Z Ren Guoqing G

Frontiers in chemistry 20220719

Single-atom catalysts (SACs) as the new frontier in heterogeneous catalysis have attracted increasing attention. However, the rational design of SACs with high catalytic activities for specified reactions still remains challenging. Herein, we report the rational design of a Pd1-PdNPs synergistic structure on 2,6-pyridinedicarbonitrile-derived covalent triazine framework (CTF) as an efficient active site for CO2 hydrogenation to formate under ambient ...[more]

PMID: 35928210

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Project description:BackgroundReplacing fossil fuels as energy carrier requires alternatives that combine sustainable production, high volumetric energy density, easy and fast refueling for mobile applications, and preferably low risk of hazard. Molecular hydrogen (H2) has been considered as promising alternative; however, practical application is struggling because of the low volumetric energy density and the explosion hazard when stored in large amounts. One way to overcome these limitations is the transient conversion of H2 into other chemicals with increased volumetric energy density and lower risk hazard, for example so-called liquid organic hydrogen carriers such as formic acid/formate that is obtained by hydrogenation of CO2. Many homogenous and heterogenous chemical catalysts have been described in the past years, however, often requiring high pressures and temperatures. Recently, the first biocatalyst for this reaction has been described opening the route to a biotechnological alternative for this conversion.ResultsThe hydrogen-dependent CO2 reductase (HDCR) is a highly active biocatalyst for storing H2 in the form of formic acid/formate by reversibly catalyzing the hydrogenation of CO2. We report the identification, isolation, and characterization of the first thermostable HDCR operating at temperatures up to 70 °C. The enzyme was isolated from the thermophilic acetogenic bacterium Thermoanaerobacter kivui and displays exceptionally high activities in both reaction directions, substantially exceeding known chemical catalysts. CO2 hydrogenation is catalyzed at mild conditions with a turnover frequency of 9,556,000 h-1 (specific activity of 900 µmol formate min-1 mg-1) and the reverse reaction, H2 + CO2 release from formate, is catalyzed with a turnover frequency of 9,892,000 h-1 (930 µmol H2 min-1 mg-1). The HDCR of T. kivui consists of a [FeFe] hydrogenase subunit putatively coupled to a tungsten-dependent CO2 reductase/formate dehydrogenase subunit by an array of iron-sulfur clusters.ConclusionsThe discovery of the first thermostable HDCR provides a promising biological alternative for a chemically challenging reaction and might serve as model for the better understanding of catalysts able to efficiently reduce CO2. The catalytic activity for reversible CO2 hydrogenation of this enzyme is the highest activity known for bio- and chemical catalysts and requiring only ambient temperatures and pressures. The thermostability provides more flexibility regarding the process parameters for a biotechnological application.

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Rational Design of Synergistic Structure Between Single-Atoms and Nanoparticles for CO₂ Hydrogenation to Formate Under Ambient Conditions.

Publications

Rational Design of Synergistic Structure Between Single-Atoms and Nanoparticles for CO<sub>2</sub> Hydrogenation to Formate Under Ambient Conditions.

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