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Pt-O bond as an active site superior to Pt0 in hydrogen evolution reaction.

ABSTRACT: The oxidized platinum (Pt) can exhibit better electrocatalytic activity than metallic Pt0 in the hydrogen evolution reaction (HER), which has aroused great interest in exploring the role of oxygen in Pt-based catalysts. Herein, we select two structurally well-defined polyoxometalates Na5[H3Pt(IV)W6O24] (PtW6O24) and Na3K5[Pt(II)2(W5O18)2] (Pt2(W5O18)2) as the platinum oxide model to investigate the HER performance. Electrocatalytic experiments show the mass activities of PtW6O24/C and Pt2(W5O18)2/C are 20.175?A?mg-1 and 10.976?A?mg-1 at 77?mV, respectively, which are better than that of commercial 20% Pt/C (0.398?A?mg-1). The in situ synchrotron radiation experiments and DFT calculations suggest that the elongated Pt-O bond acts as the active site during the HER process, which can accelerate the coupling of proton and electron and the rapid release of H2. This work complements the knowledge boundary of Pt-based electrocatalytic HER, and suggests another way to update the state-of-the-art electrocatalyst.

SUBMITTER: Yu FY

PROVIDER: S-EPMC6981163 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature

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Pt-O bond as an active site superior to Pt0 in hydrogen evolution reaction.

Yu Fei-Yang FY Lang Zhong-Ling ZL Yin Li-Ying LY Feng Kun K Xia Yu-Jian YJ Tan Hua-Qiao HQ Zhu Hao-Tian HT Zhong Jun J Kang Zhen-Hui ZH Li Yang-Guang YG

Nature communications 20200124 1

The oxidized platinum (Pt) can exhibit better electrocatalytic activity than metallic Pt0 in the hydrogen evolution reaction (HER), which has aroused great interest in exploring the role of oxygen in Pt-based catalysts. Herein, we select two structurally well-defined polyoxometalates Na5[H3Pt(IV)W6O24] (PtW6O24) and Na3K5[Pt(II)2(W5O18)2</ ...[more]

PMID: 31980657

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Project description:Computational studies are performed to analyze the physical properties of hydrogen bonds donated by Tyr16 and Asp103 to a series of substituted phenolate inhibitors bound in the active site of ketosteroid isomerase (KSI). As the solution pK(a) of the phenolate increases, these hydrogen bond distances decrease, the associated nuclear magnetic resonance (NMR) chemical shifts increase, and the fraction of protonated inhibitor increases, in agreement with prior experiments. The quantum mechanical/molecular mechanical calculations provide insight into the electronic inductive effects along the hydrogen bonding network that includes Tyr16, Tyr57, and Tyr32, as well as insight into hydrogen bond coupling in the active site. The calculations predict that the most-downfield NMR chemical shift observed experimentally corresponds to the Tyr16-phenolate hydrogen bond and that Tyr16 is the proton donor when a bound naphtholate inhibitor is observed to be protonated in electronic absorption experiments. According to these calculations, the electronic inductive effects along the hydrogen bonding network of tyrosines cause the Tyr16 hydroxyl to be more acidic than the Asp103 carboxylic acid moiety, which is immersed in a relatively nonpolar environment. When one of the distal tyrosine residues in the network is mutated to phenylalanine, thereby diminishing this inductive effect, the Tyr16-phenolate hydrogen bond becomes longer and the Asp103-phenolate hydrogen bond shorter, as observed in NMR experiments. Furthermore, the calculations suggest that the differences in the experimental NMR data and electronic absorption spectra for pKSI and tKSI, two homologous bacterial forms of the enzyme, are due predominantly to the third tyrosine that is present in the hydrogen bonding network of pKSI but not tKSI. These studies also provide experimentally testable predictions about the impact of mutating the distal tyrosine residues in this hydrogen bonding network on the NMR chemical shifts and electronic absorption spectra.

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Pt-O bond as an active site superior to Pt0 in hydrogen evolution reaction.

Publications

Pt-O bond as an active site superior to Pt<sup>0</sup> in hydrogen evolution reaction.

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