N,O-C Nanocage-mediated high-efficient hydrogen evolution reaction on IrNi@N,O-C electrocatalyst
Development of high-performance and stable electrocatalysts for hydrogen evolution reaction (HER) is crucial for hydrogen economy. Inspired by hydrogen evolution behavior on hydrogenase enzyme, in which the azadithiolate bridging ligand of active center facilitates fast proton shuttling and catalyti...
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Published in | Applied catalysis. B, Environmental Vol. 304; p. 120996 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
01.05.2022
Elsevier BV |
Subjects | |
Online Access | Get full text |
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Summary: | Development of high-performance and stable electrocatalysts for hydrogen evolution reaction (HER) is crucial for hydrogen economy. Inspired by hydrogen evolution behavior on hydrogenase enzyme, in which the azadithiolate bridging ligand of active center facilitates fast proton shuttling and catalytic turnover, here we present an efficient approach to enhance both HER kinetics and stability realizing on an IrNi@N,O-C catalyst with individual IrNi nanoparticle separately confined in N and O co-doped carbon (N,O-C) nanocage. Experimental and theoretical investigations indicate that the N,O-C nanocage provides proton-adsorbing functionality on raising H* coverage over IrNi active centers, resulting in much accelerated HER kinetics. The IrNi@N,O-C presents superior HER performances compared to all reported Ir-based catalysts, with overpotential of 22 mV at 100 mA cm−2, ultrahigh mass activity of 9.82 A mgIr−1 (−0.050 V vs. RHE) and outstanding durability of 200 h at large current density. This work affords fresh insights/strategies for design of high-performance electrocatalysts
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•The IrNi@N,O-C prepared via reactive template route features nanoreactor structure.•The IrNi@N,O-C presents record-high hydrogen evolution reaction performances.•The N,O-C nanocage-mediated HER pathway contributes to enhanced HER performances.•The HER pathway on IrNi@N,O-C is similar to that of hydrogenase enzyme. |
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ISSN: | 0926-3373 1873-3883 |
DOI: | 10.1016/j.apcatb.2021.120996 |