H2 evolution catalyzed by a FeFe-hydrogenase synthetic model covalently attached to graphite surfaces

Md Estak Ahmed; Subal Dey; Biswajit Mondal; Abhishek Dey

doi:10.1039/c7cc04281g

H₂ evolution catalyzed by a FeFe-hydrogenase synthetic model covalently attached to graphite surfaces

Md Estak Ahmed, Subal Dey, Biswajit Mondal, Abhishek Dey

Research output: Contribution to journal › Article › peer-review

32 Scopus citations

Abstract

A synthetic mimic of Fe-Fe hydrogenase (H₂ase) is reported which bears a terminal alkyne group in the ligand. Using a terminal azide bearing organic linkers, this complex could be covalently attached to various electrode surfaces (e.g. edge plane graphite, reduced graphene oxide, etc.). The electrocatalytic hydrogen evolution (HER) efficiency of these constructs is investigated and the results show that the EPG-H₂ase mimic construct is able to produce H₂ from acidic water efficiently with over 90% selectivity.

Original language	English
Pages (from-to)	8188-8191
Number of pages	4
Journal	Chemical Communications
Volume	53
Issue number	58
DOIs	https://doi.org/10.1039/c7cc04281g
State	Published - 1 Jan 2017
Externally published	Yes

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Chemistry (all)
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/c7cc04281g

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title = "H2 evolution catalyzed by a FeFe-hydrogenase synthetic model covalently attached to graphite surfaces",

abstract = "A synthetic mimic of Fe-Fe hydrogenase (H2ase) is reported which bears a terminal alkyne group in the ligand. Using a terminal azide bearing organic linkers, this complex could be covalently attached to various electrode surfaces (e.g. edge plane graphite, reduced graphene oxide, etc.). The electrocatalytic hydrogen evolution (HER) efficiency of these constructs is investigated and the results show that the EPG-H2ase mimic construct is able to produce H2 from acidic water efficiently with over 90% selectivity.",

author = "Ahmed, {Md Estak} and Subal Dey and Biswajit Mondal and Abhishek Dey",

note = "Funding Information: This research was funded by MNRE 103/180/2010-NT. E. A. acknowledges CSIR-JRF, S. D. acknowledges IACS Institute Fellow Scheme and B. M. acknowledges CSIR-SPM-SRF. The IACS XPS facility funded by DST Unit of Nano-science is gratefully acknowledged. Publisher Copyright: {\textcopyright} 2017 The Royal Society of Chemistry.",

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AU - Ahmed, Md Estak

AU - Dey, Subal

AU - Mondal, Biswajit

AU - Dey, Abhishek

N1 - Funding Information: This research was funded by MNRE 103/180/2010-NT. E. A. acknowledges CSIR-JRF, S. D. acknowledges IACS Institute Fellow Scheme and B. M. acknowledges CSIR-SPM-SRF. The IACS XPS facility funded by DST Unit of Nano-science is gratefully acknowledged. Publisher Copyright: © 2017 The Royal Society of Chemistry.

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Y1 - 2017/1/1

N2 - A synthetic mimic of Fe-Fe hydrogenase (H2ase) is reported which bears a terminal alkyne group in the ligand. Using a terminal azide bearing organic linkers, this complex could be covalently attached to various electrode surfaces (e.g. edge plane graphite, reduced graphene oxide, etc.). The electrocatalytic hydrogen evolution (HER) efficiency of these constructs is investigated and the results show that the EPG-H2ase mimic construct is able to produce H2 from acidic water efficiently with over 90% selectivity.

AB - A synthetic mimic of Fe-Fe hydrogenase (H2ase) is reported which bears a terminal alkyne group in the ligand. Using a terminal azide bearing organic linkers, this complex could be covalently attached to various electrode surfaces (e.g. edge plane graphite, reduced graphene oxide, etc.). The electrocatalytic hydrogen evolution (HER) efficiency of these constructs is investigated and the results show that the EPG-H2ase mimic construct is able to produce H2 from acidic water efficiently with over 90% selectivity.

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H₂ evolution catalyzed by a FeFe-hydrogenase synthetic model covalently attached to graphite surfaces

Abstract

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