Hydrogen Evolution from Aqueous Solutions Mediated by a Heterogenized [NiFe]‐Hydrogenase Model: Low pH Enables Catalysis through an Enzyme‐Relevant Mechanism | Zendy

Ahmed Md Estak | Zendy; Chattopadhyay Samir | Zendy; Wang Lianke | Zendy; Brazzolotto Deborah | Zendy; Pramanik Debajyoti | Zendy; Aldakov Dmitry | Zendy; Fize Jennifer | Zendy; Morozan Adina | Zendy; Gennari Marcello | Zendy; Duboc Carole | Zendy; Dey Abhishek | Zendy; Artero Vincent | Zendy

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Hydrogen Evolution from Aqueous Solutions Mediated by a Heterogenized [NiFe]‐Hydrogenase Model: Low pH Enables Catalysis through an Enzyme‐Relevant Mechanism

Author(s) -

Ahmed Md Estak,

Chattopadhyay Samir,

Wang Lianke,

Brazzolotto Deborah,

Pramanik Debajyoti,

Aldakov Dmitry,

Fize Jennifer,

Morozan Adina,

Gennari Marcello,

Duboc Carole,

Dey Abhishek,

Artero Vincent

Publication year - 2018

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.201808215

Subject(s) - hydrogenase , aqueous solution , catalysis , active site , chemistry , enzyme , combinatorial chemistry , enzyme catalysis , inorganic chemistry , photochemistry , organic chemistry

[NiFe]‐hydrogenase enzymes are efficient catalysts for H 2 evolution but their synthetic models have not been reported to be active under aqueous conditions so far. Here we show that a close model of the [NiFe]‐hydrogenase active site can work as a very active and stable heterogeneous H 2 evolution catalyst under mildly acidic aqueous conditions. Entry in catalysis is a Ni I Fe II complex, with electronic structure analogous to the Ni‐L state of the enzyme, corroborating the mechanism modification recently proposed for [NiFe]‐hydrogenases.

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