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Enzyme Mimetic Active Intermediates for Nitrate Reduction in Neutral Aqueous Media
Author(s) -
Li Yamei,
Go Yoo Kyung,
Ooka Hideshi,
He Daoping,
Jin Fangming,
Kim Sun Hee,
Nakamura Ryuhei
Publication year - 2020
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.202002647
Subject(s) - chemistry , catalysis , redox , potentiometric titration , nitrate reductase , nitrate , aqueous solution , active site , combinatorial chemistry , titration , inorganic chemistry , enzyme , molybdenum , organic chemistry , ion
Nitrate is a pervasive aquatic contaminant of global environmental concern. In nature, the most effective nitrate reduction reaction (NRR) is catalyzed by nitrate reductase enzymes at neutral pH, using a highly‐conserved Mo center ligated mainly by oxo and thiolate groups. Mo‐based NRR catalysts mostly function in organic solvents with a low water stability. Recently, an oxo‐containing molybdenum sulfide nanoparticle that serves as an NRR catalyst at neutral pH was first reported. Herein, in a nanoparticle‐catalyzed NRR system a pentavalent Mo V (=O)S 4 species, an enzyme mimetic, served as an active intermediate for the NRR. Potentiometric titration analysis revealed that a redox synergy among Mo V −S, S radicals, and Mo V (=O)S 4 likely play a key role in stabilizing Mo V (=O)S 4 , showing the importance of secondary interactions in facilitating NRR. The first identification and characterization of an oxo‐ and thiolate‐ligated Mo intermediates pave the way to the molecular design of efficient enzyme mimetic NRR catalysts in aqueous solution.