Catalytic Mechanisms and Active Species of Benzene Hydroxylation Reaction System Based on Fe-Based Enzyme-Mimetic Structure
Subject to the shortcomings of traditional heterogeneous materials (such as the limited controllability of the preparation process, the complex surface structures and the dynamic evolution of surface structures), many scholars have been inspired by natural enzyme systems (e.g. monooxygenases and per...
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Published in | Catalysis letters Vol. 153; no. 11; pp. 3311 - 3332 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
New York
Springer US
01.11.2023
Springer Springer Nature B.V |
Subjects | |
Online Access | Get full text |
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Summary: | Subject to the shortcomings of traditional heterogeneous materials (such as the limited controllability of the preparation process, the complex surface structures and the dynamic evolution of surface structures), many scholars have been inspired by natural enzyme systems (e.g. monooxygenases and peroxidases) to innovate the catalytic system for C–H bond activation. The structure and catalytic performance of the high-valent Fe–O intermediates in metalloenzymes have been well studied for this purpose. This review will firstly introduce the natural Fe-based metalloenzymes and synthetic Fe complexes, and briefly summarize their structures and catalytic mechanisms, especially for C–H bond activation. Then, the structural characteristics and research progress of four representative Fe-based enzyme-mimetic materials were reviewed. These Fe-based metalloenzymes with unique coordination environment active sites and their powerful catalytic ability will provide a good reference for the field of heterogeneous catalysis.
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
ISSN: | 1011-372X 1572-879X |
DOI: | 10.1007/s10562-022-04238-2 |