C-H Bond Cleavage by Bioinspired Nonheme Metal Complexes.
Inorg Chem
; 60(18): 13759-13783, 2021 Sep 20.
Article
em En
| MEDLINE
| ID: mdl-34491738
ABSTRACT
The functionalization of C-H bonds is one of the most challenging transformations in synthetic chemistry. In biology, these processes are well-known and are achieved with a variety of metalloenzymes, many of which contain a single metal center within their active sites. The most well studied are those with Fe centers, and the emerging experimental data show that high-valent iron oxido species are the intermediates responsible for cleaving the C-H bond. This Forum Article describes the state of this field with an emphasis on nonheme Fe enzymes and current experimental results that provide insights into the properties that make these species capable of C-H bond cleavage. These parameters are also briefly considered in regard to manganese oxido complexes and Cu-containing metalloenzymes. Synthetic iron oxido complexes are discussed to highlight their utility as spectroscopic and mechanistic probes and reagents for C-H bond functionalization. Avenues for future research are also examined.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Compostos de Ferro
Idioma:
En
Revista:
Inorg Chem
Ano de publicação:
2021
Tipo de documento:
Article
País de afiliação:
Estados Unidos