Back to Search Start Over

C-H Bond Cleavage by Bioinspired Nonheme Metal Complexes.

Authors :
Lee, Justin L
Lee, Justin L
Ross, Dolores L
Barman, Suman K
Ziller, Joseph W
Borovik, AS
Lee, Justin L
Lee, Justin L
Ross, Dolores L
Barman, Suman K
Ziller, Joseph W
Borovik, AS
Source :
Inorganic chemistry; vol 60, iss 18, 13759-13783; 0020-1669
Publication Year :
2021

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.

Details

Database :
OAIster
Journal :
Inorganic chemistry; vol 60, iss 18, 13759-13783; 0020-1669
Notes :
application/pdf, Inorganic chemistry vol 60, iss 18, 13759-13783 0020-1669
Publication Type :
Electronic Resource
Accession number :
edsoai.on1391592054
Document Type :
Electronic Resource