Functional metalloenzymes based on myoglobin and neuroglobin that exploit covalent interactions.
J Inorg Biochem
; 257: 112595, 2024 Aug.
Article
de En
| MEDLINE
| ID: mdl-38759262
ABSTRACT
Globins, such as myoglobin (Mb) and neuroglobin (Ngb), are ideal protein scaffolds for the design of functional metalloenzymes. To date, numerous approaches have been developed for enzyme design. This review presents a summary of the progress made in the design of functional metalloenzymes based on Mb and Ngb, with a focus on the exploitation of covalent interactions, including coordination bonds and covalent modifications. These include the construction of a metal-binding site, the incorporation of a non-native metal cofactor, the formation of Cys/Tyr-heme covalent links, and the design of disulfide bonds, as well as other Cys-covalent modifications. As exemplified by recent studies from our group and others, the designed metalloenzymes have potential applications in biocatalysis and bioconversions. Furthermore, we discuss the current trends in the design of functional metalloenzymes and highlight the importance of covalent interactions in the design of functional metalloenzymes.
Mots clés
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Globines
/
Neuroglobine
/
Myoglobine
/
Protéines de tissu nerveux
Limites:
Animals
/
Humans
Langue:
En
Journal:
J Inorg Biochem
Année:
2024
Type de document:
Article