Stabilizing hydroperoxyflavin intermediate formation via a peptide appendage: a neutral flavoenzyme model.
Org Biomol Chem
; 21(16): 3311-3316, 2023 04 26.
Article
em En
| MEDLINE
| ID: mdl-37000611
ABSTRACT
A bioinspired mimic for the stabilization of hydroperoxyflavin intermediate formation was designed and investigated for monooxygenase like catalytic properties. A suitable peptide appendage was covalently linked to the C7-position of the neutral isoalloxazine core to synthesize Fl-G, Fl-F, Fl-P, and Fl-ßA analogues. While the presence and identity of the peptide appendage were found to be crucial for catalytic efficiency, corroborative observations were made from theoretical studies as well, supporting the precise conformational and accessibility requirements for the stabilization of the key hydroperoxyflavin intermediate. A simple yet elegant flavopeptide model (Fl-G) was found to achieve almost quantitative catalytic efficiency compared to the control flavin analogue without a peptide appendage.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Oxigenases de Função Mista
Idioma:
En
Ano de publicação:
2023
Tipo de documento:
Article