Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins.
J Am Chem Soc
; 139(48): 17289-17292, 2017 12 06.
Article
em En
| MEDLINE
| ID: mdl-29117678
ABSTRACT
Copper-hydroperoxido species (CuII-OOH) have been proposed to be key intermediates in biological and synthetic oxidations. Using biotin-streptavidin (Sav) technology, artificial copper proteins have been developed to stabilize a CuII-OOH complex in solution and in crystallo. Stability is achieved because the Sav host provides a local environment around the Cu-OOH that includes a network of hydrogen bonds to the hydroperoxido ligand. Systematic deletions of individual hydrogen bonds to the Cu-OOH complex were accomplished using different Sav variants and demonstrated that stability is achieved with a single hydrogen bond to the proximal O-atom of the hydroperoxido ligand changing this interaction to only include the distal O-atom produced a reactive variant that oxidized an external substrate.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peróxidos
/
Cobre
/
Metaloproteínas
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article