A designed heme-[4Fe-4S] metalloenzyme catalyzes sulfite reduction like the native enzyme.
Science
; 361(6407): 1098-1101, 2018 09 14.
Article
em En
| MEDLINE
| ID: mdl-30213908
ABSTRACT
Multielectron redox reactions often require multicofactor metalloenzymes to facilitate coupled electron and proton movement, but it is challenging to design artificial enzymes to catalyze these important reactions, owing to their structural and functional complexity. We report a designed heteronuclear heme-[4Fe-4S] cofactor in cytochrome c peroxidase as a structural and functional model of the enzyme sulfite reductase. The initial model exhibits spectroscopic and ligand-binding properties of the native enzyme, and sulfite reduction activity was improved-through rational tuning of the secondary sphere interactions around the [4Fe-4S] and the substrate-binding sites-to be close to that of the native enzyme. By offering insight into the requirements for a demanding six-electron, seven-proton reaction that has so far eluded synthetic catalysts, this study provides strategies for designing highly functional multicofactor artificial enzymes.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Sulfitos
/
Coenzimas
/
Citocromo-c Peroxidase
/
Biocatálise
/
Proteínas Ferro-Enxofre
Idioma:
En
Revista:
Science
Ano de publicação:
2018
Tipo de documento:
Article