Designed Rubredoxin miniature in a fully artificial electron chain triggered by visible light

Chino, Marco ; Di Costanzo, Luigi Franklin ; Leone, Linda ; La Gatta, Salvatore ; Famulari, Antonino (Universidad de Zaragoza) ; Chiesa, Mario ; Lombardi, Angela ; Pavone, Vincenzo

Resumen: Designing metal sites into de novo proteins has significantly improved, recently. However, identifying the minimal coordination spheres, able to encompass the necessary information for metal binding and activity, still represents a great challenge, today. Here, we test our understanding with a benchmark, nevertheless difficult, case. We assemble into a miniature 28-residue protein, the quintessential elements required to fold properly around a FeCys4 redox center, and to function efficiently in electron-transfer. This study addresses a challenge in de novo protein design, as it reports the crystal structure of a designed tetra-thiolate metal-binding protein in sub-Å agreement with the intended design. This allows us to well correlate structure to spectroscopic and electrochemical properties. Given its high reduction potential compared to natural and designed FeCys4-containing proteins, we exploit it as terminal electron acceptor of a fully artificial chain triggered by visible light.

Idioma: Inglés

DOI: 10.1038/s41467-023-37941-8

Año: 2023

Publicado en: Nature communications 14, 1 (2023), 2368 [11 pp.]
ISSN: 2041-1723

Factor impacto SCIMAGO: 4.887 - Biochemistry, Genetics and Molecular Biology (miscellaneous) (Q1) - Physics and Astronomy (miscellaneous) (Q1) - Chemistry (miscellaneous) (Q1)

Financiación: info:eu-repo/grantAgreement/EC/H2020/813209/EU/Paramagnetic Species in Catalysis Research. A Unified Approach Towards Heterogeneous, Homogeneous and Enzyme Catalysis/PARACAT

Tipo y forma: Artículo (Versión definitiva)

Área (Departamento): Área Física Materia Condensada (Dpto. Física Materia Condensa.)