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.

Designed Rubredoxin miniature in a fully artificial electron chain triggered by visible light / Chino, Marco; Franklin Di Costanzo, Luigi; Leone, Linda; LA GATTA, Salvatore; Famulari, Antonino; Chiesa, Mario; Lombardi, Angelina; Pavone, Vincenzo. - In: NATURE COMMUNICATIONS. - ISSN 2041-1723. - 14:1(2023). [10.1038/s41467-023-37941-8]

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

Marco Chino
Primo
;
Luigi Franklin Di Costanzo;Linda Leone;Salvatore La Gatta;Angela Lombardi
;
Vincenzo Pavone
2023

Abstract

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.
2023
Designed Rubredoxin miniature in a fully artificial electron chain triggered by visible light / Chino, Marco; Franklin Di Costanzo, Luigi; Leone, Linda; LA GATTA, Salvatore; Famulari, Antonino; Chiesa, Mario; Lombardi, Angelina; Pavone, Vincenzo. - In: NATURE COMMUNICATIONS. - ISSN 2041-1723. - 14:1(2023). [10.1038/s41467-023-37941-8]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/919951
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