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

Marco Chino, Luigi Franklin Di Costanzo, Linda Leone, Salvatore La Gatta, Antonino Famulari, Mario Chiesa, Angela Lombardi () and Vincenzo Pavone ()
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Marco Chino: University of Naples Federico II
Luigi Franklin Di Costanzo: University of Naples Federico II
Linda Leone: University of Naples Federico II
Salvatore La Gatta: University of Naples Federico II
Antonino Famulari: University of Torino
Mario Chiesa: University of Torino
Angela Lombardi: University of Naples Federico II
Vincenzo Pavone: University of Naples Federico II

Nature Communications, 2023, vol. 14, issue 1, 1-11

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-37941-8

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