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

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.

SUBMITTER: Chino M 

PROVIDER: S-EPMC10130062 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature