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

Chemistry

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

M. Chino, L. F. D. Costanzo, et al.

Exciting advancements in the design of metal sites in *de novo* proteins are showcased by a team of researchers including Marco Chino, Luigi Franklin Di Costanzo, and others. Their innovative 28-residue tetra-thiolate metal-binding protein exhibits remarkable precision and high reduction potential, making it a groundbreaking component in artificial light-triggered electron chains.

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Playback language: English
Abstract
Designing metal sites into *de novo* proteins has significantly improved. This study reports the crystal structure of a designed 28-residue tetra-thiolate metal-binding protein, showing sub-Å agreement with the intended design. Its high reduction potential allows it to function as a terminal electron acceptor in a fully artificial visible-light-triggered electron chain.
Publisher
Nature Communications
Published On
Apr 25, 2023
Authors
Marco Chino, Luigi Franklin Di Costanzo, Linda Leone, Salvatore La Gatta, Antonino Famulari, Mario Chiesa, Angela Lombardi, Vincenzo Pavone
Tags
metal-binding
de novo proteins
tetra-thiolate
electron acceptor
crystal structure
visible-light
artificial systems

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