000126804 001__ 126804
000126804 005__ 20240731103342.0
000126804 0247_ $$2doi$$a10.1038/s41467-023-37941-8
000126804 0248_ $$2sideral$$a134188
000126804 037__ $$aART-2023-134188
000126804 041__ $$aeng
000126804 100__ $$aChino, Marco
000126804 245__ $$aDesigned Rubredoxin miniature in a fully artificial electron chain triggered by visible light
000126804 260__ $$c2023
000126804 5060_ $$aAccess copy available to the general public$$fUnrestricted
000126804 5203_ $$aDesigning 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.
000126804 536__ $$9info:eu-repo/grantAgreement/EC/H2020/813209/EU/Paramagnetic Species in Catalysis Research. A Unified Approach Towards Heterogeneous, Homogeneous and Enzyme Catalysis/PARACAT$$9This project has received funding from the European Union’s Horizon 2020 research and innovation program under grant agreement No H2020 813209-PARACAT
000126804 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000126804 590__ $$a14.7$$b2023
000126804 592__ $$a4.887$$b2023
000126804 591__ $$aMULTIDISCIPLINARY SCIENCES$$b8 / 134 = 0.06$$c2023$$dQ1$$eT1
000126804 593__ $$aBiochemistry, Genetics and Molecular Biology (miscellaneous)$$c2023$$dQ1
000126804 593__ $$aPhysics and Astronomy (miscellaneous)$$c2023$$dQ1
000126804 593__ $$aChemistry (miscellaneous)$$c2023$$dQ1
000126804 594__ $$a24.9$$b2023
000126804 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000126804 700__ $$aDi Costanzo, Luigi Franklin
000126804 700__ $$aLeone, Linda
000126804 700__ $$aLa Gatta, Salvatore
000126804 700__ $$0(orcid)0000-0002-5431-2371$$aFamulari, Antonino$$uUniversidad de Zaragoza
000126804 700__ $$aChiesa, Mario
000126804 700__ $$aLombardi, Angela
000126804 700__ $$aPavone, Vincenzo
000126804 7102_ $$12003$$2395$$aUniversidad de Zaragoza$$bDpto. Física Materia Condensa.$$cÁrea Física Materia Condensada
000126804 773__ $$g14, 1 (2023), 2368 [11 pp.]$$tNature communications$$x2041-1723
000126804 8564_ $$s2723317$$uhttps://zaguan.unizar.es/record/126804/files/texto_completo.pdf$$yVersión publicada
000126804 8564_ $$s2690950$$uhttps://zaguan.unizar.es/record/126804/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000126804 909CO $$ooai:zaguan.unizar.es:126804$$particulos$$pdriver
000126804 951__ $$a2024-07-31-09:50:35
000126804 980__ $$aARTICLE