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Here we report the effect of molecular crowding on long-range protein electron transfer (ET) and disentangle the specific responses of the redox site and the protein milieu. To this end, we studied two different one-electron redox proteins that share the cupredoxin fold but differ in the metal center, T1 mononuclear blue copper and binuclear CuA, and generated chimeras with hybrid properties by incorporating different T1 centers within the CuA scaffold or by swapping loops between orthologous proteins from different organisms to perturb the CuA site. The heterogeneous ET kinetics of the different proteins was studied by protein film electrochemistry at variable electronic couplings and in the presence of two different crowding agents. The results reveal a strong frictional control of the ET reactions, which for 10 Å tunnelling distances results in a 90% drop of the ET rate when viscosity is matched to that of the mitochondrial interior (ca. 55 cP) by addition of either crowding agent. The effect is ascribed to the dynamical coupling of the metal site and the milieu, which for T1 is found to be twice stronger than for CuA, and the activation energy of protein-solvent motion that is dictated by the overall scaffold. This work highlights the need of explicitly considering molecular crowding effects in protein ET. © 2018 Elsevier Ltd


Documento: Artículo
Título:The role of molecular crowding in long-range metalloprotein electron transfer: Dissection into site- and scaffold-specific contributions
Autor:Zitare, U.A.; Szuster, J.; Scocozza, M.F.; Espinoza-Cara, A.; Leguto, A.J.; Morgada, M.N.; Vila, A.J.; Murgida, D.H.
Filiación:Instituto de Química Física de los Materiales, Medio Ambiente y Energía (INQUIMAE), Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires and CONICET, Buenos Aires, 1428, Argentina
Instituto de Biología Molecular y Celular de Rosario (IBR), Departamento de Química Biológica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario and CONICET, Rosario, 2000, Argentina
Palabras clave:Electron transfer; Frictional control; Loop engineering; Metalloproteins; Molecular crowding; Activation energy; Electron transitions; Friction; Intelligent agents; Metals; Scaffolds; Scaffolds (biology); Dynamical coupling; Electron transfer; Electronic coupling; Metallo-proteins; Metalloprotein; Molecular crowding; Orthologous proteins; Redox proteins; Proteins
Página de inicio:117
Página de fin:125
Título revista:Electrochimica Acta
Título revista abreviado:Electrochim Acta


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---------- APA ----------
Zitare, U.A., Szuster, J., Scocozza, M.F., Espinoza-Cara, A., Leguto, A.J., Morgada, M.N., Vila, A.J.,..., Murgida, D.H. (2019) . The role of molecular crowding in long-range metalloprotein electron transfer: Dissection into site- and scaffold-specific contributions. Electrochimica Acta, 294, 117-125.
---------- CHICAGO ----------
Zitare, U.A., Szuster, J., Scocozza, M.F., Espinoza-Cara, A., Leguto, A.J., Morgada, M.N., et al. "The role of molecular crowding in long-range metalloprotein electron transfer: Dissection into site- and scaffold-specific contributions" . Electrochimica Acta 294 (2019) : 117-125.
---------- MLA ----------
Zitare, U.A., Szuster, J., Scocozza, M.F., Espinoza-Cara, A., Leguto, A.J., Morgada, M.N., et al. "The role of molecular crowding in long-range metalloprotein electron transfer: Dissection into site- and scaffold-specific contributions" . Electrochimica Acta, vol. 294, 2019, pp. 117-125.
---------- VANCOUVER ----------
Zitare, U.A., Szuster, J., Scocozza, M.F., Espinoza-Cara, A., Leguto, A.J., Morgada, M.N., et al. The role of molecular crowding in long-range metalloprotein electron transfer: Dissection into site- and scaffold-specific contributions. Electrochim Acta. 2019;294:117-125.