Search Results - "Zitare, Ulises A."

Mutational and structural analysis of an ancestral fungal dye‐decolorizing peroxidase by Zitare, Ulises A., Habib, Mohamed H., Rozeboom, Henriette, Mascotti, Maria L., Todorovic, Smilja, Fraaije, Marco W.

“…Dye‐decolorizing peroxidases (DyPs) constitute a superfamily of heme‐containing peroxidases that are related neither to animal nor to plant peroxidase…”
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Dynamical effects in metalloprotein heterogeneous electron transfer by Zitare, Ulises A., Szuster, Jonathan, Santalla, María C., Morgada, Marcos N., Vila, Alejandro J., Murgida, Daniel H.

“…In this work we assess the influence of physiological viscosities on metalloprotein electron transfer reactions. To that end we investigated the direct…”
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Electrochemical characterization of an engineered red copper protein featuring an unprecedented entropic control of the reduction potential by Szuster, Jonathan, Leguto, Alcides J., Zitare, Ulises A., Rebechi, Juan P., Vila, Alejandro J., Murgida, Daniel H.

“…•Ligand loop replacement of a CuA site leads to a T2-like mononuclear copper protein.•The T2 chimera is the first Cu site with entropically controlled redox…”
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CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential by Szuster, Jonathan, Zitare, Ulises A, Castro, María A, Leguto, Alcides J, Morgada, Marcos N, Vila, Alejandro J, Murgida, Daniel H

“…Attaining rational modulation of thermodynamic and kinetic redox parameters of metalloproteins is a key milestone towards the (re)design of proteins with new…”
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The role of molecular crowding in long-range metalloprotein electron transfer: Dissection into site- and scaffold-specific contributions by Zitare, Ulises A., Szuster, Jonathan, Scocozza, Magali F., Espinoza-Cara, Andrés, Leguto, Alcides J., Morgada, Marcos N., Vila, Alejandro J., Murgida, Daniel H.

“…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…”
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Dramatic Electronic Perturbations of Cu A Centers via Subtle Geometric Changes by Leguto, Alcides J, Smith, Meghan A, Morgada, Marcos N, Zitare, Ulises A, Murgida, Daniel H, Lancaster, Kyle M, Vila, Alejandro J

“…Cu is a binuclear copper site acting as electron entry port in terminal heme-copper oxidases. In the oxidized form, Cu is a mixed valence pair whose electronic…”
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Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function by Alvarez-Paggi, Damian, Zitare, Ulises A, Szuster, Jonathan, Morgada, Marcos N, Leguto, Alcides J, Vila, Alejandro J, Murgida, Daniel H

“…Manipulation of the partition function (Q) of the redox center CuA from cytochrome c oxidase is attained by tuning the accessibility of a low lying alternative…”
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Fine Tuning of Functional Features of the CuA Site by Loop-Directed Mutagenesis by Zitare, Ulises A, Szuster, Jonathan, Santalla, María C, Llases, María E, Morgada, Marcos N, Vila, Alejandro J, Murgida, Daniel H

“…Here we report the spectroscopic and electrochemical characterization of three novel chimeric CuA proteins in which either one or the three loops surrounding…”
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Dramatic Electronic Perturbations of CuA Centers via Subtle Geometric Changes by Leguto, Alcides J, Smith, Meghan A, Morgada, Marcos N, Zitare, Ulises A, Murgida, Daniel H, Lancaster, Kyle M, Vila, Alejandro J

“…CuA is a binuclear copper site acting as electron entry port in terminal heme-copper oxidases. In the oxidized form, CuA is a mixed valence pair whose…”
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Cu-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential by Szuster, Jonathan, Zitare, Ulises A, Castro, María A, Leguto, Alcides J, Morgada, Marcos N, Vila, Alejandro J, Murgida, Daniel H

“…Attaining rational modulation of thermodynamic and kinetic redox parameters of metalloproteins is a key milestone towards the (re)design of proteins with new…”
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Fine Tuning of Functional Features of the Cu A Site by Loop-Directed Mutagenesis by Zitare, Ulises A, Szuster, Jonathan, Santalla, María C, Llases, María E, Morgada, Marcos N, Vila, Alejandro J, Murgida, Daniel H

“…Here we report the spectroscopic and electrochemical characterization of three novel chimeric Cu proteins in which either one or the three loops surrounding…”
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SAM-modified electrodes for understanding and harnessing the properties of redox proteins by Zitare, Ulises A., Szuster, Jonathan, Murgida, Daniel H.

“…This short review describes recent work on the use of SAM-coated electrodes for studying redox proteins and enzymes. These platforms, in conjunction with…”
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CuA-based chimeric T1 copper sites allow for independent modulation of reorganization energy and reduction potential† †Electronic supplementary information (ESI) available: Resonance Raman spectra, electrochemical data and computational (MDS and QM/MM) results. See DOI: 10.1039/d0sc01620a by Szuster, Jonathan, Zitare, Ulises A., Castro, María A., Leguto, Alcides J., Morgada, Marcos N., Vila, Alejandro J., Murgida, Daniel H.

“…Attaining rational modulation of thermodynamic and kinetic redox parameters of metalloproteins is a key milestone towards the (re)design of proteins with new…”
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Drametic electronic perturbations of CuA center via subtle geometric changes by Legutot, Alcides J., Smith, Meghan A., Morgada, Marcos N., Zitare, Ulises A., Murgida, Daniel H., Lancaster, Kyle M., Vila, Alejandro J.

“…Cu A is a binuclear copper site acting as electron entry port in terminal heme-copper oxidases. In the oxidized form, Cu A is a mixed valence pair whose…”
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Superoxide versus peroxide activation of dye decolorizing peroxidases for bioelectrocatalysis by Zitare, Ulises A., Vieyra, Francisco, Scocozza, Magalí F., Rosciani, Francisco, Castro, María A., Martins, Ligia O., Murgida, Daniel H.

“…Here we show that dye decolorizing peroxidases can be electrochemically activated for substrate oxidation without addition of exogenous H2O2, yielding…”
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