Abstract:
Copper sites in proteins are designed to perform either electron transfer or redox catalysis. Type 1 and CuA sites are electron transfer hubs bound to a rigid protein fold that prevents binding of exogenous ligands and side reactions. Here we report the engineering of two Type 1 sites by loop-directed mutagenesis within a CuA scaffold with unique electronic structures and functional features. A copper-thioether axial bond shorter than the copper-thiolate bond is responsible for the electronic structure features, in contrast to all other natural or chimeric sites where the copper thiolate bond is short. These sites display highly unusual features, such as: (1) a high reduction potential despite a strong interaction with the axial ligand, which we attribute to changes in the hydrogen bond network and (2) the ability to bind exogenous ligands such as imidazole and azide. This strategy widens the possibility of using natural protein scaffolds with functional features not present in nature. © The Royal Society of Chemistry.
Registro:
Documento: |
Artículo
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Título: | Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis |
Autor: | Espinoza-Cara, A.; Zitare, U.; Alvarez-Paggi, D.; Klinke, S.; Otero, L.H.; Murgida, D.H.; Vila, A.J. |
Filiación: | Instituto de Biología Molecular y Celular de Rosario (IBR CONICET-UNR), Rosario, Argentina Área Biofísica, Departamento de Química Biológica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina Departamento de Química Inorgánica, Analítica y Química Física, INQUIMAE, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, CONICET, Buenos Aires, Argentina Fundación Instituto Leloir, IIBBA-CONICET, Buenos Aires, Argentina Plataforma Argentina de Biología Estructural y Metabolómica PLABEM, Buenos Aires, Argentina
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Palabras clave: | Binding sites; Electron transitions; Electronic structure; Hydrogen bonds; Ligands; Mutagenesis; Proteins; Scaffolds (biology); Directed mutagenesis; Electron transfer; Exogenous ligands; Functional features; Hydrogen bond networks; Natural proteins; Reduction potential; Strong interaction; Copper |
Año: | 2018
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Volumen: | 9
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Número: | 32
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Página de inicio: | 6692
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Página de fin: | 6702
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DOI: |
http://dx.doi.org/10.1039/c8sc01444b |
Título revista: | Chemical Science
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Título revista abreviado: | Chem. Sci.
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ISSN: | 20416520
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CODEN: | CSHCC
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Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_20416520_v9_n32_p6692_EspinozaCara |
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Citas:
---------- APA ----------
Espinoza-Cara, A., Zitare, U., Alvarez-Paggi, D., Klinke, S., Otero, L.H., Murgida, D.H. & Vila, A.J.
(2018)
. Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis. Chemical Science, 9(32), 6692-6702.
http://dx.doi.org/10.1039/c8sc01444b---------- CHICAGO ----------
Espinoza-Cara, A., Zitare, U., Alvarez-Paggi, D., Klinke, S., Otero, L.H., Murgida, D.H., et al.
"Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis"
. Chemical Science 9, no. 32
(2018) : 6692-6702.
http://dx.doi.org/10.1039/c8sc01444b---------- MLA ----------
Espinoza-Cara, A., Zitare, U., Alvarez-Paggi, D., Klinke, S., Otero, L.H., Murgida, D.H., et al.
"Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis"
. Chemical Science, vol. 9, no. 32, 2018, pp. 6692-6702.
http://dx.doi.org/10.1039/c8sc01444b---------- VANCOUVER ----------
Espinoza-Cara, A., Zitare, U., Alvarez-Paggi, D., Klinke, S., Otero, L.H., Murgida, D.H., et al. Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis. Chem. Sci. 2018;9(32):6692-6702.
http://dx.doi.org/10.1039/c8sc01444b