The met axial ligand determines the redox potential in CuA sites

The replacement of the axial methionine ligand in a native CuA protein rendered a series of stable mutants with spectroscopic features of a mixed valence center. The mutations resulted in minor perturbations of the electronic structure of this site but led to significant changes in the redox potenti...

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Detalles Bibliográficos
Autor principal:	Murgida, Daniel Horacio
Publicado:	2007
Materias:	copper ligand met axial ligand unclassified drug article bacillus denitrificans fluorescens electron spin resonance electron transport hydrophobicity oxidation reduction reaction Pseudomonas Rhodobacter sphaeroides Azurin Copper Electron Spin Resonance Spectroscopy Ligands Models, Molecular Oxidation-Reduction Spectrophotometry, Ultraviolet
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v129_n39_p11884_Ledesma http://hdl.handle.net/20.500.12110/paper_00027863_v129_n39_p11884_Ledesma
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00027863_v129_n39_p11884_Ledesma
record_format	dspace
spelling	paper:paper_00027863_v129_n39_p11884_Ledesma2023-06-08T14:22:43Z The met axial ligand determines the redox potential in CuA sites Murgida, Daniel Horacio copper ligand met axial ligand unclassified drug article bacillus denitrificans fluorescens electron spin resonance electron transport hydrophobicity oxidation reduction reaction Pseudomonas Rhodobacter sphaeroides Azurin Copper Electron Spin Resonance Spectroscopy Ligands Models, Molecular Oxidation-Reduction Spectrophotometry, Ultraviolet The replacement of the axial methionine ligand in a native CuA protein rendered a series of stable mutants with spectroscopic features of a mixed valence center. The mutations resulted in minor perturbations of the electronic structure of this site but led to significant changes in the redox potential. This suggests that the axial ligand plays a role in tuning the redox potential of CuA, resembling the behavior observed in blue copper sites. Copyright © 2007 American Chemical Society. Fil:Murgida, D.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2007 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v129_n39_p11884_Ledesma http://hdl.handle.net/20.500.12110/paper_00027863_v129_n39_p11884_Ledesma
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	copper ligand met axial ligand unclassified drug article bacillus denitrificans fluorescens electron spin resonance electron transport hydrophobicity oxidation reduction reaction Pseudomonas Rhodobacter sphaeroides Azurin Copper Electron Spin Resonance Spectroscopy Ligands Models, Molecular Oxidation-Reduction Spectrophotometry, Ultraviolet
spellingShingle	copper ligand met axial ligand unclassified drug article bacillus denitrificans fluorescens electron spin resonance electron transport hydrophobicity oxidation reduction reaction Pseudomonas Rhodobacter sphaeroides Azurin Copper Electron Spin Resonance Spectroscopy Ligands Models, Molecular Oxidation-Reduction Spectrophotometry, Ultraviolet Murgida, Daniel Horacio The met axial ligand determines the redox potential in CuA sites
topic_facet	copper ligand met axial ligand unclassified drug article bacillus denitrificans fluorescens electron spin resonance electron transport hydrophobicity oxidation reduction reaction Pseudomonas Rhodobacter sphaeroides Azurin Copper Electron Spin Resonance Spectroscopy Ligands Models, Molecular Oxidation-Reduction Spectrophotometry, Ultraviolet
description	The replacement of the axial methionine ligand in a native CuA protein rendered a series of stable mutants with spectroscopic features of a mixed valence center. The mutations resulted in minor perturbations of the electronic structure of this site but led to significant changes in the redox potential. This suggests that the axial ligand plays a role in tuning the redox potential of CuA, resembling the behavior observed in blue copper sites. Copyright © 2007 American Chemical Society.
author	Murgida, Daniel Horacio
author_facet	Murgida, Daniel Horacio
author_sort	Murgida, Daniel Horacio
title	The met axial ligand determines the redox potential in CuA sites
title_short	The met axial ligand determines the redox potential in CuA sites
title_full	The met axial ligand determines the redox potential in CuA sites
title_fullStr	The met axial ligand determines the redox potential in CuA sites
title_full_unstemmed	The met axial ligand determines the redox potential in CuA sites
title_sort	met axial ligand determines the redox potential in cua sites
publishDate	2007
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v129_n39_p11884_Ledesma http://hdl.handle.net/20.500.12110/paper_00027863_v129_n39_p11884_Ledesma
work_keys_str_mv	AT murgidadanielhoracio themetaxialliganddeterminestheredoxpotentialincuasites AT murgidadanielhoracio metaxialliganddeterminestheredoxpotentialincuasites
_version_	1768544664257822720

The met axial ligand determines the redox potential in CuA sites

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