Fine Tuning of Functional Features of the Cu A Site by Loop-Directed Mutagenesis

Here we report the spectroscopic and electrochemical characterization of three novel chimeric Cu A proteins in which either one or the three loops surrounding the metal ions in the Thermus thermophilus protein have been replaced by homologous human and plant sequences while preserving the set of coo...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Zitare, U.A., Szuster, J., Santalla, M.C., Llases, M.E., Morgada, M.N., Vila, A.J., Murgida, D.H.
Formato: JOUR
Materias:
copper
cytochrome c oxidase
chemistry
electrochemical analysis
electron transport
kinetics
metabolism
molecular model
thermodynamics
Thermus thermophilus
X ray crystallography
Copper
Crystallography, X-Ray
Electrochemical Techniques
Electron Transport
Electron Transport Complex IV
Kinetics
Models, Molecular
Thermodynamics
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00201669_v58_n3_p2149_Zitare
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_00201669_v58_n3_p2149_Zitare
record_format dspace
spelling todo:paper_00201669_v58_n3_p2149_Zitare2023-10-03T14:17:11Z Fine Tuning of Functional Features of the Cu A Site by Loop-Directed Mutagenesis Zitare, U.A. Szuster, J. Santalla, M.C. Llases, M.E. Morgada, M.N. Vila, A.J. Murgida, D.H. copper cytochrome c oxidase chemistry electrochemical analysis electron transport kinetics metabolism molecular model thermodynamics Thermus thermophilus X ray crystallography Copper Crystallography, X-Ray Electrochemical Techniques Electron Transport Electron Transport Complex IV Kinetics Models, Molecular Thermodynamics Thermus thermophilus Here we report the spectroscopic and electrochemical characterization of three novel chimeric Cu A proteins in which either one or the three loops surrounding the metal ions in the Thermus thermophilus protein have been replaced by homologous human and plant sequences while preserving the set of coordinating amino acids. These conservative modifications mimic basic differences between Cu A sites from different organisms and allow for fine tuning the energy gap between alternative electronic ground states of Cu A. . This results in a systematic modulation of thermodynamic and kinetic electron transfer (ET) parameters and in the selection of one of two possible redox-active molecular orbitals, which differ in the ET reorganization energy by a factor of 2. Moreover, the ET mechanism is found to be frictionally controlled, and the modifications introduced into the different chimeras do not affect the frictional activation parameter. © 2019 American Chemical Society. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00201669_v58_n3_p2149_Zitare
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
cytochrome c oxidase
chemistry
electrochemical analysis
electron transport
kinetics
metabolism
molecular model
thermodynamics
Thermus thermophilus
X ray crystallography
Copper
Crystallography, X-Ray
Electrochemical Techniques
Electron Transport
Electron Transport Complex IV
Kinetics
Models, Molecular
Thermodynamics
Thermus thermophilus
spellingShingle copper
cytochrome c oxidase
chemistry
electrochemical analysis
electron transport
kinetics
metabolism
molecular model
thermodynamics
Thermus thermophilus
X ray crystallography
Copper
Crystallography, X-Ray
Electrochemical Techniques
Electron Transport
Electron Transport Complex IV
Kinetics
Models, Molecular
Thermodynamics
Thermus thermophilus
Zitare, U.A.
Szuster, J.
Santalla, M.C.
Llases, M.E.
Morgada, M.N.
Vila, A.J.
Murgida, D.H.
Fine Tuning of Functional Features of the Cu A Site by Loop-Directed Mutagenesis
topic_facet copper
cytochrome c oxidase
chemistry
electrochemical analysis
electron transport
kinetics
metabolism
molecular model
thermodynamics
Thermus thermophilus
X ray crystallography
Copper
Crystallography, X-Ray
Electrochemical Techniques
Electron Transport
Electron Transport Complex IV
Kinetics
Models, Molecular
Thermodynamics
Thermus thermophilus
description Here we report the spectroscopic and electrochemical characterization of three novel chimeric Cu A proteins in which either one or the three loops surrounding the metal ions in the Thermus thermophilus protein have been replaced by homologous human and plant sequences while preserving the set of coordinating amino acids. These conservative modifications mimic basic differences between Cu A sites from different organisms and allow for fine tuning the energy gap between alternative electronic ground states of Cu A. . This results in a systematic modulation of thermodynamic and kinetic electron transfer (ET) parameters and in the selection of one of two possible redox-active molecular orbitals, which differ in the ET reorganization energy by a factor of 2. Moreover, the ET mechanism is found to be frictionally controlled, and the modifications introduced into the different chimeras do not affect the frictional activation parameter. © 2019 American Chemical Society.
format JOUR
author Zitare, U.A.
Szuster, J.
Santalla, M.C.
Llases, M.E.
Morgada, M.N.
Vila, A.J.
Murgida, D.H.
author_facet Zitare, U.A.
Szuster, J.
Santalla, M.C.
Llases, M.E.
Morgada, M.N.
Vila, A.J.
Murgida, D.H.
author_sort Zitare, U.A.
title Fine Tuning of Functional Features of the Cu A Site by Loop-Directed Mutagenesis
title_short Fine Tuning of Functional Features of the Cu A Site by Loop-Directed Mutagenesis
title_full Fine Tuning of Functional Features of the Cu A Site by Loop-Directed Mutagenesis
title_fullStr Fine Tuning of Functional Features of the Cu A Site by Loop-Directed Mutagenesis
title_full_unstemmed Fine Tuning of Functional Features of the Cu A Site by Loop-Directed Mutagenesis
title_sort fine tuning of functional features of the cu a site by loop-directed mutagenesis
url http://hdl.handle.net/20.500.12110/paper_00201669_v58_n3_p2149_Zitare
work_keys_str_mv AT zitareua finetuningoffunctionalfeaturesofthecuasitebyloopdirectedmutagenesis
AT szusterj finetuningoffunctionalfeaturesofthecuasitebyloopdirectedmutagenesis
AT santallamc finetuningoffunctionalfeaturesofthecuasitebyloopdirectedmutagenesis
AT llasesme finetuningoffunctionalfeaturesofthecuasitebyloopdirectedmutagenesis
AT morgadamn finetuningoffunctionalfeaturesofthecuasitebyloopdirectedmutagenesis
AT vilaaj finetuningoffunctionalfeaturesofthecuasitebyloopdirectedmutagenesis
AT murgidadh finetuningoffunctionalfeaturesofthecuasitebyloopdirectedmutagenesis
_version_ 1807320442892976128

Ejemplares similares