Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function

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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 electronic ground state and by perturbation of the electrostatic potential through point mutations, loop engineering and pH variation. We re...

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Autores principales: Alvarez-Paggi, D., Zitare, U.A., Szuster, J., Morgada, M.N., Leguto, A.J., Vila, A.J., Murgida, D.H.
Formato: JOUR
Materias:
Ground state
Redox reactions
Axial ligand
Cytochrome c oxidase
Electronic ground state
Electrostatic potentials
Partition functions
Point mutations
Redox centers
Redox potentials
Tuning
Article
conformational transition
electric activity
enthalpy
entropy
hydrophobicity
oxidation reduction potential
oxidation reduction state
partition coefficient
pH
quantum mechanics
temperature dependence
thermodynamics
chemical phenomena
chemistry
electron
metabolism
oxidation reduction reaction
static electricity
copper
cytochrome c oxidase
ligand
Copper
Electron Transport Complex IV
Electrons
Entropy
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Ligands
Oxidation-Reduction
Static Electricity
Thermodynamics
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00027863_v139_n29_p9803_AlvarezPaggi
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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