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

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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Bibliographic Details
Published in:Journal of the American Chemical Society 2017-07, Vol.139 (29), p.9803-9806
Main Authors: Alvarez-Paggi, Damian, Zitare, Ulises A, Szuster, Jonathan, Morgada, Marcos N, Leguto, Alcides J, Vila, Alejandro J, Murgida, Daniel H
Format: Article
Language:English
Subjects:
Copper - chemistry
Copper - metabolism
Electron Transport Complex IV - chemistry
Electron Transport Complex IV - metabolism
Electrons
Entropy
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Ligands
Oxidation-Reduction
Static Electricity
Thermodynamics
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Summary: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 report clear correlations of the entropic and enthalpic contributions to redox potentials with Q and with the identity and hydrophobicity of the weak axial ligand, respectively.
ISSN:0002-7863
1520-5126
DOI:10.1021/jacs.7b05199