Journal of the American Chemical Society
Journal of the American Chemical Society
5 years ago

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

Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function
Alejandro J. Vila, Daniel H. Murgida, Marcos N. Morgada, Jonathan Szuster, Ulises A. Zitare, Damian Alvarez-Paggi, Alcides J. Leguto
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.

Publisher URL: http://dx.doi.org/10.1021/jacs.7b05199

DOI: 10.1021/jacs.7b05199

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