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

ZITARE, ULISES A.; LEGUTO, ALCIDES J.; ALVAREZ-PAGGI, DAMIAN; ALVAREZ-PAGGI, DAMIAN; MORGADA, MARCOS N.; MORGADA, MARCOS N.; SZUSTER, JONATHAN; MURGIDA, DANIEL H.; MURGIDA, DANIEL H.; VILA, ALEJANDRO J.; SZUSTER, JONATHAN; ZITARE, ULISES A.; VILA, ALEJANDRO J.; LEGUTO, ALCIDES J.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

AMER CHEMICAL SOC

Año: 2017 vol. 139 p. 9803 - 9806

0002-7863

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.