Studies of the Thermodynamics of Some Native and Ruthenated Metalloproteins by Spectroelectrochemistry

• Main Author: Chiang, Huey-jenn
• Format: Thesis
• Language: English
• Published: 1987
• Subjects: Sperm whale
• Online Access: https://thesis.library.caltech.edu/11878/; https://thesis.library.caltech.edu/11878/1/Chiang_H-J_1987.pdf; https://resolver.caltech.edu/CaltechTHESIS:10312019-170145504

The thermodynamic parameters of redox centers in some metalloproteins have been investigated using spectroelectrochemical techniques, with the employment of an OTTLE (Optically Transparent Thin-Layer Electrode) cell. With the aid of various carefully selected mediators, the temperature dependence of the formal redox potentials of type I copper (blue copper) ions in Rhus vernicifera (tree) laccase, as well as in native and in pentaammineruthenium-modified azurins from Pseudomonas aeruginosa , have been measured. Similar experiments have been carried out for the heme site of cis -[Ru(en) 2 (OH)(His)]-horse heart cytochrome c (en: ethylenediamine; His: histidine). Cyclic voltammetry has been used to study the pH-dependence of the formal redox potentials of the appended ruthenium ion in cis -[Ru(en) 2 (OH)(His)]-horse heart cytochrome c . Finally, the synthesis and spectroelectrochemistry of sperm whale myoglobin reconstituted with [Ru(MpIX)(DMSO) dicarboxylic acid]- moiety (MpIX: mesoporphyrin IX; DMSO: dimethyl sulfoxide) have also been carried out.