Studies of the Thermodynamics of Some Native and Ruthenated Metalloproteins by Spectroelectrochemistry
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...
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| Format: | Thesis |
| Language: | English |
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California Institute of Technology
1987
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| Online Access: | https://dx.doi.org/10.7907/8fcf-kt72 https://resolver.caltech.edu/CaltechTHESIS:10312019-170145504 |
| Summary: | 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. |
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