Electrochemical investigation of redox thermodynamics of immobilized myoglobin : ionic and ligation effects
In this study, we investigated redox thermodynamics of myoglobin as well as the ionic (phosphate ions) and ligation (imidazole) effects via a dynamic electrochemical approach. We employed a previously established system that features nonmediated, direct electrochemistry of myoglobin and myoglobin in...
| Publié dans: | Langmuir : the ACS journal of surfaces and colloids. - 1991. - 21(2005), 1 vom: 04. Jan., Seite 375-8 |
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| Auteur principal: | |
| Autres auteurs: | , , , , |
| Format: | Article |
| Langue: | English |
| Publié: |
2005
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| Accès à la collection: | Langmuir : the ACS journal of surfaces and colloids |
| Sujets: | Journal Article Research Support, Non-U.S. Gov't Ions Myoglobin |
| Résumé: | In this study, we investigated redox thermodynamics of myoglobin as well as the ionic (phosphate ions) and ligation (imidazole) effects via a dynamic electrochemical approach. We employed a previously established system that features nonmediated, direct electrochemistry of myoglobin and myoglobin in an immobilized state (i.e., diffusionless electrochemistry). Thermodynamics parameters were obtained by measuring redox potential (E degrees ') of myoglobin at varied temperature (T), in the presence and in the absence of specific ions or axial ligands. As a step further, we evaluated contributions from allosteric effect and axial iron ligation by partitioning E degrees ' changes into entropic and enthalpic terms. Compensation phenomena between the entropic and enthalpic changes were observed in all these cases. On the basis of these studies, we also correlated these phenomena to possible structural variations |
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| Description: | Date Completed 28.06.2006 Date Revised 15.11.2006 published: Print Citation Status MEDLINE |
| ISSN: | 0743-7463 |