Offres de thèse et d'emploi

Understanding how protein conformational dynamics influence enzymatic activity is a major challenge at the interface of chemistry, biophysics and molecular biology. While advanced structural methods provide valuable information on static protein structures, establishing direct correlations between conformational changes and catalytic activity remains particularly difficult. The ANR-funded project ECLECTYC (Electrochemical and EPR approach of the impact of Conformational Changes on enzymatic ELectrocaTalYsis: case of copper efflux oxidase CueO) aims to develop innovative methodologies combining electrochemistry, spectroscopy and microscopy to investigate conformational dynamics of enzymes and their impact on bioelectrocatalysis.
The project focuses on the multicopper oxidase CueO, a model enzyme possessing a flexible methionine-rich domain whose structural dynamics are believed to regulate enzymatic activity. A central prerequisite for these studies is the development of well-defined electrochemical interfaces enabling the site-specific immobilization of engineered enzymes on gold electrodes with controlled orientation.
Within this framework, the successful candidate will contribute to the design of molecular platforms for enzyme immobilization and to the establishment of robust structure-property relationships governing interfacial electron transfer and enzyme orientation.