Investigating redox switch mechanisms in hydrogenases

About the topic

Redox-active enzymes primarily utilize metallocofactors to facilitate complex oxidative and reductive transformations. Understanding the electronic structure of these metallocofactors is crucial for manipulating enzyme activity. Our laboratory focuses on investigating metalloproteins using advanced EPR spectroscopy, complemented by biochemical and theoretical techniques.

 We have demonstrated that the FeFe-hydrogenase CrHydA1, known for its efficient catalysis of the reversible conversion of molecular hydrogen into protons and electrons, operates via a novel 'redox switch' mechanism influenced by its environment and solvation. This project aims to elucidate the principles and regulators of this redox switch and to determine whether this mechanism is universal among hydrogenases. To this end, we will explore recently discovered minimal and ultra-minimal hydrogenases related to CrHydA1.

What they expect from students

We are looking for a motivated student with a solid foundation in magnetic resonance techniques and a strong interest in acquiring knowledge in EPR spectroscopy. Prior experience with magnetic resonance methods is highly desirable, as it will facilitate a deeper understanding of the concepts involved in our research. Additionally, familiarity with sequence analysis would be a valuable asset, enhancing the student's ability to contribute effectively to our projects. A genuine enthusiasm for learning and exploring the intricacies of metalloproteins will be essential for success in this role.

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