Summary
Redox enzymes catalyze numerous biological processes that are also relevant for a variety of applications, including energy conversion, biosensing, and electrosynthesis of complex molecules. The intrinsic lability of enzymes that gradually lose catalytic activity over time, however, restricts their operational half-life for practical large-scale application of this sustainable and incredibly energy-saving system. Moreover, enzymes are nanometer-sized macromolecules, that must be properly aligned with the electrode surface for efficient electron transfer and substrate access to the active site regardless of the electron transfer mechanism, direct or mediated, which typically necessitates laborious procedures. The goal of this Marie Skłodowska-Curie Postdoctoral Fellowship project is to develop a reversible immobilization approach that can attach enzymes on an electrode surface in a defined orientation and permit their controlled release on demand upon stimulation (ReversE). This will be accomplished by capitalizing on a gold (Au)-binding peptide fused to [FeFe]-hydrogenase as the model enzyme to have the dual functionality of orienting enzymes on the Au electrode surface in a precise manner to support efficient electron transfer and substrate access to the active site, as well as allowing the bound Au-binding peptide fused enzymes to be released by electrochemical or chemical stimuli and replaced with fresh enzymes when the catalytic activity is reduced to a predetermined value. This will open up the possibility for enzyme regeneration which will be groundbreaking in the context of sustainable deployment of enzyme‒electrode systems.
Unfold all
/
Fold all
More information & hyperlinks
| Web resources: | https://cordis.europa.eu/project/id/101110795 |
| Start date: | 01-08-2023 |
| End date: | 31-07-2025 |
| Total budget - Public funding: | - 189 687,00 Euro |
Cordis data
Original description
Redox enzymes catalyze numerous biological processes that are also relevant for a variety of applications, including energy conversion, biosensing, and electrosynthesis of complex molecules. The intrinsic lability of enzymes that gradually lose catalytic activity over time, however, restricts their operational half-life for practical large-scale application of this sustainable and incredibly energy-saving system. Moreover, enzymes are nanometer-sized macromolecules, that must be properly aligned with the electrode surface for efficient electron transfer and substrate access to the active site regardless of the electron transfer mechanism, direct or mediated, which typically necessitates laborious procedures. The goal of this Marie Skłodowska-Curie Postdoctoral Fellowship project is to develop a reversible immobilization approach that can attach enzymes on an electrode surface in a defined orientation and permit their controlled release on demand upon stimulation (ReversE). This will be accomplished by capitalizing on a gold (Au)-binding peptide fused to [FeFe]-hydrogenase as the model enzyme to have the dual functionality of orienting enzymes on the Au electrode surface in a precise manner to support efficient electron transfer and substrate access to the active site, as well as allowing the bound Au-binding peptide fused enzymes to be released by electrochemical or chemical stimuli and replaced with fresh enzymes when the catalytic activity is reduced to a predetermined value. This will open up the possibility for enzyme regeneration which will be groundbreaking in the context of sustainable deployment of enzyme‒electrode systems.Status
SIGNEDCall topic
HORIZON-MSCA-2022-PF-01-01Update Date
31-07-2023
Images
No images available.
Geographical location(s)
