Proteins immobilized on inorganic surfaces are important in technological fields such as biosensors, enzymatic biofuel cells and biomolecular electronics. In these frameworks, it has been demonstrated that some proteins are able to keep their functionality, although the latter may be somewhat modified by the interaction with the surface. Cytochrome C, an heme-based electron transfer protein, has been found to be able to exchange electrons with the gold surface on which it is immobilized, but some deviations from the expected electron transfer rates were evidenced [C. A. Bortolotti, et al., J. Phys. Chem. C 2007, 111, 12100-12105]. In this work we have used molecular dynamics simulations of (native and mutated) yeast cytochrome C supported on Au(111) to investigate the microscopic picture behind the experimental behavior of the molecule. In particular, we have focused on the structural re-arrangements due to the interactions with the surface. We found that, despite being secondary-structure preserving, they can profoundly affect protein-surface electronic coupling and, in turn, electron transfer rates, explaining experimental findings. The conformational flexibility of the protein in the region of the protein-surface bond is thus pivotal in determining the resulting ET functionality of the immobilized protein.
|Evidence ID||Analyze ID||Interactor||Interactor Systematic Name||Interactor||Interactor Systematic Name||Type||Assay||Annotation||Action||Modification||Phenotype||Source||Reference||Note|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Gene Ontology Term||Gene Ontology Term ID||Qualifier||Aspect||Method||Evidence||Source||Assigned On||Reference||Annotation Extension|
|Evidence ID||Analyze ID||Gene||Gene Systematic Name||Phenotype||Experiment Type||Experiment Type Category||Mutant Information||Strain Background||Chemical||Details||Reference|
|Evidence ID||Analyze ID||Regulator||Regulator Systematic Name||Target||Target Systematic Name||Experiment||Conditions||Strain||Source||Reference|