Abstract
Because redox energy can be converted into conformational energy, heme redox proteins offer a unique opportunity to examine the coupling between redox reactions and protein mechanics. Here, we use Atomic Force Microscopy-based single-molecule force spectroscopy (SMFS) to directly examine the effect of heme and its oxidation state on the mechanical properties of cytochrome b562 (cyt b562). We found that cyt b562 is mechanically stronger in its reduced state as compared to its oxidized state. In addition, we discovered the shortening of the folded length of cytochrome b562 in its reduced state. This novel observation could be the basis of heme protein-based “piezoelectric-like” nanomaterials and actuators.View Large Image | View Hi-Res Image | Download PowerPoint Slide
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