Elastic control of electron transfer enthalpy and intensity of light absorption by cupric blue proteins
1Department of Physics and Biophysics Program, University of Virginia, Charlottesville, VA 22901, USA. asbox@virginia.edu
Abstract:
The experimental data available shows that the change in enthalpy accompanying electron transfer to cupric blue proteins decreases as the ratio of the strengths of two visible light absorption bands increases. A compact mathematical expression for this inverse relation is formulated, the derivation of which demonstrates that the unusual geometry imposed by the protein upon the redox site is responsible both for the optical band intensity ratio and for a significant fraction of the enthalpy change.
Related Concept Videos
The Antenna Complex
Colors and Magnetism
When atoms or molecules absorb light at the proper frequency, their electrons are excited to higher-energy orbitals. For many main group atoms and molecules, the absorbed photons are in the ultraviolet range of the electromagnetic spectrum, which cannot be detected by the human eye. For coordination compounds, the energy difference between the d orbitals often allows photons in the visible range to be absorbed and emitted, which is seen as colors by the human eye.
The Photochemical Reaction Center
Protein Dynamics in Living Cells
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Channel Rhodopsins
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...


