AI Article Synopsis
- The study examines whether the protein medium in biophysics behaves more like a fluid or a solid at room temperature, specifically analyzing the dynamics of photosystem I in cyanobacteria.
- It was found that the dielectric properties during early electron transfer reactions suggest a solid-like behavior, indicating a need to consider electron-phonon coupling even at moderate temperatures.
- This coupling may explain why electron transfer in pigment-protein complexes shows weak sensitivity to changes in environmental factors like temperature and chemical composition.
Article Abstract
One of the fundamental problems in biophysics is whether the protein medium at room temperature can be properly treated as a fluid dielectric or whether its dynamics is determined by a highly ordered molecular structure resembling the properties of crystalline and amorphous solids. Here, we measured the recombination between reduced A and the oxidized chlorophyll special pair P over a wide temperature range using preparations of photosystem I from the cyanobacterium Synechococcus sp. PCC 7002 depleted of the iron-sulfur clusters. We found that the dielectric properties of the protein matrix in early electron transfer reactions of photosystem I resemble the behavior of solids that require an implicit treatment of electron-phonon coupling even at ambient temperatures. The quantum effects of electron-phonon coupling in proteins could account for a variety of phenomena, such as the weak sensitivity of electron transfer in pigment-protein complexes to changing environmental conditions including temperature, driving force, polarity, and chemical composition.
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| http://dx.doi.org/10.1021/acs.jpcb.8b03906 | DOI Listing |
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