Electron–Phonon Coupling in Cyanobacterial Photosystem I
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...
Saved in:
Published in | The journal of physical chemistry. B Vol. 122; no. 33; pp. 7943 - 7955 |
---|---|
Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
23.08.2018
|
Online Access | Get full text |
Cover
Loading…
Summary: | 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 A1 and the oxidized chlorophyll special pair P700 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. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1520-6106 1520-5207 |
DOI: | 10.1021/acs.jpcb.8b03906 |