Bidirectional Electron Transfer in Photosystem I:  Direct Evidence from High-Frequency Time-Resolved EPR Spectroscopy

Efficient charge separation occurring within membrane-bound reaction center proteins is the most important step of photosynthetic solar energy conversion. All reaction centers are classified into two types, I and II. X-ray crystal structures reveal that both types bind two symmetric membrane-spannin...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2005-08, Vol.127 (34), p.11910-11911
Main Authors: Poluektov, Oleg G, Paschenko, Sergei V, Utschig, Lisa M, Lakshmi, K. V, Thurnauer, Marion C
Format: Article
Language:English
Subjects:
Biological and medical sciences
Electron Spin Resonance Spectroscopy - methods
Electron Transport
Fundamental and applied biological sciences. Psychology
Iron - chemistry
Models, Chemical
Molecular biophysics
Oxidation-Reduction
Photochemistry. Photosynthesis. Bioluminescence
Photosynthesis - physiology
Photosynthetic Reaction Center Complex Proteins - chemistry
Photosynthetic Reaction Center Complex Proteins - metabolism
Photosystem I Protein Complex - chemistry
Photosystem I Protein Complex - metabolism
Photosystem II Protein Complex - chemistry
Photosystem II Protein Complex - metabolism
Radiation-biomolecule interaction
Sulfur - chemistry
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Summary:Efficient charge separation occurring within membrane-bound reaction center proteins is the most important step of photosynthetic solar energy conversion. All reaction centers are classified into two types, I and II. X-ray crystal structures reveal that both types bind two symmetric membrane-spanning branches of potential electron-transfer cofactors. Determination of the functional roles of these pairs of branches is of fundamental importance. While it is established that in type II reaction centers only one branch functions in electron transfer, we present the first direct spectroscopic evidence that both cofactor branches are active in the type I reaction center, photosystem I.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja053315t