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

• 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
• ISSN: 0002-7863; 1520-5126
• DOI: 10.1021/ja053315t

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.