Light-induced spin polarization in type I photosynthetic reaction centres.
The use of light-induced spin polarization to study the structure and function of type I reaction centres is reviewed. The absorption of light by these systems generates a series of sequential radical pairs, which exhibit spin polarization as a result of the correlation of the unpaired electron spins. A description of how the polarization patterns can be used to deduce the relative orientation of the radicals is given and the most important structural results from such studies on photosystem I (PS I) are summarized. Quinone exchange experiments which demonstrate the influence of protein-cofactor interactions on the polarization patterns are discussed. The results show that there are significant differences between the binding sites of the primary quinone acceptors in PS I and purple bacterial reaction centres and suggest that pi-pi interactions probably play a more important role in PS I. Studies using spin-polarized EPR transients and spectra to investigate the electron transfer pathway and kinetics are also reviewed. The results from PS I, green-sulphur bacteria and Heliobacteria are compared and the controversy surrounding the role of a quinone in the electron transfer in the latter two systems is discussed.
van der Est
A
A
Department of Chemistry, Brock University, 500 Glenridge Avenue, L2S 3A1, St. Catharines, ON, Canada. avde@spartan.ac.brocku.ca
D001665:Binding Sites; D019414:Chlorobi / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D008027:Light; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry*; D045331:Photosystem I Protein Complex; D011809:Quinones / Q000737:chemistry
D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D011809:Quinones