Evidence from time resolved studies of the P700(.+)/A1(.-) radical pair for photosynthetic electron transfer on both the PsaA and PsaB branches of the photosystem I reaction centre.
Kinetic analysis using pulsed electron paramagnetic resonance (EPR) of photosynthetic electron transfer in the photosystem I reaction centres of Synechocystis 6803, in wild-type Chlamydomonas reinhardtii, and in site directed mutants of the phylloquinone binding sites in C. reinhardtii, indicates that electron transfer from the reaction centre primary electron donor, P700, to the iron-sulphur centres, Fe-S(X/A/B), can occur through either the PsaA or PsaB side phylloquinone. At low temperature reaction centres are frozen in states which allow electron transfer on one side of the reaction centre only. A fraction always donates electrons to the PsaA side quinone, the remainder to the PsaB side.
Muhiuddin
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IP
Department of Biology, University College London, UK.
Heathcote
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P
Carter
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Purton
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Rigby
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Evans
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MC
D000818:Animals; D016825:Chlamydomonas reinhardtii / Q000502:physiology; D004578:Electron Spin Resonance Spectroscopy; D005609:Free Radicals; D045342:Light-Harvesting Protein Complexes; D008565:Membrane Proteins / Q000502:physiology*; D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D010940:Plant Proteins / Q000502:physiology*
D005609:Free Radicals; D045342:Light-Harvesting Protein Complexes; D008565:Membrane Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D010940:Plant Proteins; C089909:photosystem I, psaB subunit