Secondary pair charge recombination in photosystem I under strongly reducing conditions: temperature dependence and suggested mechanism.
Photoinduced electron transfer in photosystem I (PS I) proceeds from the excited primary electron donor P700 (a chlorophyll a dimer) via the primary acceptor A0 (chlorophyll a) and the secondary acceptor A1 (phylloquinone) to three [4Fe-4S] clusters, Fx, FA, and FB. Prereduction of the iron-sulfur clusters blocks electron transfer beyond A1. It has been shown previously that, under such conditions, the secondary pair P700+A1- decays by charge recombination with t1/2 approximately 250 ns at room temperature, forming the P700 triplet state (3P700) with a yield exceeding 85%. This reaction is unusual, as the secondary pair in other photosynthetic reaction centers recombines much slower and forms directly the singlet ground state rather than the triplet state of the primary donor. Here we studied the temperature dependence of secondary pair recombination in PS I from the cyanobacterium Synechococcus sp. PCC6803, which had been illuminated in the presence of dithionite at pH 10 to reduce all three iron-sulfur clusters. The reaction P700+A1- --> 3P700 was monitored by flash absorption spectroscopy. With decreasing temperature, the recombination slowed down and the yield of 3P700 decreased. In the range between 303 K and 240 K, the recombination rates could be described by the Arrhenius law with an activation energy of approximately 170 meV. Below 240 K, the temperature dependence became much weaker, and recombination to the singlet ground state became the dominating process. To explain the fast activated recombination to the P700 triplet state, we suggest a mechanism involving efficient singlet to triplet spin evolution in the secondary pair, thermally activated repopulation of the more closely spaced primary pair P700+A0- in a triplet spin configuration, and subsequent fast recombination (intrinsic rate on the order of 10(9) s(-1)) forming 3P700.
Polm
M
M
Section de Bioénergétique and CNRS-URA 2096, Département de Biologie Cellulaire et Moléculaire, CEA Saclay, Gif-sur-Yvette, France.
Brettel
K
K
D002734:Chlorophyll / Q000378:metabolism; D000077194:Chlorophyll A; D000458:Cyanobacteria / Q000378:metabolism; D019281:Dimerization; D004579:Electron Transport; D007506:Iron-Sulfur Proteins / Q000378:metabolism; D007700:Kinetics; D008027:Light; D045342:Light-Harvesting Protein Complexes; D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism*; D045331:Photosystem I Protein Complex; D013696:Temperature; D013816:Thermodynamics; D013997:Time Factors; D010837:Vitamin K 1 / Q000378:metabolism
D007506:Iron-Sulfur Proteins; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex; D002734:Chlorophyll; C001785:chlorophyll P 700; D010837:Vitamin K 1; D000077194:Chlorophyll A