title: Temperature dependence of forward and reverse electron transfer from A1-, the reduced secondary electron acceptor in photosystem I.
abstract: Electron-transfer reactions following the formation of P700(+)A1- have been studied in isolated Photosystem I complexes from Synechococcus elongatus between 300 and 5 K by flash absorption spectroscopy. (1) In the range from 300 to 200 K, A1- is reoxidized by electron transfer to the iron-sulfur cluster FX. The rate slows down with decreasing temperature, corresponding to an activation energy of 220 +/- 20 meV in this temperature range. Analyzing the temperature dependence of the rate in terms of nonadiabatic electron-transfer theory, one obtains a reorganization energy of about 1 eV and an edge-to-edge distance between A1 and FX of about 8 A assuming the same distance dependence of the electron-transfer rate as in purple bacterial reaction centers. (2) At temperatures below 150 K, different fractions of PS I complexes attributed to frozen conformational substates can be distinguished. A detailed analysis at 77 K gave the following results: (a) In about 45%, flash-induced electron transfer is limited to the formation and decay of the secondary pair P700(+)A1-. The charge recombination occurs with a t1/2 of about 170 micros. (b) In about 20%, the state P700(+)FX- is formed and recombines with complex kinetics (t1/2 = 5-100 ms). (c) In about 35%, irreversible formation of P700(+)FA- or P700(+)FB- is possible. (3) The transition from efficient forward electron transfer at higher temperatures to heterogeneous photochemistry at low temperatures has been investigated in different glass-forming solvents. The yield of forward electron transfer to the iron-sulfur clusters decreases in a narrow temperature interval. The temperature of the half-maximal effect varies between different solvents and appears to be correlated with their liquid to glass transition. It is proposed that reorganization processes in the surroundings of the reactants which are required for the stabilization of the charge-separated state become arrested near the glass transition. This freezing of protein motions and/or solvent reorganization may affect electron-transfer reactions through changes in the free-energy gap and the reorganization energy. (4) The rate of charge recombination between P700(+) and A1- increases slightly (about 1.5-fold) when the temperature is decreased from 300 to 5 K. This charge recombination characterized by a large driving force is much less influenced by the solvent properties than the forward electron-transfer steps from A1- to FX and FA/B.
authors.affiliation: Max-Volmer-Institut für Biophysikalische Chemie und Biochemie, Technische Universität Berlin, Germany.
authors.forename: E
authors.initials: E
authors.lastname: Schlodder
authors.forename: K
authors.initials: K
authors.lastname: Falkenberg
authors.forename: M
authors.initials: M
authors.lastname: Gergeleit
authors.forename: K
authors.initials: K
authors.lastname: Brettel
mesh_terms: D003080:Cold Temperature; D000458:Cyanobacteria / Q000737:chemistry / Q000378:metabolism; D004579:Electron Transport; D006358:Hot Temperature; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D010084:Oxidation-Reduction; D010782:Photolysis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism; D013053:Spectrophotometry; D013696:Temperature
chemical_list: D007506:Iron-Sulfur Proteins; D045322:Photosynthetic Reaction Center Complex Proteins