Temperature dependence of forward and reverse electron transfer from A1-, the reduced secondary electron acceptor in photosystem I

Biochemistry
E SchlodderKlaus Brettel

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). ...Continue Reading

References

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