Role for bound water and CH-π aromatic interactions in photosynthetic electron transfer

Photosystem I (PSI) is one of two photosynthetic reaction centers present in plants, algae, and cyanobacteria. and catalyzes the reduction of ferredoxin and the oxidation of cytochrome c or plastocyanin. The PSI primary chlorophyll donor, which is oxidized in the primary electron-transfer events, is a heterodimer of chl a and a' called P-700. It has been suggested that protein relaxation accompanies light-induced electron transfer in this reaction center (Dashdorj, N.; Xu, W.; Martinsson, P.; Chitnis, P. R.; Savikhin, S. Biophys. J. 2004, 86, 3121. Kim, S.; Sacksteder, C. A.; Bixby, K. A.; Barry, B. A. Biochemistry 2001, 40,15384). To investigate the details of electron transfer and relaxation events in PSI, we have employed several experimental approaches. First, we report a pH-dependent viscosity effect on P-700(+) reduction; this result suggests a role for proton transfer in the PSI electron-transfer reactions. Second, we find that changes in hydration alter the rate of P-700(+) reduction and the interactions of P-700 with the protein environment. This result suggests a role for bound water in electron transfer to P-700(+). Third, we present evidence that deuteration of the tyrosine aromatic side chain perturbs the vibrational spectrum, associated with P-700(+) reduction. We attribute this result to a linkage between CH-pi interactions and electron transfer to P-700(+).