Photosystem II (PSII) has two symmetrically located, redox-active tyrosine residues, YZ and YD. Whereas YZ mediates the electron transfer from the water-oxidizing center to P680 in the main electron transfer pathway, YD functions as a peripheral electron donor to P680. To understand the mechanism of this functional difference between YZ and YD, it is essential to know where the proton is transferred upon its oxidation in the proton-coupled electron transfer process. In this study, we used Fourier transform infrared (FTIR) spectroscopy to examine whether the proton from YD is released from the protein into the bulk. The proton detection method previously used for water oxidation in PSII [Suzuki et al. (2009) J. Am. Chem. Soc. 131, 7849-7857] was applied to YD; a proton released into the bulk upon YD oxidation was trapped by a high-concentration Mes buffer, and the protonation reaction of Mes was monitored by FTIR difference spectroscopy. It was shown that 0.84 ± 0.10 protons are released into the bulk by oxidation of YD in one PSII center. This result indicates that the proton of YD is not transferred to the neighboring D2-His198 but is released from the protein; this is in sharp contrast to the YZ reaction, in which a proton is transferred to D1-His190 through a strong hydrogen bond. This functional difference is caused by differences in the hydrogen-bonded structures of YD and YZ, which are determined by the hydrogen bond partners at the Nπ sites of these His residues, i.e., D2-Arg294 and D1-Asn298, which function as a hydrogen bond donor and acceptor, respectively. This FTIR spectroscopy result supports the recent theoretical prediction [Saito et al. (2013) Proc. Natl. Acad. Sci. U.S.A. 110, 7690-7695] based on the X-ray crystallographic structure of PSII and explains the different rates of the redox reactions of YD and YZ.
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