| Autor: |
Sakashita N; Department of Applied Chemistry, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8654, Japan., Ishikita H; Department of Applied Chemistry, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8654, Japan and Research Center for Advanced Science and Technology, The University of Tokyo, 4-6-1 Komaba, Meguro-ku, Tokyo, 153-8904, Japan. ksaito@appchem.t.u-tokyo.ac.jp., Saito K; Department of Applied Chemistry, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8654, Japan and Research Center for Advanced Science and Technology, The University of Tokyo, 4-6-1 Komaba, Meguro-ku, Tokyo, 153-8904, Japan. ksaito@appchem.t.u-tokyo.ac.jp. |
| Abstrakt: |
In the water-splitting enzyme photosystem II (PSII), the proton is released from the catalytic site and transferred to the protein bulk surface via the proton-relay mechanism. Proton transfer occurs in a proton-conducting channel consisting of a series of water molecules connected by hydrogen-bonded (H-bonded) chains. The water-transport protein aquaporin (AQP) also contains a water chain with structure similar to that of the PSII proton channel, although the water chain does not transport protons. We compared the PSII proton channel with the AQP water channel from the following standpoints: (1) the energetics of proton transfer based on crystal structures obtained from quantum mechanical/molecular mechanical calculations, and (2) fluctuations in water molecules obtained from molecular dynamics simulations. The results showed that residues facing the channel and acting as H-bonded partners of water molecules predominantly determined the proton-transfer ability. In PSII, the water chain is surrounded by H-bond acceptors (e.g., carbonyl groups), and the water chain transports protons where the water molecules are rigidly fixed. In AQP, the water chain is surrounded by hydrophobic sidechains or H-bond donors (e.g., NH2 groups), and it does not transport protons where the water molecules are flexible and fluctuating. |
