Trehalose-induced local distorsions in iron proteins

The coupling between electron transfer and protein dynamics in the bacterial photosynthetic reaction center: trapping of conformational substates in room temperature amorphous matrices

The photosynthetic reaction center (RC) from purple bacteria is becoming a prototype in exploring the coupling between internal protein motions and long-range electron transfer (ET). This interplay has been extensively investigated by hampering RC substate interconversion and relaxations at low temperatures (McMahon et al., 1998, Biophys. J. 74, 2567). As a complementary approach for limiting RC dynamics at room temperature we embedded the protein within a dehydrated trehalose matrix. Spectroscopic studies and molecular dynamics simulations performed on myoglobin/trehalose/water systems have shown that the nonharmonic contributions to the protein motions (attributed to thermal fluctuations …