@misc{oai:repo.qst.go.jp:00083940,
 author = {Masahiko, Taguchi and Shun, Sakuraba and Soon Chan, Wai and Hidetoshi, Kono and Masahiko, Taguchi and Shun, Sakuraba and Soon Chan, Wai and Hidetoshi, Kono},
 month = {Nov},
 note = {OaPAC is a photoactivated enzyme that forms a homodimer. It has two BLUF photoreceptor domains with long coiled-coil C-terminal helixes connecting to the catalytic domains. It is thought that during photoactivation, hydrogen bonding network between Tyr6, Gln48, and chromophore is disrupted, and keto-enol tautomerization of Gln48 occurs in the BLUF domain. However, it remains to be solved how the structural change in the BLUF domain propagates towards the catalytic domain. To investigate the mechanism, we performed QM/MM free energy calculations of the BLUF domain at dark and light states. In the light state, we observed a distinct flip of Trp90 nearby the C-terminal helix, causing the subsequent structural changes in the BLUF core and the C-terminal helix., 第59回日本生物物理学会年会},
 title = {Molecular insight into photoactivation of BLUF photoreceptor from QM/MM free energy calculation},
 year = {2021}
}