TY - JOUR
T1 - Theoretical studies on the magnetic interaction and reversible dioxygen binding of the active site in hemocyanin
AU - Takano, Yu
AU - Kubo, Shigehiro
AU - Onishi, Taku
AU - Isobe, Hiroshi
AU - Yoshioka, Yasunori
AU - Yamaguchi, Kizashi
N1 - Funding Information:
This work has been supported by a Grant-in-Aid for Scientific Research on Priority Areas (No. 10149105 `Metal Assembled Complexes') from the Ministry of Education, Science, Sports and Culture, Japan. Y.Y. was supported by ACT (Research and Development for Applying Advanced Computational Science and Technology) of Japan Science and Technology Corporation (JST), and Y.T. was also supported by Research Fellowships of the Japan Society for the Promotion of Science for Young Scientists.
PY - 2001/3/2
Y1 - 2001/3/2
N2 - We have investigated the magnetic interaction, the shape of the whole potential energy surface, and the electronic structure of realistic models of the active site in hemocyanin for the reversible dioxygen binding by UHF and DFT calculations. The results are discussed in relation to the effective exchange integrals and the charge and spin density distributions as well as the shape and symmetry of natural orbitals. The superexchange interaction via bridging dioxygen accounts for the strong antiferromagnetic interaction between the two copper ions. The shapes of the potential energy curve suggest that the structural change of hemocyanin controls dioxygen binding.
AB - We have investigated the magnetic interaction, the shape of the whole potential energy surface, and the electronic structure of realistic models of the active site in hemocyanin for the reversible dioxygen binding by UHF and DFT calculations. The results are discussed in relation to the effective exchange integrals and the charge and spin density distributions as well as the shape and symmetry of natural orbitals. The superexchange interaction via bridging dioxygen accounts for the strong antiferromagnetic interaction between the two copper ions. The shapes of the potential energy curve suggest that the structural change of hemocyanin controls dioxygen binding.
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U2 - 10.1016/S0009-2614(01)00067-7
DO - 10.1016/S0009-2614(01)00067-7
M3 - Article
AN - SCOPUS:0001569263
SN - 0009-2614
VL - 335
SP - 395
EP - 403
JO - Chemical Physics Letters
JF - Chemical Physics Letters
IS - 5-6
ER -