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Spin-inversion mechanisms in O2 binding to a model heme complex revisited by density function theory calculations.

Authors
  • Saito, Kohei1
  • Watabe, Yuya1
  • Fujihara, Takashi1
  • Takayanagi, Toshiyuki1
  • Hasegawa, Jun-Ya2
  • 1 Department of Chemistry, Saitama University, Shimo-Okubo 255, Sakura-ku, Saitama City, Saitama, 338-8570, Japan. , (Japan)
  • 2 Instituteof Catalysis, Hokkaido University, Kita 21, Nishi 10, Kita-ku, Sapporo, Hokkaido, 001-0021, Japan. , (Japan)
Type
Published Article
Journal
Journal of Computational Chemistry
Publisher
Wiley (John Wiley & Sons)
Publication Date
Apr 30, 2020
Volume
41
Issue
11
Pages
1130–1138
Identifiers
DOI: 10.1002/jcc.26159
PMID: 32020659
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Spin-inversion mechanisms in O2 binding to a model heme complex, consisting of Fe(II)-porphyrin and imidazole, were investigated using density-functional theory calculations. First, we applied the recently proposed mixed-spin Hamiltonian method to locate spin-inversion structures between different total spin multiplicities. Nine spin-inversion structures were successfully optimized for the singlet-triplet, singlet-quintet, triplet-quintet, and quintet-septet spin-inversion processes. We found that the singlet-triplet spin-inversion points are located around the potential energy surface region at short Fe-O distances, whereas the singlet-quintet and quintet-septet spin-inversion points are located at longer Fe-O distances. This suggests that both narrow and broad crossing models play roles in O2 binding to the Fe-porphyrin complex. To further understand spin-inversion mechanisms, we performed on-the-fly Born-Oppenheimer molecular dynamics calculations. The reaction coordinates, which are correlated to the spin-inversion dynamics between different spin multiplicities, are also discussed. © 2020 Wiley Periodicals, Inc.

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