Density functional study of porphyrin distortion effects on redox potential of heme
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- Yasuhiro Imada
- Research Center for State‐of‐the‐Art Functional Protein Analysis, Institute for Protein Research, Osaka University, 3‐2 Yamadaoka Suita Osaka 565‐0871 Japan
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- Haruki Nakamura
- Research Center for State‐of‐the‐Art Functional Protein Analysis, Institute for Protein Research, Osaka University, 3‐2 Yamadaoka Suita Osaka 565‐0871 Japan
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- Yu Takano
- Research Center for State‐of‐the‐Art Functional Protein Analysis, Institute for Protein Research, Osaka University, 3‐2 Yamadaoka Suita Osaka 565‐0871 Japan
書誌事項
- 公開日
- 2017-09-02
- 資源種別
- journal article
- 権利情報
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- http://onlinelibrary.wiley.com/termsAndConditions#vor
- DOI
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- 10.1002/jcc.25058
- 公開者
- Wiley
この論文をさがす
説明
<jats:p>Heme is involved in various biochemical roles in hemoproteins. In the present study, the effect of heme distortion on the redox potential was systematically investigated with density functional calculations. We focused on the ruffled and saddled distortions of heme, which correspond to the two lowest‐frequency normal modes. Our computations demonstrated that the ruffled distortion tended to reduce the redox potential of heme and that the transition of the electronic configuration occurred from (d<jats:sub>xz</jats:sub>, d<jats:sub>yz</jats:sub>)<jats:sup>3</jats:sup>(d<jats:sub>xy</jats:sub>)<jats:sup>2</jats:sup> to (d<jats:sub>xz</jats:sub>, d<jats:sub>yz</jats:sub>)<jats:sup>4</jats:sup>(d<jats:sub>xy</jats:sub>)<jats:sup>1</jats:sup>. In contrast, the saddled distortion had a tendency toward an increase in the redox potential, and no transition of the electronic configuration occurred. In experiments, these tendencies were found in the relationship between with the heme distortions and the redox potentials in cytochrome <jats:italic>c</jats:italic><jats:sub>3</jats:sub>. © 2017 Wiley Periodicals, Inc.</jats:p>
収録刊行物
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- Journal of Computational Chemistry
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Journal of Computational Chemistry 39 (3), 143-150, 2017-09-02
Wiley
