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Study on dioxygen reduction by mutational modifications of the hydrogen bond network leading from bulk water to the trinuclear copper center in bilirubin oxidase
http://hdl.handle.net/2297/40208
http://hdl.handle.net/2297/4020860fd298c-9d2d-43d4-b365-269b49c03bb7
名前 / ファイル | ライセンス | アクション |
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SC-PR-SAKURAI-T-767.pdf (598.8 kB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2017-10-03 | |||||
タイトル | ||||||
タイトル | Study on dioxygen reduction by mutational modifications of the hydrogen bond network leading from bulk water to the trinuclear copper center in bilirubin oxidase | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
著者 |
Morishita, Hirotoshi
× Morishita, Hirotoshi× Kurita, Daisuke× Kataoka, Kunishige× Sakurai, Takeshi |
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書誌情報 |
Biochemical and Biophysical Research Communications 巻 450, 号 1, p. 767-772, 発行日 2014-07-18 |
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ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0006-291X | |||||
NCID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA00564395 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1016/j.bbrc.2014.06.052 | |||||
出版者 | ||||||
出版者 | Academic Press / Elsevier | |||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | The hydrogen bond network leading from bulk water to the trinuclear copper center in bilirubin oxidase is constructed with Glu463 and water molecules to transport protons for the four-electron reduction of dioxygen. Substitutions of Glu463 with Gln or Ala were attributed to virtually complete loss or significant reduction in enzymatic activities due to an inhibition of the proton transfer steps to dioxygen. The single turnover reaction of the Glu463Gln mutant afforded the highly magnetically interacted intermediate II (native intermediate) with a broad g = 1.96 electron paramagnetic resonance signal detectable at cryogenic temperatures. Reactions of the double mutants, Cys457Ser/Glu463Gln and Cys457Ser/Glu463Ala afforded the intermediate I (peroxide intermediate) because the type I copper center to donate the fourth electron to dioxygen was vacant in addition to the interference of proton transport due to the mutation at Glu463. The intermediate I gave no electron paramagnetic resonance signal, but the type II copper signal became detectable with the decay of the intermediate I. Structural and functional similarities between multicopper oxidases are discussed based on the present mutation at Glu463 in bilirubin oxidase. © 2014 Elsevier Inc. All rights reserved. | |||||
著者版フラグ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa |