論文

査読有り
2018年10月

Structures and Catalytic Activities of Complexes between Heme and All Parallel-Stranded Monomeric G-Quadruplex DNAs

Biochemistry
  • Yamamoto, Yasuhiko
  • ,
  • Araki, Haruka
  • ,
  • Shinomiya, Ryosuke
  • ,
  • Hayasaka, Kosuke
  • ,
  • Nakayama, Yusaku
  • ,
  • Ochi, Kentaro
  • ,
  • Shibata, Tomokazu
  • ,
  • Momotake, Atsuya
  • ,
  • Ohyama, Takako
  • ,
  • Hagihara, Masaki
  • ,
  • Hemmi, Hikaru

57
41
開始ページ
5938
終了ページ
5948
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1021/acs.biochem.8b00792
出版者・発行元
AMER CHEMICAL SOC

Heme in its ferrous and ferric states [heme(Fe) and heme(Fe), respectively] binds selectively to the 3'-terminal G-quartet of all parallel-stranded monomeric G-quadruplex DNAs formed from inosine(I)-containing sequences, i.e., d(TAGGGTGGGTTGGGTGIG) DNA(18mer) and d(TAGGGTGGGTTGGGTGIGA) DNA(18mer/A), through a π-π stacking interaction between the porphyrin moiety of the heme and the G-quartet, to form 1:1 complexes [heme-DNA(18mer) and heme-DNA(18mer/A) complexes, respectively]. These complexes exhibited enhanced peroxidase activities, compared with that of heme(Fe) alone, and the activity of the heme(Fe)-DNA(18mer/A) complex was greater than that of the heme(Fe)-DNA(18mer) one, indicating that the 3'-terminal A of the DNA sequence acts as an acid-base catalyst that promotes the catalytic reaction. In the complexes, a water molecule (HO) at the interface between the heme and G-quartet is coordinated to the heme Fe atom as an axial ligand and possibly acts as an electron-donating ligand that promotes heterolytic peroxide bond cleavage of hydrogen peroxide bound to the heme Fe atom, trans to the HO, for the generation of an active species. The intermolecular nuclear Overhauser effec

リンク情報
DOI
https://doi.org/10.1021/acs.biochem.8b00792
ID情報
  • DOI : 10.1021/acs.biochem.8b00792
  • ISSN : 1520-4995

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