Characterization of Structure and Catalytic Activity of a Complex between Heme and an All Parallel-Stranded Tetrameric G-Quadruplex Formed from DNA/RNA Chimera Sequence d(TTA)r(GGG)dT

Access this Article


    • Neya Saburo
    • Department of Physical Chemistry, Graduate School of Pharmaceutical Sciences, Chiba University
    • Ishizuka Takumi
    • Division of Chemistry, Department of Medical Sciences, Faculty of Medicine, University of Miyazaki
    • Xu Yan
    • Division of Chemistry, Department of Medical Sciences, Faculty of Medicine, University of Miyazaki
    • Yamamoto Yasuhiko
    • Department of Chemistry, University of Tsukuba|Tsukuba Research Center for Energy Materials Science (TREMS), University of Tsukuba|Life Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba


<p>An all-parallel tetrameric G-quadruplex formed from a DNA/RNA chimera sequence, d(TTA)r(GGG)d(T) ([Chimera(7mer)]<sub>4</sub>), and its interaction with heme have been characterized. [Chimera(7mer)]<sub>4</sub> was found to be remarkably more stable compared with a G-quadruplex formed from its DNA counterpart d(TTAGGGT), ([DNA(7mer)]<sub>4</sub>), despite the structural similarity between them, and the increased stability of [Chimera(7mer)]<sub>4</sub> is likely to be due to the formation of interstrand hydrogen bonds between the rG5 2′-OH and rG6 amino NH<sub>2</sub> groups. Heme bound selectively to the 3′-terminal G-quartet (rG6 G-quartet) in the rG6dT7 step of [Chimera(7mer)]<sub>4</sub> did not exhibit the heme orientational disorder resulting from the formation of two isomers possessing heme orientations differing by 180° rotation about the pseudo-<i>C</i><sub>2</sub> axis, with respect to the interacting G-quartet, although it is a general feature of heme-DNA complexes. In a complex between heme and [Chimera(7mer)]<sub>4</sub>, the predominance of one isomer in the heme orientational disorder over the other one is possibly due to contacts between the rG6 2′-OH group of the G-quartet and heme side chain ones. Peroxidase activity of heme bound to a G-quartet was found to be independent of the presence of the 2′-OH group in the ribose of the constituent units of the G-quartet.</p>


  • Bulletin of the Chemical Society of Japan

    Bulletin of the Chemical Society of Japan 93(5), 621-629, 2020

    The Chemical Society of Japan


  • NII Article ID (NAID)
  • Text Lang
  • ISSN
  • Data Source
Page Top