Synthesis, Crystal Structures and DNA-Cleaving Activities of [Cemp]₂[MCl₄] (Cemp=N-Carbethoxymethyl-1,10-phenanthrolinium, M=Cu[Ⅱ], Zn[Ⅱ], Co[Ⅱ], Ni[Ⅱ] and Mn[Ⅱ])
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- Chen Ming-Zhen
- School of Pharmaceutical Sciences, Southern Medical University
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- Chen Ming
- School of Pharmaceutical Sciences, Southern Medical University
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- Zhou Chun-Qiong
- School of Pharmaceutical Sciences, Southern Medical University
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- Lin Wei-Er
- School of Pharmaceutical Sciences, Southern Medical University
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- Chen Jin-Xiang
- School of Pharmaceutical Sciences, Southern Medical University
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- Chen Wen-Hua
- School of Pharmaceutical Sciences, Southern Medical University
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- Jiang Zhi-Hong
- School of Pharmaceutical Sciences, Southern Medical University Macau Institute for Applied Research in Medicine and Health, Macau University of Science and Technology
書誌事項
- タイトル別名
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- Synthesis, Crystal Structures and DNA-Cleaving Activities of [Cemp]<sub>2</sub>[MCl<sub>4</sub>] (Cemp=<i>N</i>-Carbethoxymethyl-1,10-phenanthrolinium, M=Cu<sup>II</sup>, Zn<sup>II</sup>, Co<sup>II</sup>, Ni<sup>II</sup> and Mn<sup>II</sup>)
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N-Carbethoxymethyl-1,10-phenanthrolinium bromide (CempBr) and its five ionic metal complexes, [Cemp]2[MCl4] where M=CuII (1), ZnII (2), CoII (3), NiII (4) and MnII (5) were synthesized and fully characterized. Complexes 1–5 have similar structures, and consist of isolated [Cemp]+ cations and [MCl4]2− anions in which there are no obvious interactions between the oxygen or nitrogen donor atoms in [Cemp]+ and the metal center in [MCl4]2−. Agarose gel electrophoresis studies on the cleavage of plasmid pBR322 DNA by complexes 1–5 indicated that complex 1 was capable of efficiently cleaving DNA under physiological conditions, most probably via an oxidative mechanism. Kinetic assay of complex 1 afforded the maximal catalytic rate constant kmax of 0.55 h−1 and Michaelis constant KM of 47.6 µM, respectively, which gives about 1.5×107-fold rate acceleration over uncatalyzed cleavage of supercoiled DNA. Ethidium bromide displacement experiments indicated that complex 1 had a binding affinity of (1.58±1.12)×106 M−1 toward calf-thymus DNA, 20–100-fold higher than those shown by CempBr and complexes 2–5. The high cleaving efficacy of complex 1 is thought to be due to the efficient catalysis of the copper(II)-coordinated center and the efficient binding of the quaternized 1,10-phenanthroline cation to DNA.
収録刊行物
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- CHEMICAL & PHARMACEUTICAL BULLETIN
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CHEMICAL & PHARMACEUTICAL BULLETIN 61 (7), 714-721, 2013
公益社団法人 日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1390001204177541120
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- NII論文ID
- 130003360798
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- NII書誌ID
- AA00602100
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- COI
- 1:STN:280:DC%2BC3sjmsV2jsg%3D%3D
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- ISSN
- 13475223
- 00092363
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- NDL書誌ID
- 024644853
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- PubMed
- 23812396
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可