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DNA binding and nuclease activity of cationic iron(IV) and manganese(III) corrole complexes
Author(s) -
Zhang Yang,
Wen Jinyan,
Wang Xiangli,
Mahmood Mian HR,
Liu ZeYu,
Wang Hui,
Ji Liangnian,
Liu Haiyang
Publication year - 2014
Publication title -
applied organometallic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.53
H-Index - 71
eISSN - 1099-0739
pISSN - 0268-2605
DOI - 10.1002/aoc.3163
Subject(s) - corrole , chemistry , cationic polymerization , intercalation (chemistry) , dna , manganese , dimer , circular dichroism , nuclease , monomer , photochemistry , singlet oxygen , stereochemistry , crystallography , polymer chemistry , inorganic chemistry , oxygen , biochemistry , polymer , organic chemistry
Cationic meso (4‐ N ‐methylpyridyl)‐based metallocorroles, μ‐oxo iron corrole dimer ( 1b ) and manganese corrole monomer ( 2b ), were synthesized and characterized. The interactions of these two metal corrole complexes with CT‐DNA were studied by UV–visible, fluorescence and circular dichroism spectroscopic methods, as well as by viscosity measurements. The results revealed that 1b interacts with CT‐DNA in a difunctional binding mode, i.e. non‐classical intercalation and outside groove binding with H‐aggregation, while 2b can interact with CT‐DNA via an outside groove binding mode only. The binding constants K b of 1b and 2b were 4.71 × 10 5 m −1 and 2.17 × 10 5 m −1 , respectively, indicating that 1b can bind more tightly to CT‐DNA than 2b . Furthermore, both complexes may cleave the supercoiled plasmid DNA efficiently in the presence of hydrogen peroxide or tert ‐butyl hydroperoxide (TBHP), albeit 1b exhibited a little higher efficiency. The inhibitor tests suggested that singlet oxygen and high‐valent (oxo)iron(VI) corrole or (oxo)manganese(V) corrole might be the active intermediates responsible for the oxidative DNA scission. Copyright © 2014 John Wiley & Sons, Ltd.