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DNA Binding and Oxidative Cleavage by a Water‐soluble Carboxyl Manganese(III) Corrole
Author(s) -
Zhang Yang,
Wang Qi,
Wen Jinyan,
Wang Xiangli,
Mahmood Mian HR,
Ji Liangnian,
Liu Haiyang
Publication year - 2013
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.201300488
Subject(s) - corrole , chemistry , dna , manganese , radical , hydrogen peroxide , nuclease , cleavage (geology) , singlet oxygen , photochemistry , hydroxyl radical , oxidative phosphorylation , stereochemistry , oxygen , biochemistry , organic chemistry , geotechnical engineering , fracture (geology) , engineering
The interaction of calf thymus DNA (CT DNA) and water‐soluble manganese corrole, 5,10,15‐tris(4‐carboxyphenyl)corrolatomanganese(III) (Mn III TCPC) has been studied by absorption spectra, fluorescence spectra and CD spectra, as well as by viscosity measurements. Results revealed that this manganese corrole binds to CT DNA via an outside groove binding mode with intrinsic binding constant K b of 4.67×10 4 L·mol− 1 . DNA cleavage activities of Mn III TCPC in the presence of various oxidants were also investigated. Mn III TCPC can cleave the supercoiled plasmid pBR322 DNA to both nicked and linear form in the presence of hydrogen peroxide or tert ‐BuOOH, while no nuclease activity was observed by using KHSO 5 as oxidant. Inhibitor tests revealed that hydroxyl radicals or singlet oxygen was not involved in Mn III TCPC mediated DNA oxidative cleavage. It is suggested that (oxo)manganese(V) corrole is the possibly active intermediate in this oxidative cleavage reactions.