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Single\u2010crystal X\u2010ray diffraction studies have revealed a highly distorted trigonal\u2010bipyramidal structure for <jats:bold>1<\/jats:bold> (<jats:italic>\u03c4<\/jats:italic> = 0.68) and an almost perfect trigonal\u2010bipyramidal geometry for <jats:bold>2<\/jats:bold> (<jats:italic>\u03c4<\/jats:italic> = 0.92). DNA binding studies, which were performed by thermal denaturation, viscometry, fluorescence spectroscopy, and cyclic voltammetry, indicated a partial intercalation of <jats:bold>1<\/jats:bold> with <jats:italic>K<\/jats:italic><jats:sub>app<\/jats:sub> = 2.45\u2009\u00d7\u200910<jats:sup>6<\/jats:sup> <jats:sc>M<\/jats:sc><jats:sup>\u20131<\/jats:sup>. The nuclease activity of <jats:bold>1<\/jats:bold> was investigated upon photoirradiation, with ascorbate\/H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub> as the activating agent, and also in the absence of any external reagent. In all cases, <jats:bold>1<\/jats:bold> was able to perform DNA cleavage, and its nuclease efficiency varied in the order ascorbate\/H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub> &gt; photoirradiation &gt; without external cofactors. Mechanistic investigations suggest an oxidative cleavage of DNA involving reactive oxygen species (ROS). 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