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Here, we have investigated the interactions of Ru\u2010cymene complexes with a zinc\u2010finger protein NCp7, aiming to understand the effects of various ligands on the reaction. Five different binding modes were observed on selected Ru\u2010complexes. Ru\u2010cymene complex can bind to proteins through either noncovalent binding alone or through a combination of covalent and noncovalent binding modes. Moreover, the noncovalent interaction can promote the coordination of Ru<jats:sup>II<\/jats:sup> to NCp7, resulting synergistic effects of the different ligands. The binding of Ru(Cym) complexes leads to dysfunction of NCp7 through zinc\u2010ejection and structural perturbation. These results indicate that the reactivity of Ru\u2010complexes can be modulated by ligands through different approaches, which could be closely correlated to their different therapeutic effects.<\/jats:p>","DOI":"10.1002\/chem.201902434","type":"journal-article","created":{"date-parts":[[2019,8,6]],"date-time":"2019-08-06T03:44:22Z","timestamp":1565063062000},"page":"12789-12794","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Covalent versus Noncovalent Binding of Ruthenium \u03b7<sup>6<\/sup>\u2010<i>p<\/i>\u2010Cymene Complexes to Zinc\u2010Finger Protein NCp7"],"prefix":"10.1002","volume":"25","author":[{"given":"Yaping","family":"Sheng","sequence":"first","affiliation":[{"name":"CAS Key Laboratory of Soft Matter Chemistry Department of Chemistry University of Science and Technology of China  Hefei Anhui 230026 P.R. 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