{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T04:49:31Z","timestamp":1789879771453,"version":"4.0.1"},"reference-count":31,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2008,11,17]],"date-time":"2008-11-17T00:00:00Z","timestamp":1226880000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Chemistry A European J"],"published-print":{"date-parts":[[2009,1,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>For the first time, the existence of a substrate adduct of a nickel superoxide dismutase (NiSOD) model, based on the first nine residues from the N terminus of the active form of <jats:italic>Streptomyces coelicolor<\/jats:italic> NiSOD, has been proven and the adduct has been isolated. This adduct is based on the cyanide anion (CN<jats:sup>\u2212<\/jats:sup>), as a substrate analogue of the superoxide anion (O<jats:sub>2<\/jats:sub><jats:sup>.\u2212<\/jats:sup>), and the nickel metallopeptide H\u2010HCDLPCGVY\u2010NH<jats:sub>2<\/jats:sub>\u2010Ni. Spectroscopic studies, including IR, UV\/Vis, and liquid\u2010 and solid\u2010state NMR spectroscopy, show a single nickel\u2010bound cyanide anion, which is embedded in the metallopeptide structure. This complex sheds new light on the question of whether the mode of action of the NiSOD enzyme is an inner\u2010 or outer\u2010sphere mechanism. Whereas discussion was previously biased in favor of an outer\u2010sphere electron\u2010transfer mechanism due to the fact that binding of cyanide or azide moieties to the nickel active site had never been observed, our results are a clear indication in favor of the inner\u2010sphere electron\u2010transfer mechanism for the disproportionation of the O<jats:sub>2<\/jats:sub><jats:sup>.\u2212<\/jats:sup> ion, whereby the substrate is attached to the Ni atom in the active site of the NiSOD.<\/jats:p>","DOI":"10.1002\/chem.200800870","type":"journal-article","created":{"date-parts":[[2008,11,17]],"date-time":"2008-11-17T08:35:20Z","timestamp":1226910920000},"page":"517-523","source":"Crossref","is-referenced-by-count":41,"title":["New Insight into the Mode of Action of Nickel Superoxide Dismutase by Investigating Metallopeptide Substrate 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