Tietze, D. ; Breitzke, H. ; Imhof, D. ; Kothe, E. ; Weston, J. ; Buntkowsky, G. (2009)
New Insight into the Mode of Action of Nickel Superoxide Dismutase by Investigating Metallopeptide Substrate Models.
In: Chemistry-a European Journal, 15 (2)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
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 Streptomyces coelicolor NiSOD. has been proven and the adduct has been isolated. This adduct is based on the evanide anion (CN). as a substrate analogue of the superoxide anion (O(2)(center dot-)). and the nickel metallopeptide H-HCDLPCGVY-NH(2)-Ni. Spectroscopic Studies. including IR. UV/Vis, and liquid- and solid-state NMR spectroscopy, show a single nickel-bound eyanide 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- or outer-sphere mechanism. Whereas discussion was previously biased in favor of an outer-sphere electron-transfer mechanism due to the fact that binding Of Cyanide or azide moieties to the nickel active site had never been observed. our results arc a clear indication in favor of the inner-sphere electron-transfer mechanism for the disproportionation of the O(2)(center dot-) ion, whereby the substrate is attached to the Ni atom in the active site of the NiSOD.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2009 |
| Autor(en): | Tietze, D. ; Breitzke, H. ; Imhof, D. ; Kothe, E. ; Weston, J. ; Buntkowsky, G. |
| Art des Eintrags: | Bibliographie |
| Titel: | New Insight into the Mode of Action of Nickel Superoxide Dismutase by Investigating Metallopeptide Substrate Models |
| Sprache: | Englisch |
| Publikationsjahr: | 2009 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Chemistry-a European Journal |
| Jahrgang/Volume einer Zeitschrift: | 15 |
| (Heft-)Nummer: | 2 |
| URL / URN: | http://apps.webofknowledge.com/full_record.do?product=WOS&se... |
| Kurzbeschreibung (Abstract): | 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 Streptomyces coelicolor NiSOD. has been proven and the adduct has been isolated. This adduct is based on the evanide anion (CN). as a substrate analogue of the superoxide anion (O(2)(center dot-)). and the nickel metallopeptide H-HCDLPCGVY-NH(2)-Ni. Spectroscopic Studies. including IR. UV/Vis, and liquid- and solid-state NMR spectroscopy, show a single nickel-bound eyanide 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- or outer-sphere mechanism. Whereas discussion was previously biased in favor of an outer-sphere electron-transfer mechanism due to the fact that binding Of Cyanide or azide moieties to the nickel active site had never been observed. our results arc a clear indication in favor of the inner-sphere electron-transfer mechanism for the disproportionation of the O(2)(center dot-) ion, whereby the substrate is attached to the Ni atom in the active site of the NiSOD. |
| Freie Schlagworte: | enzyme catalysis nickel substrate binding superoxide dismutase reaction-mechanism crystal-structure streptomyces site coordination amine/amide ni |
| Zusätzliche Informationen: | 394ZK Times Cited:22 Cited References Count:31 |
| Fachbereich(e)/-gebiet(e): | 07 Fachbereich Chemie 07 Fachbereich Chemie > Eduard Zintl-Institut > Fachgebiet Physikalische Chemie |
| Hinterlegungsdatum: | 27 Okt 2014 20:51 |
| Letzte Änderung: | 29 Mai 2019 12:56 |
| PPN: | |
| Export: | |
| Suche nach Titel in: | TUfind oder in Google |
 |
Frage zum Eintrag |
Optionen (nur für Redakteure)
 |
Redaktionelle Details anzeigen |
Drucken
Impressum