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New Insight into the Mode of Action of Nickel Superoxide Dismutase by Investigating Metallopeptide Substrate Models

Tietze, D. and Breitzke, H. and Imhof, D. and Kothe, E. and Weston, J. and Buntkowsky, G. (2009):
New Insight into the Mode of Action of Nickel Superoxide Dismutase by Investigating Metallopeptide Substrate Models.
15, In: Chemistry-a European Journal, (2), pp. 517-523. [Article]

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.

Item Type: Article
Erschienen: 2009
Creators: Tietze, D. and Breitzke, H. and Imhof, D. and Kothe, E. and Weston, J. and Buntkowsky, G.
Title: New Insight into the Mode of Action of Nickel Superoxide Dismutase by Investigating Metallopeptide Substrate Models
Language: English
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.

Journal or Publication Title: Chemistry-a European Journal
Volume: 15
Number: 2
Uncontrolled Keywords: enzyme catalysis nickel substrate binding superoxide dismutase reaction-mechanism crystal-structure streptomyces site coordination amine/amide ni
Divisions: 07 Department of Chemistry
07 Department of Chemistry > Physical Chemistry
Date Deposited: 27 Oct 2014 20:51
Official URL: http://apps.webofknowledge.com/full_record.do?product=WOS&se...
Additional Information:

394ZK Times Cited:22 Cited References Count:31

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