Tietze, D. and Tischler, M. and Voigt, S. and Imhof, D. and Ohlenschlager, O. and Görlach, M. and Buntkowsky, G. (2010):
Development of a Functional cis-Prolyl Bond Biomimetic and Mechanistic Implications for Nickel Superoxide Dismutase.
16, In: Chemistry-a European Journal, (25), pp. 7572-7578, [Online-Edition: http://apps.webofknowledge.com/full_record.do?product=WOS&se...],
[Article]
Abstract
During recent years several peptide-based Ni superoxide dismutase (NiSOD) models have been developed. These NiSOD models show an important structural difference compared to the native NiSOD enzyme, which could cause a completely different mechanism of superoxide dismutation. In the native enzyme the peptide bond between Leu4 and Pro5 is cis-configured, while the NiSOD models exhibit a trans-configured peptide bond between these two residues. To shed light on how the configuration of this single peptide bond influences the activity of the NiSOD model peptides, a new cis-prolyl bond surrogate was developed. As surrogate we chose a leucine/alanine-based disubstituted 1,2,3-triazole, which was incorporated into the NiSOD model peptide replacing residues Leu4 and Pro5. The yielded 1,5-disubstituted triazole nickel peptide exhibited high SOD activity, which was approximately the same activity as its parent trans-configured analogue. Hence, the conformation of the prolyl peptide bond apparently has of minor importance for the catalytic activity of the metallopeptides as postulated in literature. Furthermore, it is shown that the triazole metallopeptide is forming a stable cyanide adduct as a substrate analogue model complex.
| Item Type: | Article |
|---|---|
| Erschienen: | 2010 |
| Creators: | Tietze, D. and Tischler, M. and Voigt, S. and Imhof, D. and Ohlenschlager, O. and Görlach, M. and Buntkowsky, G. |
| Title: | Development of a Functional cis-Prolyl Bond Biomimetic and Mechanistic Implications for Nickel Superoxide Dismutase |
| Language: | English |
| Abstract: | During recent years several peptide-based Ni superoxide dismutase (NiSOD) models have been developed. These NiSOD models show an important structural difference compared to the native NiSOD enzyme, which could cause a completely different mechanism of superoxide dismutation. In the native enzyme the peptide bond between Leu4 and Pro5 is cis-configured, while the NiSOD models exhibit a trans-configured peptide bond between these two residues. To shed light on how the configuration of this single peptide bond influences the activity of the NiSOD model peptides, a new cis-prolyl bond surrogate was developed. As surrogate we chose a leucine/alanine-based disubstituted 1,2,3-triazole, which was incorporated into the NiSOD model peptide replacing residues Leu4 and Pro5. The yielded 1,5-disubstituted triazole nickel peptide exhibited high SOD activity, which was approximately the same activity as its parent trans-configured analogue. Hence, the conformation of the prolyl peptide bond apparently has of minor importance for the catalytic activity of the metallopeptides as postulated in literature. Furthermore, it is shown that the triazole metallopeptide is forming a stable cyanide adduct as a substrate analogue model complex. |
| Journal or Publication Title: | Chemistry-a European Journal |
| Volume: | 16 |
| Number: | 25 |
| Uncontrolled Keywords: | biomimetic synthesis enzyme catalysis nickel superoxide dismutase delta-conotoxin evia streptomyces-seoulensis trans isomerization molecular timer site ni coordination amine/amide insight alkynes |
| 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: | 629RC Times Cited:13 Cited References Count:34 |
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