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New insights into the mechanism of nickel superoxide degradation from studies of model peptides

Tietze, Daniel ; Sartorius, Jana ; Koley Seth, Banabithi ; Herr, Kevin ; Heimer, Pascal ; Imhof, Diana ; Mollenhauer, Doreen ; Buntkowsky, Gerd (2017)
New insights into the mechanism of nickel superoxide degradation from studies of model peptides.
In: Scientific Reports, 7 (1)
doi: 10.1038/s41598-017-17446-3
Artikel, Bibliographie

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Kurzbeschreibung (Abstract)

A series of small, catalytically active metallopeptides, which were derived from the nickel superoxide dismutase (NiSOD) active site were employed to study the mechanism of superoxide degradation especially focusing on the role of the axial imidazole ligand. In the literature, there are contradicting propositions about the catalytic importance of the N-terminal histidine. Therefore, we studied the stability and activity of a set of eight NiSOD model peptides, which represent the major model systems discussed in the literature to date, yet differing in their length and their Ni-coordination. UV-Vis-coupled stopped-flow kinetic measurements and mass spectrometry analysis unveiled their high oxidation sensitivity in the presence of oxygen and superoxide resulting into a much faster Ni(II)-peptide degradation for the amine/amide Ni(II) coordination than for the catalytically inactive bis-amidate Ni(II) coordination. With respect to these results we determined the catalytic activities for all NiSOD mimics studied herein, which turned out to be in almost the same range of about 2 × 106 M−1 s−1. From these experiments, we concluded that the amine/amide Ni(II) coordination is clearly the key factor for catalytic activity. Finally, we were able to clarify the role of the N-terminal histidine and to resolve the contradictory literature propositions, reported in previous studies.

Typ des Eintrags: Artikel
Erschienen: 2017
Autor(en): Tietze, Daniel ; Sartorius, Jana ; Koley Seth, Banabithi ; Herr, Kevin ; Heimer, Pascal ; Imhof, Diana ; Mollenhauer, Doreen ; Buntkowsky, Gerd
Art des Eintrags: Bibliographie
Titel: New insights into the mechanism of nickel superoxide degradation from studies of model peptides
Sprache: Englisch
Publikationsjahr: 2017
Ort: Darmstadt
Verlag: Springer
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Scientific Reports
Jahrgang/Volume einer Zeitschrift: 7
(Heft-)Nummer: 1
DOI: 10.1038/s41598-017-17446-3
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Kurzbeschreibung (Abstract):

A series of small, catalytically active metallopeptides, which were derived from the nickel superoxide dismutase (NiSOD) active site were employed to study the mechanism of superoxide degradation especially focusing on the role of the axial imidazole ligand. In the literature, there are contradicting propositions about the catalytic importance of the N-terminal histidine. Therefore, we studied the stability and activity of a set of eight NiSOD model peptides, which represent the major model systems discussed in the literature to date, yet differing in their length and their Ni-coordination. UV-Vis-coupled stopped-flow kinetic measurements and mass spectrometry analysis unveiled their high oxidation sensitivity in the presence of oxygen and superoxide resulting into a much faster Ni(II)-peptide degradation for the amine/amide Ni(II) coordination than for the catalytically inactive bis-amidate Ni(II) coordination. With respect to these results we determined the catalytic activities for all NiSOD mimics studied herein, which turned out to be in almost the same range of about 2 × 106 M−1 s−1. From these experiments, we concluded that the amine/amide Ni(II) coordination is clearly the key factor for catalytic activity. Finally, we were able to clarify the role of the N-terminal histidine and to resolve the contradictory literature propositions, reported in previous studies.

Sachgruppe der Dewey Dezimalklassifikatin (DDC): 500 Naturwissenschaften und Mathematik > 540 Chemie
Fachbereich(e)/-gebiet(e): 07 Fachbereich Chemie
07 Fachbereich Chemie > Eduard Zintl-Institut
07 Fachbereich Chemie > Eduard Zintl-Institut > Fachgebiet Physikalische Chemie
Hinterlegungsdatum: 01 Dez 2023 10:46
Letzte Änderung: 01 Mär 2024 09:58
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