Peroxidase Mimicking Activity of Palladium Nanocluster Altered by Heparin
NADH, composed of metal binding, charged and redox groups, acts as a “three-in-one” template to construct peroxidase mimicking Pd nanoclusters (NCs). The physicochemical properties of Pd NCs are highly dependent upon the molar ratio of [NADH]/[Na 2 PdCl 4 ], thereby contributing to distinct peroxida...
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Veröffentlicht in: | Catalysis letters 2021-09, Vol.151 (9), p.2537-2546 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
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Zusammenfassung: | NADH, composed of metal binding, charged and redox groups, acts as a “three-in-one” template to construct peroxidase mimicking Pd nanoclusters (NCs). The physicochemical properties of Pd NCs are highly dependent upon the molar ratio of [NADH]/[Na
2
PdCl
4
], thereby contributing to distinct peroxidase mimicking activities. The ultrasmall Pd nanozyme that contains 30% metallic Pd
0
species, exhibits the
K
m
of 0.063 mM toward TMB and 80.8 mM toward H
2
O
2
. Notably, addition of heparin enables the enhancement of its peroxidase-like activity in neutral media. A colorimetric assay was well-established at pH 6 for quantitatively monitoring heparin in aqueous solution and biological fluid. The linear response lies in the range of 0.5–25 µg mL
−1
, with the limit of detection of 1.1 ng mL
−1
. This work paves a promising pathway to manufacture highly active enzyme mimetics with desirable physicochemical properties.
Graphic Abstract |
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ISSN: | 1011-372X 1572-879X |
DOI: | 10.1007/s10562-021-03530-x |