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Construction of the Active Site of Metalloenzyme on Au NC Micelles
Author(s) -
ZHANG Zhiming,
FU Qiuan,
HUANG Xin,
XU Jiayun,
LIU Junqiu,
SHEN Jiacong
Publication year - 2009
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.200990203
Subject(s) - micelle , chemistry , cleavage (geology) , catalysis , ribonuclease , ligand (biochemistry) , kinetics , stereochemistry , combinatorial chemistry , polymer chemistry , organic chemistry , aqueous solution , biochemistry , rna , receptor , fracture (geology) , gene , physics , geotechnical engineering , quantum mechanics , engineering
For developing an efficient nanoenzyme system with self‐assembly strategy, gold nanocrystal micelles (Au NC micelles) with inserted catalytic Zn(II) centers were constructed by self‐assembly of a catalytic ligand [ N , N ‐bis(2‐aminoethyl)‐ N′ ‐dodecylethylenediamine] Zn(II) complexes (Zn(II)L) on the surface of Au NC via hydrophobic interaction. The functionalized Au NC micelles acted as an excellent nanoenzyme model for imitating ribonuclease. The catalytic capability of the Au NC micelles was evaluated by accelerating the cleavage of 2‐hydroxypropyl p ‐nitrophenyl phosphate (HPNP). These functionalized Au NC micelles exhibited considerable ribonuclease‐like activities by a factor of 4.9×10 4 ( k cat / k uncat ) for the cleavage of HPNP in comparison to the spontaneous cleavage of HPNP at 37°C. The catalytic capability of the functionalized Au NC micelles can be considerably compared to other models reported previously as nanoenzymes under the comparable conditions.