Open AccessCu‐induced assembly of methanobactin‐modified gold nanoparticles and its peroxidase mimic activity
Author(s) -
JiaYing Xin,
ChunYu Li,
Shuai Zhang,
Yan Wang,
Wei Zhang,
ChunGu Xia
Publication year - 2018
Publication title -
iet nanobiotechnology
Language(s) - English
Resource type - Journals
ISSN - 1751-875X
DOI - 10.1049/iet-nbt.2018.0069
Subject(s) - catalysis , chemistry , copper , hydroquinone , colloidal gold , hydrogen peroxide , ligand (biochemistry) , nanomaterial based catalyst , nanoparticle , methane monooxygenase , photochemistry , inorganic chemistry , combinatorial chemistry , organic chemistry , nanotechnology , materials science , biochemistry , receptor
Methanobactin (Mb) is a small copper‐chelating molecule that functions as an agent for copper acquisition, uptake and copper‐containing methane monooxygenase catalysis in methane‐oxidising bacteria. The UV–visible spectral and fluorescence spectral suggested that Mb/Cu coordination complex as a monomer (Mb‐Cu), dimmer (Mb 2 ‐Cu) and tetramer (Mb 4 ‐Cu) could be obtained at different ratios of Mb to Cu (II). The kinetics of the oxidation of hydroquinone with hydrogen peroxide catalysed by the different Mb/Cu coordination complex were investigated. The results suggested that Mb 2 ‐Cu coordination form has highest catalytic capacity. Further, Mb‐modified gold nanoparticles (AuNPs) were obtained by ligand exchange and assembled into two‐ and three‐D nanocluster structure by metal‐organic coordination as driving force. It has been found that AuNPs increased the catalytic activity of Mb 2 ‐Cu on AuNPs. The more significant catalytic activity was exhibited by the nanocluster assembly with multi‐catalytic centres. This may be attributed to the multivalent collaborative characteristics of the catalytic active centres in the nanocluster network assembly. The assembly of Mb‐modified AuNPs can act as excellent nanoenzyme models for imitating peroxidase.