Direct electrochemistry and electrocatalysis of myoglobin covalently immobilized in mesopores cellular foams.
Myoglobin (Mb) was firstly covalently immobilized into mesopores cellular foams (MCFs) to fabricate the protein electrode (Mb-MCFs/GC electrode) and study the direct electrochemistry of redox protein. The results of UV-vis and FTIR spectra illustrated that the covalently immobilized Mb well retained its native structure and presented good stability. Cyclic voltammetry of Mb-MCFs/GC electrode showed nearly reversible cyclic voltammetric peaks, indicating the direct electron transfer of Mb-FeIII/FeII. In addition, Mb-MCFs/GC electrode exhibited favorable electrocatalytic reduction to H2O2 with high sensitivity, good thermal and long-time stability. Such an avenue, which integrated mesopores cellular foams and redox protein via a simple covalent method, may provide a novel and efficient platform for the fabrication of the third generation biosensor.
Zhang
Ling
L
College of Chemistry and Life Science, Shenyang Normal University, Shenyang 110034, China.
Zhang
Qian
Q
Li
Jinghong
J
D000327:Adsorption; D002384:Catalysis; D003217:Conductometry / Q000379:methods*; D004563:Electrochemistry / Q000379:methods*; D005740:Gases / Q000737:chemistry*; D009211:Myoglobin / Q000032:analysis* / Q000737:chemistry*; D016062:Porosity; D011485:Protein Binding
D005740:Gases; D009211:Myoglobin