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Direct electrochemistry and electrocatalysis of myoglobin(Mb) were studied with Mb immobilized on dodecyltrimethylammonium bromide(DTAB) film modified carbon ceramic(CC) electrode.Cyclic voltammetry showed a pair of well-defined and nearly reversible redox peaks of Mb(Fe~Ⅱ/Fe~Ⅲ) at about—0.3 V vs.SCE(pH = 6.98).The currents of the redox peak were linear to scan rate,and rate constant(Ks) was estimated to be 3.03 s~(-1).The formal potential(E°’) of Mb in the DTAB/CC electrodes shifted linearly with pH with a slope of -36.44 mV/pH,implying that the electron transfer between DTAB and CC electrodes is accompanied by proton transportation.The immobilized Mb exhibited excellent electrocatalytic response to the reduction of hydrogen peroxide(H_2O_2).
Direct electrochemistry and electrocatalysis of myoglobin (Mb) were studied with Mb immobilized on dodecyltrimethylammonium bromide (DTAB) film modified carbon ceramic (CC) electrode. Cyclic voltammetry showed a pair of well-defined and nearly reversible redox peaks of Mb (Fe ~ Ⅱ / The currents of the redox peak were linear to scan rate, and rate constant (Ks) was estimated to be 3.03 s ~ (-1). The form of Fe ~ Ⅲ) at about -0.3 V vs. SCE (pH = 6.98) potential (E ° ’) of Mb in the DTAB / CC electrode shifted linearly with pH with a slope of -36.44 mV / pH, implying that the electron transfer between DTAB and CC electrodes is accompanied by proton transportation.The immobilized Mb demonstrated excellent electrocatalytic response to the reduction of hydrogen peroxide (H 2 O 2).