Myoglobin was immobilized on edge-plane pyrolytic graphite（EPG）electrodes by sodium alginate hydrogel.The protein entrapped in the sodium alginate film undergoes fast direct electron-transfer reactions with the form...Myoglobin was immobilized on edge-plane pyrolytic graphite（EPG）electrodes by sodium alginate hydrogel.The protein entrapped in the sodium alginate film undergoes fast direct electron-transfer reactions with the formal potential(Eo′)of-0.296V（vs SCE）,corresponding to FeⅢ+e-→FeⅡ,The Eo′s are linearly dependent on solution pH with the slope value of-35.0 mV/pH,indicating that the electron transfer was proton-coupled.The mechanisms for catalytic reduction of oxygen,hydrogen peroxide and nitric oxide by myoglobin entrapped in sodium alginate hydrogel were also explored.展开更多
The Cu（Ⅱ）complexes of 2-aminopyrimidine were synthesized and characterized by elemental analyses,TG-DTG.The dissolution enthalpies of the[AP（s）+CuCl2·2H2O（s）]and Cu（AP） Cl2（s）in 100.00 mL 2 mol.L-1HCl ...The Cu（Ⅱ）complexes of 2-aminopyrimidine were synthesized and characterized by elemental analyses,TG-DTG.The dissolution enthalpies of the[AP（s）+CuCl2·2H2O（s）]and Cu（AP） Cl2（s）in 100.00 mL 2 mol.L-1HCl solution were measured at 298.15 K by classical solution calorimetry.The standard molar reaction enthalpy of the coondination reaction of 2-aminopyrimidine with Cu（Ⅱ）has been determined by a thermochemical cycle(ΔrH<sup>○-m=-1.92±0.27kJ·mol-1).From the result,the standard molar enthalpy of formation ΔfH<sup>○-m[Cu（AP）Cl2,s,298.15K] of Cu（AP）Cl2 has been calculated to be-297.46±1.72kJ·mol-1.展开更多
Myoglobin(Mb)was immobilized’on glassy carbon electrode(GCE)surface by carl·ageenan.The enzyme-Iike properties of immobilized Mb,such as catalytic reduction of peroxides(hydrogen peroxide,cumene hydroperoxide,t-...Myoglobin(Mb)was immobilized’on glassy carbon electrode(GCE)surface by carl·ageenan.The enzyme-Iike properties of immobilized Mb,such as catalytic reduction of peroxides(hydrogen peroxide,cumene hydroperoxide,t-butyl hydroperoxide,2-butanone peroxide),and dehalogenation of haloethanes(hexachloroethane,pentachloroethane,tetrachloroethane),were explored by cyclic voltammetry.Stability and reproducibility of the modified electrode make it possible to determine the substances.展开更多
文摘Myoglobin was immobilized on edge-plane pyrolytic graphite（EPG）electrodes by sodium alginate hydrogel.The protein entrapped in the sodium alginate film undergoes fast direct electron-transfer reactions with the formal potential(Eo′)of-0.296V（vs SCE）,corresponding to FeⅢ+e-→FeⅡ,The Eo′s are linearly dependent on solution pH with the slope value of-35.0 mV/pH,indicating that the electron transfer was proton-coupled.The mechanisms for catalytic reduction of oxygen,hydrogen peroxide and nitric oxide by myoglobin entrapped in sodium alginate hydrogel were also explored.
文摘The Cu（Ⅱ）complexes of 2-aminopyrimidine were synthesized and characterized by elemental analyses,TG-DTG.The dissolution enthalpies of the[AP（s）+CuCl2·2H2O（s）]and Cu（AP） Cl2（s）in 100.00 mL 2 mol.L-1HCl solution were measured at 298.15 K by classical solution calorimetry.The standard molar reaction enthalpy of the coondination reaction of 2-aminopyrimidine with Cu（Ⅱ）has been determined by a thermochemical cycle(ΔrH<sup>○-m=-1.92±0.27kJ·mol-1).From the result,the standard molar enthalpy of formation ΔfH<sup>○-m[Cu（AP）Cl2,s,298.15K] of Cu（AP）Cl2 has been calculated to be-297.46±1.72kJ·mol-1.
文摘Myoglobin(Mb)was immobilized’on glassy carbon electrode(GCE)surface by carl·ageenan.The enzyme-Iike properties of immobilized Mb,such as catalytic reduction of peroxides(hydrogen peroxide,cumene hydroperoxide,t-butyl hydroperoxide,2-butanone peroxide),and dehalogenation of haloethanes(hexachloroethane,pentachloroethane,tetrachloroethane),were explored by cyclic voltammetry.Stability and reproducibility of the modified electrode make it possible to determine the substances.
