Myoglobin immobilization on electrodeposited nanometer-scale nickel oxide particles and direct voltammetry.
Prosperity of information on the reactions of redox-active sites in proteins can be attained by voltammetric studies in which the protein sample is located on a suitable surface. This work reports the presentation of myoglobin/nickel oxide nanoparticles/glassy carbon (Mb/NiO NPs/GC) electrode, ready by electrochemical deposition of the NiO NPs on glassy carbon electrode and myoglobin immobilization on their surfaces by the potential cycling method. Images of electrodeposited NiO NPs on the surface of glassy carbon electrode were obtained by scanning electron microscopy (SEM) and atomic force microscopy (AFM). A pair of well-defined redox peaks for Mb(Fe(III)-Fe(II)) was obtained at the prepared electrode by direct electron transfer between the protein and nanoparticles. Electrochemical parameters of immobilized myoglobin such as formal potential (E(0')), charge transfer coefficient (alpha) and apparent heterogeneous electron transfer rate constant (k(s)) were estimated by cyclic voltammetry and nonlinear regression analysis. Biocatalytic activity was exemplified at the prepared electrode for reduction of hydrogen peroxide.
Moghaddam
Abdolmajid Bayandori
AB
Center of Excellence in Electrochemistry, Faculty of Chemistry, University of Tehran, P. O. Box 14155-6455, Tehran, Iran.
Ganjali
Mohammad Reza
MR
Dinarvand
Rassoul
R
Ahadi
Sara
S
Saboury
Ali Akbar
AA
D002244:Carbon / Q000737:chemistry; D002384:Catalysis; D004566:Electrodes; D004595:Electroplating; D006861:Hydrogen Peroxide / Q000737:chemistry; D053768:Metal Nanoparticles / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D008855:Microscopy, Electron, Scanning; D009211:Myoglobin / Q000737:chemistry*; D009532:Nickel / Q000737:chemistry*; D010084:Oxidation-Reduction; D011485:Protein Binding
D009211:Myoglobin; D002244:Carbon; D009532:Nickel; D006861:Hydrogen Peroxide; C028007:nickel monoxide