Interfacial electron transfer kinetics of the haem (Fe III /Fe II) group in human hemoglobin molecules were investigated on glass/tin-doped indium oxide electrodes. Factors such as surface roughness, crystallinity, hydrophilicity and partial polarization of the working electrode played an important role to provide a more compatible microenvironment for protein adsorption. Results suggested that direct electron transfer from electrode to haem (Fe III)-H 2 O intermediate is coupled to proton at near physiological pH (I = 0.035, pH = 7.2).
Electron transfer properties of the haem (FeIII/FeII) redox center, in human haemoglobin molecules, were investigated, in vitro, on glass/tin-doped indium oxide electrodes. The total surface concentration of electrochemically active haemoglobin molecules corres-ponded to a single protein monolayer. In addition, anodic and cathodic peak currents changed in direct proportion with the scan rate, sugges-ting a surface-controlled electrode process.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.