Electrochemistry of Metalloproteins Attached through Functional Self-Assembled Monolayers on Gold and Ferromagnetic Electrodes.
Prakash Chandra MondalClaudio FontanesiPublished in: Chemphyschem : a European journal of chemical physics and physical chemistry (2017)
We report the experimental results of a study of the electron-transfer processes of redox-active metalloproteins bound to mixed self-assembled monolayers (SAMs) on magnetic (nickel or ultrathin gold-coated nickel) or nonmagnetic (gold) electrodes. Metalloproteins, such as hemoglobin (Hb), Cytochrome C (Cyt C), and Cyt C oxidase, are attached through electrostatic interactions to the free carboxylate or imidazole groups present in the mixed SAMs. The formation of both mixed SAMs and SAM/metalloprotein heterostructures were confirmed by using advanced surface analysis techniques, such as polarization modulation infrared reflection absorption spectroscopy and aqueous contact angle measurements. Electrochemical measurements indicated a stronger electronic coupling between Hb and Cyt C oxidase and the mixed-SAM-coated gold or gold-coated-nickel electrodes, whereas a weaker coupling was found between the protein and the pure nickel electrode. Surface coverage and the electron-transfer rate constant were estimated from the cyclic voltammetry data.
Keyphrases
- electron transfer
- reduced graphene oxide
- carbon nanotubes
- gold nanoparticles
- room temperature
- solid state
- silver nanoparticles
- metal organic framework
- oxide nanoparticles
- high resolution
- ionic liquid
- healthcare
- mass spectrometry
- single molecule
- electronic health record
- molecularly imprinted
- high efficiency
- data analysis
- molecular dynamics simulations
- amino acid
- simultaneous determination