Abstract
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.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
