Abstract
The immobilization of two acidic, low isoelectric point proteins, green fluorescence protein and ferredoxin (FRD) is investigated on nanocrystalline, mesoporous TiO2 and SnO2 electrodes. Modification of these electrodes with a cationic polypeptide (poly-L-lysine) or an aminosilane prior to protein immobilization is found to enhance protein binding at least ten fold, attributed to more favorable protein/electrode electrostatic interactions. Cyclic voltammetry studies of FRD-modified SnO2 electrodes indicate reversible protein electrochemistry with a midpoint potential of -0.59 V (vs. Ag/AgCl) and an interfacial electron transfer rate constant of 0.45 s(-1).
Original language | English |
---|---|
Pages (from-to) | 1035-1041 |
Number of pages | 7 |
Journal | Electroanalysis |
Volume | 17 |
Issue number | 12 |
DOIs | |
Publication status | Published - Jun 2005 |
Keywords / Materials (for Non-textual outputs)
- protein immobilization
- ferredoxin
- nanocrystalline SnO2
- TiO2
- electrode modification
- cylic voltammetry
- PYROLYTIC-GRAPHITE ELECTRODES
- CYTOCHROME-C
- FILM VOLTAMMETRY
- NANOPOROUS TIO2
- ADSORPTION
- FERREDOXIN
- BIOELECTROCHEMISTRY
- SPECTROSCOPY
- MECHANISMS