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Immobilization and Electrochemistry of Negatively Charged Proteins on Modified Nanocrystalline Metal Oxide Electrodes
Author(s) -
Topoglidis Emmanuel,
Palomares Emilio,
Astuti Yeni,
Green Alex,
Campbell Colin J.,
Durrant James R.
Publication year - 2005
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/elan.200403211
Subject(s) - isoelectric point , nanocrystalline material , electrode , electrochemistry , cyclic voltammetry , electron transfer , chemistry , inorganic chemistry , metal , materials science , crystallography , photochemistry , organic chemistry , enzyme
The immobilization of two acidic, low isoelectric point proteins, green fluorescence protein and ferredoxin (FRD) is investigated on nanocrystalline, mesoporous TiO 2 and SnO 2 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 SnO 2 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 .