Immobilization and Electrochemistry of Negatively Charged Proteins on Modified Nanocrystalline Metal Oxide Electrodes | Zendy

Topoglidis Emmanuel | Zendy; Palomares Emilio | Zendy; Astuti Yeni | Zendy; Green Alex | Zendy; Campbell Colin J. | Zendy; Durrant James R. | Zendy

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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 .

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