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Immobilization of hemoglobin on electrodeposited cobalt-oxide nanoparticles: direct voltammetry and electrocatalytic activity.
Biophys Chem. 2007 Nov; 130(3):122-31.BC

Abstract

Cyclic voltammetry at potential range -1.1 to 0.5 V from aqueous buffer solution (pH 7) containing CoCl(2) produced a well defined cobalt oxide (CoOx) nanoparticles deposited on the surface of glassy carbon electrode. The morphology of the modified surface and cobalt oxide formation was examined with SEM and cyclic voltammetry techniques. Hemoglobin (Hb) was successfully immobilized in cobalt-oxide nanoparticles modified glassy carbon electrode. Immobilization of hemoglobin onto cobalt oxide nanoparticles have been investigated by cyclic voltammetry and UV-visible spectroscopy. The entrapped protein can take direct electron transfer in cobalt-oxide film. A pair of well defined, quasi-reversible cyclic voltammetric peaks at about -0.08 V vs. SCE (pH 7), characteristic of heme redox couple (Fe(III)/Fe(II)) of hemoglobin, and the response showed surface controlled electrode process. The dependence of formal potential (E(0')) on the solution pH (56 mV pH(-1)) indicated that the direct electron transfer reaction of hemoglobin was a one-electron transfer coupled with a one proton transfer reaction process. The average surface coverage of Hb immobilized on the cobalt oxide nanoparticles was about 5.2536x10(-11) mol cm(-2), indicating high loading ability of nanoparticles for hemoglobin entrapment. The heterogeneous electron transfer rate constant (k(s)) was 1.43 s(-1), indicating great of facilitation of the electron transfer between Hb and electrodeposited cobalt oxide nanoparticles. Modified electrode exhibits a remarkable electrocatalytic activity for the reduction of hydrogen peroxide and oxygen. The Michaels-Menten constant K(m) of 0.38 mM, indicating that the Hb immobilized onto cobalt oxide film retained its peroxidases activity. The biosensor exhibited a fast amperometric response <5 s, a linear response over a wide concentration range 5 microM to 700 microM and a low detection limit 0.5 microM. According to the direct electron transfer property and enhanced activity of Hb in cobalt oxide film, a third generation reagentless biosensor without using any electron transfer mediator or specific reagent can be constructed for determination of hydrogen peroxide in anaerobic solutions.

Authors+Show Affiliations

Department of Chemistry, University of Kurdistan, P.O.Box 416, Sanandaj, Iran. absalimi@uok.ac.irNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17825977

Citation

Salimi, Abdollah, et al. "Immobilization of Hemoglobin On Electrodeposited Cobalt-oxide Nanoparticles: Direct Voltammetry and Electrocatalytic Activity." Biophysical Chemistry, vol. 130, no. 3, 2007, pp. 122-31.
Salimi A, Hallaj R, Soltanian S. Immobilization of hemoglobin on electrodeposited cobalt-oxide nanoparticles: direct voltammetry and electrocatalytic activity. Biophys Chem. 2007;130(3):122-31.
Salimi, A., Hallaj, R., & Soltanian, S. (2007). Immobilization of hemoglobin on electrodeposited cobalt-oxide nanoparticles: direct voltammetry and electrocatalytic activity. Biophysical Chemistry, 130(3), 122-31.
Salimi A, Hallaj R, Soltanian S. Immobilization of Hemoglobin On Electrodeposited Cobalt-oxide Nanoparticles: Direct Voltammetry and Electrocatalytic Activity. Biophys Chem. 2007;130(3):122-31. PubMed PMID: 17825977.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Immobilization of hemoglobin on electrodeposited cobalt-oxide nanoparticles: direct voltammetry and electrocatalytic activity. AU - Salimi,Abdollah, AU - Hallaj,Rahman, AU - Soltanian,Saied, Y1 - 2007/08/24/ PY - 2007/06/21/received PY - 2007/08/15/revised PY - 2007/08/17/accepted PY - 2007/9/11/pubmed PY - 2007/12/12/medline PY - 2007/9/11/entrez SP - 122 EP - 31 JF - Biophysical chemistry JO - Biophys Chem VL - 130 IS - 3 N2 - Cyclic voltammetry at potential range -1.1 to 0.5 V from aqueous buffer solution (pH 7) containing CoCl(2) produced a well defined cobalt oxide (CoOx) nanoparticles deposited on the surface of glassy carbon electrode. The morphology of the modified surface and cobalt oxide formation was examined with SEM and cyclic voltammetry techniques. Hemoglobin (Hb) was successfully immobilized in cobalt-oxide nanoparticles modified glassy carbon electrode. Immobilization of hemoglobin onto cobalt oxide nanoparticles have been investigated by cyclic voltammetry and UV-visible spectroscopy. The entrapped protein can take direct electron transfer in cobalt-oxide film. A pair of well defined, quasi-reversible cyclic voltammetric peaks at about -0.08 V vs. SCE (pH 7), characteristic of heme redox couple (Fe(III)/Fe(II)) of hemoglobin, and the response showed surface controlled electrode process. The dependence of formal potential (E(0')) on the solution pH (56 mV pH(-1)) indicated that the direct electron transfer reaction of hemoglobin was a one-electron transfer coupled with a one proton transfer reaction process. The average surface coverage of Hb immobilized on the cobalt oxide nanoparticles was about 5.2536x10(-11) mol cm(-2), indicating high loading ability of nanoparticles for hemoglobin entrapment. The heterogeneous electron transfer rate constant (k(s)) was 1.43 s(-1), indicating great of facilitation of the electron transfer between Hb and electrodeposited cobalt oxide nanoparticles. Modified electrode exhibits a remarkable electrocatalytic activity for the reduction of hydrogen peroxide and oxygen. The Michaels-Menten constant K(m) of 0.38 mM, indicating that the Hb immobilized onto cobalt oxide film retained its peroxidases activity. The biosensor exhibited a fast amperometric response <5 s, a linear response over a wide concentration range 5 microM to 700 microM and a low detection limit 0.5 microM. According to the direct electron transfer property and enhanced activity of Hb in cobalt oxide film, a third generation reagentless biosensor without using any electron transfer mediator or specific reagent can be constructed for determination of hydrogen peroxide in anaerobic solutions. SN - 0301-4622 UR - https://www.unboundmedicine.com/medline/citation/17825977/Immobilization_of_hemoglobin_on_electrodeposited_cobalt_oxide_nanoparticles:_direct_voltammetry_and_electrocatalytic_activity_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0301-4622(07)00196-2 DB - PRIME DP - Unbound Medicine ER -