Reversible heterogeneous reduction and oxidation of sperm whale myoglobin at a surface modified gold minigrid electrode

Stargardt, Joyce F.; Hawkridge, Fred M.; Landrum, H. L.

doi:10.1021/ac50029a026

Cited by 91 publications

(24 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Myoglobin (Mb) is a single-chain protein of 153 amino acids containing a heme (iron-containing porphyrin) group in the center which is found in mammalian skeleton and muscle tissues. Mb functions physiologically in the storage of oxygen and in the enhancement of the rate of oxygen diffusion, and has catalytic activity for H 2 O 2 decomposition similar to horseradish peroxidase [17,18]. It is an ideal model molecule for the study of electron transfer reactions of heme proteins and also for biosensing and biocatalysis.…”

Section: Introductionmentioning

confidence: 99%

Myoglobin/gold nanoparticles/carbon spheres 3-D architecture for the fabrication of a novel biosensor

et al. 2009

View full text Add to dashboard Cite

A novel biosensor based on a myoglobin/gold nanoparticles/carbon spheres (Mb AuNPs CNs) 3-D architecture bioconjunction has been fabricated for the determination of hydrogen peroxide (H 2 O 2 ). Cyclic voltammetry (CV), Fourier transform infrared (FT-IR) spectroscopy and scanning electron microscopy (SEM) were used to characterize the bioconjunction of the AuNPs CNs with Mb. Experimental results demonstrate that the AuNPs CNs hybrid material is more effective in facilitating electron transfer of the immobilized enzyme than CNs alone, which can be attributed to the unique nanostructure and larger surface area of the bioconjunction. The biosensor displayed good performance for the detection of H 2 O 2 with a wide linear range from 0.28 μmol/L to 116.5 μmol/L and a detection limit of 0.12 μmol/L. The Michaelis-Menten constant K M app value was estimated to be 0.3 mmol/L. The resulting biosensor exhibited fast amperometric response, and good stability, reproducibility, and selectivity to H 2 O 2 .

show abstract

Section: Introductionmentioning

confidence: 99%

Myoglobin/gold nanoparticles/carbon spheres 3-D architecture for the fabrication of a novel biosensor

et al. 2009

View full text Add to dashboard Cite

show abstract

“…The electrochemistry of Mb has been described in a number of publications such as early on dropping mercury electrodes [1,2] and later by using methyl viologen modified gold electrode [3,4] and indium oxide electrode [5]. However, electron transfer between Mb and bare solid electrodes is usually slow and the protein is irreversibly denatured [3]. Great efforts have been made to facilitate electron transfer for Mb by using different mediators or promoters [6,7].…”

Section: Introductionmentioning

confidence: 99%

Electrocatalysis via Direct Electrochemistry of Myoglobin Immobilized on Colloidal Gold Nanoparticles

Liu

2003

Electroanalysis

View full text Add to dashboard Cite

The direct electron transfer between immobilized myoglobin (Mb) and colloidal gold modified carbon paste electrode was studied. The Mb immobilized on the colloidal gold nanoparticles displayed a pair of redox peaks in 0.1 M pH 7.0 PBS with a formal potential of ±(0.108 AE 0.002) V (vs. NHE). The response showed a surface-controlled electrode process with an electron transfer rate constant of (26.7 AE 3.7) s À1 at scan rates from 10 to 100 mV s À1 and a diffusioncontrolled process involving the diffusion of proton at scan rates more than 100 mV s À1 . The immobilized Mb maintained its activity and could electrocatalyze the reduction of both hydrogen peroxide and nitrite. Thus, the novel renewable reagentless sensors for hydrogen peroxide and nitrite were developed, respectively. The activity of Mb with respect to the pseudo peroxidase with a K M app value of 0.65 mM could respond linearly to hydrogen peroxide concentration from 4.6 to 28 mM. The sensor exhibited a fast amperometric response to NO 2 À reduction and reached 93% of steady-state current within 5 s. The linear range for NO 2 À determination was from 8.0 to 112 mM with a detection limit of 0.7 mM at 3s.

show abstract

“…Myoglobin (Mb) is a single-chain protein of 153 amino acids, containing a heme (iron-containing porphyrin) group in the center. Mb is found in mammalian skeleton and muscle tissues, which functions in the storage of oxygen and in the enhancement of the rate of oxygen diffusion [1,2]. But the electron transfer of Mb is very slow on conventional electrodes because of protein adsorption and subsequent passivation of the electrodes surface.…”

Section: Introductionmentioning

confidence: 99%

A Novel NH₂/ITO Ion Implantation Electrode: Preparation, Characterization, and Application in Bioelectrochemistry

Cao

et al. 2009

Electroanalysis

View full text Add to dashboard Cite

A novel NH 2 þ ion implantation-modified indium tin oxide (NH 2 /ITO) electrode was prepared. Acid-pretreated, negatively charged MWNTs were firstly modified on the surface of NH 2 þ ion implantation electrode, then, positively charged Mb was adsorbed onto MWNTs films by electrostatic interaction. The assembly of MWNTs and Mb was characterized with electrochemical impedance spectroscopy (EIS) and cyclic voltammetry (CV). The immobilized Mb showed a couple of quasireversible cyclic voltammetry peaks in pH 7.0 phosphate buffer solution (PBS). The apparent surface concentration of Mb at the electrode surface was 1.06 Â 10 À9 mol cm À2. The Mb/MWNTs/NH 2 /ITO electrode also gave an improved electrocatalytic activity towards the reduction of hydrogen peroxide. The catalysis currents increased linearly to the H 2 O 2 concentration in a wide range from 9 Â 10 À7 to 9.2 Â 10 À5 M with a correlation coefficient of 0.999. The detection limit was 9.0 Â 10 À7 M. The experiment results demonstrated that the modified electrode provided a biocompatible microenvironment for protein and supplied a necessary pathway for its direct electron transfer.

show abstract

Reversible heterogeneous reduction and oxidation of sperm whale myoglobin at a surface modified gold minigrid electrode

Cited by 91 publications

References 15 publications

Myoglobin/gold nanoparticles/carbon spheres 3-D architecture for the fabrication of a novel biosensor

Myoglobin/gold nanoparticles/carbon spheres 3-D architecture for the fabrication of a novel biosensor

Electrocatalysis via Direct Electrochemistry of Myoglobin Immobilized on Colloidal Gold Nanoparticles

A Novel NH₂/ITO Ion Implantation Electrode: Preparation, Characterization, and Application in Bioelectrochemistry

Contact Info

Product

Resources

About

Reversible heterogeneous reduction and oxidation of sperm whale myoglobin at a surface modified gold minigrid electrode

Cited by 91 publications

References 15 publications

Myoglobin/gold nanoparticles/carbon spheres 3-D architecture for the fabrication of a novel biosensor

Myoglobin/gold nanoparticles/carbon spheres 3-D architecture for the fabrication of a novel biosensor

Electrocatalysis via Direct Electrochemistry of Myoglobin Immobilized on Colloidal Gold Nanoparticles

A Novel NH2/ITO Ion Implantation Electrode: Preparation, Characterization, and Application in Bioelectrochemistry

Contact Info

Product

Resources

About

A Novel NH₂/ITO Ion Implantation Electrode: Preparation, Characterization, and Application in Bioelectrochemistry