Films of hemoglobin and didodecyldimethylammonium bromide with enhanced electron transfer rates

Lu, Zhongqing; Huang, Qingdong; Rusling, James F.

doi:10.1016/s0022-0728(96)04843-7

Cited by 133 publications

(81 citation statements)

References 28 publications

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“…Based on CV data, Ma and coworkers [16] concluded that direct electron transfer reaction of Hb is not promoted by the surfactant CTAB or Nafion but is rather promoted by CB due to the presence of the oxygen-containing groups and many active sites on the surface. However, based on researches by Rusling s group [17][18][19][20] and our above-cited results (see Figure 2) it was inferred that surfactants (DDAB, CTAB) play an important role in direct electron transfer reactions of heme proteins. Without DDAB, CB did not exhibited any catalytic properties towards heme proteins.…”

Section: Direct Electrochemistry Of Heme Proteins On Ddab/cb/spementioning

confidence: 76%

“…The electron transfer rate of the Hb heme s Fe(III)/Fe(II) couple was much greater in DDAB films than it was on bare edge-plane pyrolytic graphite electrodes or electrodes modified with mediators with Hb in solution [20]. Electronic absorbance linear dichroism showed that Hb and Mb are preferentially oriented in the films [19,20]. Therefore, surfactants (DDAB, CTAB) provide good adsorption of heme proteins and serve not only as dispersants to prevent the powder aggregation but also as catalysts of electrochemical reactions.…”

Section: Introductionmentioning

confidence: 90%

“…Mb retains the heme iron and near-native conformation in DDAB films [19]. The electron transfer rate of the Hb heme s Fe(III)/Fe(II) couple was much greater in DDAB films than it was on bare edge-plane pyrolytic graphite electrodes or electrodes modified with mediators with Hb in solution [20]. Electronic absorbance linear dichroism showed that Hb and Mb are preferentially oriented in the films [19,20].…”

Section: Introductionmentioning

confidence: 99%

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Direct Electrochemistry of Heme Proteins on Electrodes Modified with Didodecyldimethyl Ammonium Bromide and Carbon Black

et al. 2012

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A novel matrix based on commercially available carbon black (CB) N220 and didodecyldimethyl ammonium bromide (DDAB) was shown to be a reliable support for direct electron transfer reactions between screen printed electrode (SPE) and Fe(III)-heme proteins. Cytochrome c (cyt c), myoglobin (Mb), horseradish peroxidase (HRP) and cytochromes P450 (CYP 51A1, CYP 3A4, CYP 2B4) generated well-shaped cyclic voltammograms on SPE/CB/ DDAB electrodes (both in solution and in immobilized state). The attractive performance characteristics of CB modified electrodes are advantageous over single-walled carbon nanotubes (SW CNT) based ones. The achieved direct electrochemistry of heme proteins on CB/DDAB-modified electrodes provided successful elaboration of the immunosensor for cardiac Mb. The immunosensor showed applicability for diagnostics of myocardial infarction displaying significant difference in cardiac Mb content of human blood plasma samples taken from the corresponding patients.

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Section: Direct Electrochemistry Of Heme Proteins On Ddab/cb/spementioning

confidence: 76%

Section: Introductionmentioning

confidence: 90%

Section: Introductionmentioning

confidence: 99%

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Direct Electrochemistry of Heme Proteins on Electrodes Modified with Didodecyldimethyl Ammonium Bromide and Carbon Black

et al. 2012

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“…In order to improve the slow rates of electron transfer between hemoglobin and solid electrodes, functionalized electrodes using mediators, promoters or nanomaterials have been reported by several groups [11][12][13][14]23]. Films cast from didodecyldimethylammonium bromide (DDAB) microemulsions containing myoglobin onto pyrolytic graphite electrodes gave good electron transfer properties [24].…”

Section: Enhanced Electron Transfer For Hemoglobin In Hemoglobin-surfmentioning

confidence: 99%

“…Because of slow rates of electron transfer between hemoglobin and solid electrodes, efforts have been made to facilitate the electron transfer of hemoglobin by using mediators, promoters or special electrode materials [9][10][11]. The direct electron transfer was greatly enhanced for hemoglobin as well as myoglobin in stable lamellar liquid crystal surfactant films [12][13]. Most recently, the electrochemical studies of hemoglobin have also involved primarily heterogeneous electron transfer based on the nano-structural materials [14][15][16][17].…”

Section: Introductionmentioning

confidence: 99%

Comparison of Kinetics of Hemoglobin Electron Transfer in Solution and Immobilized on Electrode Surface

Li¹,

Liu²,

Prabhulkar³

2009

Am. J. Biomed. Sci.

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The electron transfer properties of horse heart hemoglobin are compared using a hydrophilic indium tin oxide electrode and a dilaurydimethylammonium bromide (DDAB) polymer modified PG electrodes. A clear, stable and quasi-reversible redox curve of hemoglobin (Hb) was obtained in the absence of electron transfer mediators or promoters. The formal redox potential of -0.17 vs. Ag/AgCl of Hb was determined. The effects of the sixth axial binding ligands including cyanoand azido binding ligands on the redox properties of Hb were investigated. There are no significant impacts of these ligands on the redox properties of Hb, whereas big effects of the binding ligand on the electrochemical properties of myoglobin were reported. The cyclic voltammetric behavior of hemoglobin was also studied in a DDAB film coated on a pyrolytic graphite electrode. Surface immobilized Hb in DDAB film gave direct, quasi-reversible, nondiffusion-kinetic-controlled electron transfer on the electrode surface. The formal redox potential for Hb in the DDAB film negatively shifted about 140 mV as compared to the diffusion-controlled redox reaction of Hb.

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Direct Reduction of Oxyhemoglobin on a Bare Glassy Carbon Electrode

et al. 1998

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Irreversible electrochemical reduction of oxyhemoglobin (HbO 2 ) has been observed on a bare glassy carbon electrode (GCE) in acetate buffer solution. It is the bonded oxygen of HbO 2 , not the heme iron in hemoglobin that reacts electrochemically on the electrode. The peak current was a maximum value in acetate buffer solution at pH 5.0. The peak potential was pH dependent, which suggests that protons are involved in the electrochemical reaction. A possible reaction mechanism is proposed as: HbO 2 + 2H + + 2e → Hb + H 2 O 2 . Surfactants such as hexadecyltrimethylammonium bromide can promote the electrochemical reduction of HbO 2 and 0.09 % (w/w) was the optimum concentration of surfactant for the current response. Moreover, the peak current was linearly proportional to the concentration of HbO 2 in the range from 5 × 10 ¹8 to 1.5 × 10 ¹7 mol/L. The detection limit was 10 ¹8 mol/L. This method can be used for the determination of oxyhemoglobin in samples.

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Films of hemoglobin and didodecyldimethylammonium bromide with enhanced electron transfer rates

Cited by 133 publications

References 28 publications

Direct Electrochemistry of Heme Proteins on Electrodes Modified with Didodecyldimethyl Ammonium Bromide and Carbon Black

Direct Electrochemistry of Heme Proteins on Electrodes Modified with Didodecyldimethyl Ammonium Bromide and Carbon Black

Comparison of Kinetics of Hemoglobin Electron Transfer in Solution and Immobilized on Electrode Surface

Direct Reduction of Oxyhemoglobin on a Bare Glassy Carbon Electrode

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