Electrochemical investigation of the effect of some organic phosphates on haemoglobin

Rezaei‐Zarchi, Saeed; Saboury, Ali Akbar; Ghourchian, Hedayatollah; Hong, Jun; Barzegar, Abolfazl; Norouzi, Parviz; Moosavi-Movahedi, Ali Akbar; Javed, Aisha

doi:10.1007/s12038-007-0027-y

Cited by 5 publications

(7 citation statements)

References 37 publications

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“…GTP facilitated both reduction and oxidation, so its effect on the structure of haemoglobin was to transfer haem to the surface of the protein. The work of Peng et al [15] and our previous work [36] showed that 30 lM concentration of 2,3-diphosphoglycerate (DPG as a typically allosteric effector to haemoglobin) can cause a positive shift in cathodic peak near 45 mV. Our present work shows that a high GTP concentration (4.5 mM) is required for its binding to haemoglobin; therefore, GTP has low affinity to haemoglobin compared to that of DPG.…”

Section: Dependence Of Peak Current On the Scan Ratesupporting

confidence: 55%

“…To date, Li et al used pyrolytic graphite (PG) disk electrode with the haemoglobin entrapped on a membrane consisting of eggphosphatidylcholine (egg-PC) [15]. Other examples include the use of an iodide modified silver electrode [36] and our present study. Furthermore, the use of a nanosilver modified graphite electrode in this study results in welldefined peaks for haemoglobin, better than the method of Peng et al, and this method is more stable than the use of the iodide modified silver electrode.…”

Section: Gdp and Gmp Effectsmentioning

confidence: 98%

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Use of silver nanoparticles as an electron transfer facilitator in electrochemical ligand-binding of haemoglobin

et al. 2007

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Silver nanoparticles have an activity for high intensity electron transfer. They can facilitate the electron transfer from the redox centre of a protein, as a high volume molecule, to the electrode surface. In this study, silver nanoparticles were deposited on the surface of a graphite carbon electrode in the 1 V potential region. Deposition of silver nanoparticles, with a diameter between 70 and 150 nm, was observed on the graphite electrode by transmission electron microscopy (TEM). The results demonstrated that the fine redox waves of haemoglobin could be achieved after modification of the graphite electrode by silver nanoparticles. The cathodic and anodic peaks of haemoglobin were at -135 and +375 mV vs. Ag/AgCl, respectively. The effect of guanosine 3¢,5¢-triphosphate (GTP), guanosine diphosphate (GDP) and guanosine monophosphate (GMP) on the structure of haemoglobin was investigated. It was observed that GTP shifts the cathodic and anodic peaks positively, indicating the transfer of the haem group to the surface of protein as a reflex of easier oxidation and reduction, while GDP and GMP do not show this behaviour. GTP binds with haemoglobin, while GDP and GMP do not.

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Section: Dependence Of Peak Current On the Scan Ratesupporting

confidence: 55%

Section: Gdp and Gmp Effectsmentioning

confidence: 98%

Use of silver nanoparticles as an electron transfer facilitator in electrochemical ligand-binding of haemoglobin

et al. 2007

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“…The preparation of a GC electrode was similar to that given in previous articles. 20,32,[37][38][39][40] Prior to coating, the GC electrode was mechanically polished twice with alumina (particle sizes 1, 0.3 and 0.05 μm, respectively) to a mirror finish. Then, it was treated electrochemically in 200 mM sulfuric acid, cycling between -1.0 and +0.5 V (vs. Ag/AgCl) at a sweep rate of 0.1 V/s for approximately 10 min.…”

Section: Preparation Of An Ap Modified Electrodementioning

confidence: 99%

“…At a certain pH, NF turns to aggregation in solution, because of electrostatic interactions of the sulfonate anion. 20 It could be firmly fixed by the number of electroactive material through ion exchange. 21,22 NF has a high chemical stability, and good biocompatibility, and is a biological macromolecule.…”

Section: Introductionmentioning

confidence: 99%

A Highly Efficient Nano-Cluster Artificial Peroxidase and Its Direct Electrochemistry on a Nano Complex Modified Glassy Carbon Electrode

et al. 2012

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A nano-cluster with highly efficient peroxide activity was constructed based on nafion (NF) and cytochrome c (Cyt c). UV-Vis spectrometry and transmission electron microscopy (TEM) methods were utilized for characterization of the nano-structured enzyme or artificial peroxidase (AP). The nano-cluster was composed of a Chain-Ball structure, with an average ball size of about 40 nm. The Michaelis-Menten (K(m)) and catalytic rate (k(cat)) constants of the AP were determined to be 2.5 ± 0.4 µM and 0.069 ± 0.001 s(-1), respectively, in 50 mM PBS at pH 7.0. The catalytic efficiency of the AP was evaluated to be 0.028 ± 0.005 µM(-1) s(-1), which was 39 ± 5% as efficient as the native horseradish peroxidase (HRP). The AP was also immobilized on a functional multi-wall carbon nanotube (MWNCTs)-gold colloid nanoparticles (AuNPs) nano-complex modified glassy carbon (GC) electrode. The cyclic voltammetry of AP on the nano complex modified GC electrode showed a pair of well-defined redox peaks with a formal potential (E°') of -45 ± 2 mV (vs. Ag/AgCl) at a scan rate of 0.05 V/s. The heterogeneous electron transfer rate constant (k(s)) was evaluated to be 0.65 s(-1). The surface concentration of electroactive AP on GC electrode (Γ) was 7 × 10(-10) mol cm(-2). The apparent Michaelis-Menten constant (K(m)(app)) was 0.23 nM.

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“…Furthermore, immobilized enzyme has a longer life time and predictable decay rate. [13][14][15][16][17] In this study, alcohol oxidase from Hansenula polymorpha was induced, purified and immobilized with DEAE-cellulose particles. The biochemical properties of immobilized enzyme were compared with those of free enzyme.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Hansenula polymorpha Alcohol Oxidase for Alcohol Biosensor Applications

Chung¹,

Cho²,

Kong

2009

Bulletin of the Korean Chemical Society

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Alcohol oxidase catalyzes the oxidation of short lines alcohol to aldehyde. In this study, alcohol oxidase from Hansenula polymorpha (HpAOD) was induced by addition of 0.5% methanol as the carbon source and purified to electrophoretic homogeneity by column chromatographies. The purified HpAOD was immobilized with DEAE-cellulose particles and its biochemical properties were compared with those of free enzyme. The substrate specificity and the optimum pH of immobilized enzyme were similar to those of free enzyme. On the other hand, the Km values of free and immobilized enzymes for ethanol were 6.66 and 14.65 mM, respectively. The optimum temperature for free enzyme was 50°C, whereas that for immobilized enzyme was 65°C. Immobilized enzyme showed high stability against long storage. Immobilized enzyme was also tested for the enzymatic determination of ethanol by the colorimetric method. We detected 1 mg/liter ethanol (1×10 -4 % ethanol) by 2,6-dichloroindophenol system. Therefore, the present study demonstrated that immobilized HpAOD has high substrate specificity toward ethanol and storage stability, which may be of considerable interest for alcohol biosensor and industrial application.

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Electrochemical investigation of the effect of some organic phosphates on haemoglobin

Cited by 5 publications

References 37 publications

Use of silver nanoparticles as an electron transfer facilitator in electrochemical ligand-binding of haemoglobin

Use of silver nanoparticles as an electron transfer facilitator in electrochemical ligand-binding of haemoglobin

A Highly Efficient Nano-Cluster Artificial Peroxidase and Its Direct Electrochemistry on a Nano Complex Modified Glassy Carbon Electrode

Immobilization of Hansenula polymorpha Alcohol Oxidase for Alcohol Biosensor Applications

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