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Inhibition of Human Hemoglobin Autoxidaiton by Sodium n-Dodecyl Sulphate
Reza, Dayer Mohammad,Ali Akbar, Moosavi-Movahedi,Parviz, Norouzi,Ghourchian, Ghourchian,Hedayat-Olah, Hedayat-Olah,Shahrokh, Safarian 생화학분자생물학회 2002 Journal of biochemistry and molecular biology Vol.35 No.4
The effect of sodium n-dodecyl sulphate (SDS) on hemoglobin autoxidation was studied in the presence of a 100mM phosphate buffer (pH 7.0) by different methods. These included spectorphotometry, fluorescence technique, cyclic voltametry, differential scanning calorimetry, and densitometry. Spectroscopic studies showed that SDS concentrations up to 1 mM increased deoxy-, decreases oxy-, and had no significant effect on the met- conformation of hemoglobin. Therefore, a SDS concentration up to 1 mM increased the deoxy form of hemoglobin as the folded, compact state and decreases the oxy conformation. The turbidity measurements and differential scanning calorimetry techniques indicated a more stable conformation for hemoglobin in the presence of SDS up to 1mM. Electrochemical studies also confirmed a more difficult oxidation under these conditions. The induction of the deoxy form in the presence of SDS was confirmed by densitometry techniques. The compact structure of deoxyhemoglobin blocks the formation of met-conformation in low SDS concentrations.
Thermal Dissociation and Conformational Lock of Superoxide Dismutase
Hong, J.,Moosavi-Movahedi, A.A.,Ghourchian, H.,Amani, M.,Amanlou, M.,Chilaka, F.C. Korean Society for Biochemistry and Molecular Biol 2005 Journal of biochemistry and molecular biology Vol.38 No.5
The kinetics of thermal dissociation of superoxide dismutase (SOD) was studied in 0.05 M Tris-HCl buffer at pH 7.4 containing $10^{-4}\;M$ EDTA. The number of conformational locks and contact areas and amino acid residues of dimers of SOD were obtained by kinetic analysis and biochemical calculation. The cleavage bonds between dimers of SOD during thermal dissociation and type of interactions between specific amino acid residues were also simulated. Two identical contact areas between two subunits were identified. Cleavage of these contact areas resulted in dissociation of the subunits, with destruction of the active centers, and thus, lost of activity. It is suggested that the contact areas interact with active centers by conformational changes involving secondary structural elements.
Inhibition of Human Hemoglobin Autoxidation by Sodium n - Dodecyl Sulphate
(Dayer Mohammad Reza),(Moosavi Movahedi Ali Akbar),(Norouzi Parviz),(Ghourchian),(Hedayat Olah),(Safarian Shahrokh) 생화학분자생물학회 2002 BMB Reports Vol.35 No.4
The effect of sodium n-dodecyl sulphate (SDS) on hemoglobin autoxidation was studied in the presence of a 100 mM phosphate buffer (pH 7.0) by different methods. These included spectrophotometry, fluorescence technique, cyclic voltametry, differential scanning calorimetry, and densitometry. Spectroscopic studies showed that SDS concentrations up to 1 mM increased deoxy-, decreases oxy-, and had no significant effect on the met- conformation of hemoglobin. Therefore, a SDS concentration up to 1 mM increased the deoxy form of hemoglobin as the folded, compact state and decreases the oxy conformation. The turbidity measurements and differential scanning calorimetry techniques indicated a more stable conformation for hemoglobin in the presence of SDS up to 1 mM. Electrochemical studies also confirmed a more difficult oxidation under these conditions. The induction of the deoxy form in the presence of SDS was confirmed by densitometry techniques. The compact structure of deoxyhemoglobin blocks the formation of met-conformation in low SDS concentrations.
Electrochemical Behavior of Redox Proteins Immobilized on Nafion-Riboflavin Modified Gold Electrode
Rezaei-Zarchi, S.,Saboury, A.A.,Hong, J.,Norouzi, P.,Moghaddam, A.B.,Ghourchian, H.,Ganjali, M.R.,Moosavi-Movahedi, A.A.,Javed, A.,Mohammadian, A. Korean Chemical Society 2007 Bulletin of the Korean Chemical Society Vol.28 No.12
Electron transfer of a redox protein at a bare gold electrode is too slow to observe the redox peaks. A novel Nafion-riboflavin functional membrane was constructed during this study and electron transfer of cytochrome c, superoxide dismutase, and hemoglobin were carried out on the functional membrane-modified gold electrode with good stability and repeatability. The immobilized protein-modified electrodes showed quasireversible electrochemical redox behaviors with formal potentials of 0.150, 0.175, and 0.202 V versus Ag/AgCl for the cytochrome c, superoxide dismutase and hemoglobin, respectively. Whole experiment was carried out in the 50 mM MOPS buffer solution with pH 6.0 at 25 oC. For the immobilized protein, the cathodic transfer coefficients were 0.67, 0.68 and 0.67 and electron transfer-rate constants were evaluated to be 2.25, 2.23 and 2.5 s?1, respectively. Hydrogen peroxide concentration was measured by the peroxidase activity of hemoglobin and our experiment revealed that the enzyme was fully functional while immobilized on the Nafion-riboflavin membrane.
Electrochemical Behavior of Redox Proteins Immobilized on Nafion-Riboflavin Modified Gold Electrode
S. Rezaei-Zarchi,A. A. Saboury*,J. Hong,P. Norouzi,A. B. Moghaddam,H. Ghourchian,M. R. Ganjali,A. A. Moosavi-Movahedi,A. Javed,A. Mohammadian 대한화학회 2007 Bulletin of the Korean Chemical Society Vol.28 No.12
Electron transfer of a redox protein at a bare gold electrode is too slow to observe the redox peaks. A novel Nafion-riboflavin functional membrane was constructed during this study and electron transfer of cytochrome c, superoxide dismutase, and hemoglobin were carried out on the functional membrane-modified gold electrode with good stability and repeatability. The immobilized protein-modified electrodes showed quasi-reversible electrochemical redox behaviors with formal potentials of 0.150, 0.175, and 0.202 V versus Ag/AgCl for the cytochrome c, superoxide dismutase and hemoglobin, respectively. Whole experiment was carried out in the 50 mM MOPS buffer solution with pH 6.0 at 25 oC. For the immobilized protein, the cathodic transfer coefficients were 0.67, 0.68 and 0.67 and electron transfer-rate constants were evaluated to be 2.25, 2.23 and 2.5 s-1, respectively. Hydrogen peroxide concentration was measured by the peroxidase activity of hemoglobin and our experiment revealed that the enzyme was fully functional while immobilized on the Nafion-riboflavin membrane.