Spectroscopic investigation on molecular aspects and structural and functional effects of tetraethyl pyrophosphate organophosphorus insecticide interaction with adult human hemoglobin

References

• Abbasi-Tajarag, K., Divsalar, A., Saboury, A. A., Ghalandari, B., & Ghourchian, H. (2016). Destructive effect of anticancer oxali-palladium on heme degradation through the generation of endogenous hydrogen peroxide. Journal of Biomolecular Structure & Dynamics, 34(11), 2493–2504. https://doi.org/10.1080/07391102.2015.1121408
   PubMed Web of Science ®Google Scholar
• Alcantara, R. E., Xu, C., Spiro, T. G., & Guallar, V. (2007). A quantum-chemical picture of hemoglobin affinity. Proceedings of the National Academy of Sciences of the United States of America, 104(47), 18451–18455. https://doi.org/10.1073/pnas.0706026104
   PubMed Web of Science ®Google Scholar
• Ali, I., & Naseem, I. (2002). Hemolysis of human red blood cells by combination of riboflavin and aminophylline. Life Sciences, 70(17), 2013–2022. https://doi.org/10.1016/s0024-3205(01)01540-5
   PubMed Web of Science ®Google Scholar
• Amjadi, R., Ghourchian, H., Moosavi-Movahedi, A. A., & Banaie, A. (2015). Aggregation of adult and fetal hemoglobin by ingested nitrate anions. Pardis Science Tehran University, Progress in Biological Sciences, 5(2), 261–271.
   Google Scholar
• Ariaeenejad, S., Habibi-Rezaei, M., Jamili, S., Fatemi, M. R., Poursasan, N., Ahmad, F., Sheibani, N., Kavousi, K., & Moosavi-Movahedi, A. A. (2012). Biochemical characterization of hemoglobins from Caspian Sea sturgeons (Acipenser persicus and Acipenser stellatus). Cell Biochemistry and Biophysics, 62(1), 73–81. https://doi.org/10.1007/s12013-011-9261-x
   PubMed Web of Science ®Google Scholar
• Benesch, R. E., Benesch, R., & Yung, S. (1973). Equations for the spectrophotometric analysis of hemoglobin mixtures. Analytical Biochemistry, 55(1), 245–248. https://doi.org/10.1016/0003-2697(73)90309-6
   PubMed Web of Science ®Google Scholar
• Benesi, H. A., & Hildebrand, J. H. (1949). A spectrophotometric investigation of the interaction of iodine with aromatic hydrocarbons. Journal of the American Chemical Society, 71(8), 2703–2707. https://doi.org/10.1021/ja01176a030
   Web of Science ®Google Scholar
• Briehl, R. W., & Hobbs, J. F. (1970). Ultraviolet difference spectra in human hemoglobin I. Difference spectra in hemoglobin A and their relation to the function of hemoglobin. The Journal of Biological Chemistry, 245(3), 544–554.
   PubMed Web of Science ®Google Scholar
• Burtis, C. A., Ashwood, E. R., & Bruns, D. E. (2012). Tietz textbook of clinical chemistry and molecular diagnostics (pp. 1-1888).
   Google Scholar
• Cai, S., & Singh, B. R. (2004). A distinct utility of the amide III infrared band for secondary structure estimation of aqueous protein solutions using partial least squares methods. Biochemistry, 43(9), 2541–2549. https://doi.org/10.1021/bi030149y
   PubMed Web of Science ®Google Scholar
• Colovic, M. B., Krstic, D. Z., Lazarevic-Pasti, T. D., Bondzic, A. M., & Vasic, V. M. (2013). Acetylcholinesterase inhibitors: Pharmacology and toxicology. Current Neuropharmacology, 11(3), 315–335. https://doi.org/10.2174/1570159X11311030006
   PubMed Web of Science ®Google Scholar
• Considine, D. M., & Considine, G. D. (1982). Foods and food production encyclopedia (pp. 1–125). Springer US. https://doi.org/10.1007/978-1-4684-8511-0_1
   Google Scholar
• Cui, Y., Guo, J., Xu, B., & Chen, Z. (2006). Binding of chlorpyrifos and cypermethrin to blood proteins. Pesticide Biochemistry and Physiology 85(2), 110–114.
   Web of Science ®Google Scholar
• Ding, F., Han, B. Y., Liu, W., Zhang, L., & Sun, Y. (2010). Interaction of imidacloprid with hemoglobin by fluorescence and circular dichroism. Journal of Fluorescence, 20(3), 753–762. https://doi.org/10.1007/s10895-010-0618-0
   PubMed Web of Science ®Google Scholar
• Dohare, N., Siddiquee, M. A., din Parray, M., Kumar, A., & Patel, R. (2020). Esterase activity and interaction of human hemoglobin with diclofenac sodium: A spectroscopic and molecular docking study. Journal of Molecular Recognition, 33(8), e2841 (1–11). https://doi.org/10.1002/jmr.2841
   Google Scholar
• Edson, K. F. (1961). Applied toxicology of pesticides. International Journal of Pest Management: Part A, 7(2–3), 233–245. https://doi.org/10.1080/04345546109415009
   Google Scholar
• Emadi, M., Maghami, P., Khorsandi, K., & Hosseinzadeh, R. (2019). Biophysical study on the interaction of cartap hydrochloride and hemoglobin: Heme degradation and functional changes of protein. Journal of Biochemical and Molecular Toxicology, 33(7), e22325 (1-10). https://doi.org/10.1002/jbt.22325
   Google Scholar
• Faust, J. (1949). Poisoning due to tetraethylpyrophosphate. Journal of the American Medical Association, 141(3), 192. https://doi.org/10.1001/jama.1949.62910030001006
   PubMed Web of Science ®Google Scholar
• Frawley, J. P., Hagan, E. C., & Fitzhugh, G. (1952). A comparative pharmacological and toxicological study of organic phosphate-anticholinesterase compounds. Citeseer, 105(2),156–165.
   Google Scholar
• Ghisaidoobe, A., & Chung, S. (2014). Intrinsic tryptophan fluorescence in the detection and analysis of proteins: A focus on förster resonance energy transfer techniques. International Journal of Molecular Sciences, 15(12), 22518–22538. https://doi.org/10.3390/ijms151222518
   PubMed Web of Science ®Google Scholar
• Grigoryan, K., & Sargsyan, L. (2014). Denaturation of hemoglobin in the presence of tannic acid. Proceedings of the Yerevan State University, 1, 23–27.
   Google Scholar
• Horecker, B. L. (1943). The absorption spectra of hemoglobin and its derivatives in the visible and near infra-red regions. Journal of Biological Chemistry, 148(1), 173–183.
   Google Scholar
• Hosseinzadeh, R., & Moosavi-Movahedi, A. A. (2016). Human hemoglobin structural and functional alterations and heme degradation upon interaction with benzene: A spectroscopic study. Spectrochimica Acta Part A, Molecular and Biomolecular Spectroscopy, 157, 41–49. https://doi.org/10.1016/j.saa.2015.12.014
   PubMed Web of Science ®Google Scholar
• Hosseinzadeh, R., Moosavi Movahedi, A. A., & Ghourchian, H. (2014). New insight on biological interaction analysis: New nanocrystalline mixed metal oxide SPME fiber for GC-FID analysis of BTEX and its application in human hemoglobin-benzene interaction studies. PloS One, 9(7), e102992–318. https://doi.org/10.1371/journal.pone.0102992
   PubMed Web of Science ®Google Scholar
• Kamimura, H., Matsumoto, A., Miyazaki, Y., & Yamamoto, I. (2014). Agricultural and biological chemistry studies on nicotinoids as an insecticide part IV. Relation of Structure to Toxicity of Pyridylmethylamines, 27(10), 684–688. https://doi.org/10.1080/00021369.1963.10858171
   Google Scholar
• Kenoth, R., Simanshu, D. K., Kamlekar, R. K., Pike, H. M., Molotkovsky, J. G., Benson, L. M., Bergen, H. R., Prendergast, F. G., Malinina, L., Venyaminov, S. Y., Patel, D. J., & Brown, R. E. (2010). Structural determination and tryptophan fluorescence of heterokaryon incompatibility C2 protein (HET-C2), a fungal glycolipid transfer protein (GLTP), provide novel insights into glycolipid specificity and membrane interaction by the GLTP fold. The Journal of Biological Chemistry, 285(17), 13066–13078. https://doi.org/10.1074/jbc.M109.093203
   PubMed Web of Science ®Google Scholar
• Kong, J., & Yu, S. (2007). Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochimica et Biophysica Sinica, 39(8), 549–559. https://doi.org/10.1111/j.1745-7270.2007.00320.x
   PubMed Web of Science ®Google Scholar
• Konigsberg, W., & Hilly, R. J. (1962). The structure of human hemoglobin III. The sequence of amino acids in the tryptic peptides of the OL chain. The Journal of Biological Chemistry, 237, 2547–2561.
   Web of Science ®Google Scholar
• Laskowski, R. A., & Swindells, M. B. (2011). LigPlot+: Multiple ligand-protein interaction diagrams for drug discovery. Journal of Chemical Information and Modeling, 51(10), 2778–2786. https://doi.org/10.1021/ci200227u
   PubMed Web of Science ®Google Scholar
• Li, T., Bonkovsky, H. L., & Guo, J. T. (2011). Structural analysis of heme proteins: Implications for design and prediction. BMC Structural Biology, 11(1), 13. https://doi.org/10.1186/1472-6807-11-13
   PubMedGoogle Scholar
• Malarkani, K., Sarkar, I., & Selvam, S. (2018). Denaturation studies on bovine serum albumin-bile salt system: Bile salt stabilizes bovine serum albumin through hydrophobicity. Journal of Pharmaceutical Analysis, 8(1), 27–36. https://doi.org/10.1016/j.jpha.2017.06.007
   PubMed Web of Science ®Google Scholar
• Marengo-Rowe, A. J. (2006). Structure-function relations of human hemoglobins. Proceedings (Baylor University Medical Center), 19(3), 239–245. https://doi.org/10.1080/08998280.2006.11928171
   PubMedGoogle Scholar
• Nagababu, E., & Rifkind, J. M. (1998). Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide. Biochemical and Biophysical Research Communications, 247(3), 592–596. https://doi.org/10.1006/bbrc.1998.8846
   PubMed Web of Science ®Google Scholar
• Nagababu, E., & Rifkind, J. M. (2004). Heme degradation by reactive oxygen species. Antioxidants & Redox Signaling, 6(6), 967–978. https://doi.org/10.1089/ars.2004.6.967
   PubMed Web of Science ®Google Scholar
• Najdegerami, I. H., Maghami, P., Sheikh-Hasani, V., Hosseinzadeh, G., Sheibani, N., & Moosavi-Movahedi, A. A. (2017). Antichaperone activity and heme degradation effect of methyl tert-butyl ether (MTBE) on normal and diabetic hemoglobins. Journal of Molecular Recognition, 30(5), e2596. https://doi.org/10.1002/jmr.2596
   Web of Science ®Google Scholar
• Pan, T., Peng, A., Huang, W., Yin, H., & Han, Y. (2011). FTIR/ATR spectroscopy applied to the rapid analysis for hemoglobin in human soluble blood samples. In 2011 Third International Conference on Measuring Technology and Mechatronics Automation (pp. 268–271). IEEE. https://doi.org/10.1109/ICMTMA.2011.354
   Google Scholar
• Perutz, M. F. (1978). Hemoglobin structure and respiratory transport. JSTOR, 239, 92–125.
   Google Scholar
• Reeder, D. H. (1961). Organic phosphate insecticide poisoning. Journal of Occupational and Environmental Medicine, 3(3), 129–131.
   Google Scholar
• Reza, D. M., Akbar, M.-M., Parviz, N., Ghourchian, Hedayat-Olah, & Shahrokh, S. (2002). Inhibition of human hemoglobin autoxidation by sodium n-dodecyl sulphate. Journal of Biochemistry and Molecular Biology, 35(4), 364–370.
   PubMedGoogle Scholar
• Riggs, A. (1981). Preparation of blood hemoglobins of vertebrates (pp. 5–29). https://doi.org/10.1016/0076-6879(81)76111-1
   Google Scholar
• Roberts, S., James, R., & Williams, P. (2014). Principles of toxicology: Environmental and industrial applications.
   Google Scholar
• Roumenina, L. T., Lacroix-Desmazes, S., & Dimitrov, J. D. (2016). Heme: Modulator of plasma systems in hemolytic diseases. Trends in Molecular Medicine, 22(3), 200–213. https://doi.org/10.1016/j.molmed.2016.01.004
   Google Scholar
• Salehi, N., Moosavi-Movahedi, A. A., Fotouhi, L., Yousefinejad, S., Shourian, M., Hosseinzadeh, R., Sheibani, N., & Habibi-Rezaei, M. (2014). Heme degradation upon production of endogenous hydrogen peroxide via interaction of hemoglobin with sodium dodecyl sulfate. Journal of Photochemistry and Photobiology B, Biology, 133(0), 11–17. https://doi.org/10.1016/j.jphotobiol.2014.02.014
   PubMedGoogle Scholar
• Savino, C., Miele, A. E., Draghi, F., Johnson, K. A., Sciara, G., Brunori, M., & Vallone, B. (2009). Pattern of cavities in globins: The case of human hemoglobin. Biopolymers, 91(12), 1097–1107. https://doi.org/10.1002/bip.21201
   PubMed Web of Science ®Google Scholar
• Shaanan, B. (1982). The iron-oxygen bond in human oxyhaemoglobin. Nature, 296(5858), 683–684. https://doi.org/10.1038/296683a0
   PubMed Web of Science ®Google Scholar
• Simion, A.-M., Aprodu, I., Dumitrașcu, L., Bahrim, G. E., Alexe, P., & Stănciuc, N. (2015). Exploring the heat-induced structural changes of β-lactoglobulin-linoleic acid complex by fluorescence spectroscopy and molecular modeling techniques. Journal of Food Science and Technology, 52(12), 8095–8103. https://doi.org/10.1007/s13197-015-1949-2
   PubMed Web of Science ®Google Scholar
• Singh, B. R., DeOliveira, D. B., Fu, F.-N., & Fuller, M. P. (1993). Fourier transform infrared analysis of amide III bands of proteins for the secondary structure estimation. In L. A. Nafie & H. H. Mantsch (Eds.), Biomolecular spectroscopy III (Vol. 1890, pp. 47–55). https://doi.org/10.1117/12.145242
   Google Scholar
• Sowemimo-Coker, S. O. (2002). Red blood cell hemolysis during processing. Transfusion Medicine Reviews, 16(1), 46–60. https://doi.org/10.1053/tmrv.2002.29404
   PubMed Web of Science ®Google Scholar
• Trott, O., & Olson, A. J. (2010). Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. Journal of Computational Chemistry, 31(2), 455–461.
   PubMed Web of Science ®Google Scholar
• Uddin, M. H., Shahjahan, M., Ruhul Amin, A. K. M., Haque, M. M., Islam, M. A., & Azim, M. E. (2016). Impacts of organophosphate pesticide, sumithion on water quality and benthic invertebrates in aquaculture ponds. Aquaculture Reports, 3, 88–92. https://doi.org/10.1016/j.aqrep.2016.01.002
   Web of Science ®Google Scholar
• Urry, D. W. (1967). The heme chromophore in the ultraviolet. The Journal of Biological Chemistry, 242.
   PubMed Web of Science ®Google Scholar
• Wang, Y.-Q., Zhang, H.-M., Zhang, G.-C., Liu, S.-X., Zhou, Q.-H., Fei, Z.-H., & Liu, Z.-T. (2007). Studies of the interaction between paraquat and bovine hemoglobin. International Journal of Biological Macromolecules, 41(3), 243–250. https://doi.org/10.1016/j.ijbiomac.2007.02.011
   PubMed Web of Science ®Google Scholar