Reaction of Hg2+ Insertion into Cysteine Pairs Within Bovine Insulin Crystals Followed via Raman Spectroscopy(320 views) Caterino M, Merlino A, Balsamo A, Russo Krauss I, Parisi S, Vergara A
Keywords: Disulfide Bridges, Insulin, Mercury Binding, Protein Crystallization, Raman Spectroscopy,
Affiliations: *** IBB - CNR ***
Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario di Monte sant'Angelo, Via Cintia, 80126 Naples, Italy
CNR, Institute of Biostructures and Bioimages, Naples, Italy
Department of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy
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Park, J. D., Zheng, W., Human exposure and health effects of inorganic and elemental mercury (2012) J. Prev. Med. Public Health, 45, pp. 344-352. , 10. 3961/jpmph. 2012. 45. 6. 34
Karagas, M. R., Choi, A. L., Oken, E., Horvat, M., Schoeny, R., Kamai, E., Cowell, W., Korrick, S., Evidence on the human health effects of low-level methylmercury exposure (2012) Environ. Health Perspect., 120, p. 799806. , 10. 1289/ehp. 1104494
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Houston, M. C., Role of mercury toxicity in hypertension, cardiovascular disease, and stroke (2011) J. Clin. Hypertens. (Greenwich), 13, pp. 621-637. , 1: CAS: 528: DC%2BC3MXht1ejtrvK 10. 1111/j. 1751-7176. 2011. 00489. x
Bernhoft, R. A., Mercury toxicity and treatment: A review of the literature (2012) J. Environ. Public Health., 2012, pp. 460-508. , 10. 1155/2012/460508
Carvalho, C. M., Chew, E. H., Hashemy, S. I., Lu, J., Holmgren, A., Inhibition of the human thioredoxin system (2008) J. Biol. Chem., 283, pp. 11913-11923. , 1: CAS: 528: DC%2BD1cXltVyku7k%3D 10. 1074/jbc. M710133200
Shim, S. M., Dorworth, L., Lasrado, J., Santerre, C., Mercury and fatty acids in canned tuna, salmon, and mackerel (2004) J. Food Sci., 69, pp. 681-C684. , 1: CAS: 528: DC%2BD2cXhtFars7bN 10. 1111/j. 1365-2621. 2004. tb09915. x
Corbeil, M. C., Beauchamp, A. L., Alex, S., Savoie, R., Interaction of the methylmercury cation with glycine and alanine: A vibrational and X-ray diffraction study (1986) Can. J. Chem., 64, pp. 1876-1884. , 1: CAS: 528: DyaL2sXosFSgtQ%3D%3D 10. 1139/v86-309
Adams M., . J., Hodgkin D., . C., Raeburn U., . A., Crystal structure of a complex of mercury (II) chloride and histidine hydrochloride (1970) J. Chem. Soc. A, pp. 2632-2635
Alcock N., . W., Lampe P., . A., Moore, P., Crystal structures of methyl (L-tyrosinato) mercury (II) monohydrate and [L- (2-amino-4-phenylbutanoato)] methylmercury (II) (1978) J. Chem. Soc. Dalton Trans, pp. 1324-1328
Carey, P. R., Dong, J., Following ligand binding and ligand reactions in proteins via Raman crystallography (2004) Biochemistry, 43, pp. 8885-8893. , 1: CAS: 528: DC%2BD2cXltVKru7s%3D 10. 1021/bi049138a
Smith, G. D., Pangborn, W. A., Blessing, R. H., The structure of T6 bovine insulin (2005) Acta Crystallogr. Sect. D, 61, pp. 1476-1482. , 10. 1107/S0907444905025771
During, J. R., Cox, A. W., Spectra and structure of organophosphorus compounds. XIV. Infrared and Raman spectra, vibrational assignment and the asymmetric potential function for ethylphosphine and ethylphosphine-d2 (1975) J. Chem. Phys., 63, pp. 2303-2310. , 10. 1063/1. 431681
Hoffmann, G. G., Brockner, W., Steinfatt, I., Bis (n-alkanethiolato) mercury (II) compounds, Hg (SC n H 2n+1) 2 (n = 1 to 10, 12): Preparation methods, vibrational spectra, GC/MS investigations, and exchange reactions with diorganyl disulfides (2001) Inorg. Chem., 40, pp. 977-985. , 1: CAS: 528: DC%2BD3MXnvVOmsw%3D%3D 10. 1021/ic000638b
Fahey, R. C., Hunt, J. S., Windham, G. C., On the cysteine and cystine content of proteins. Differences between intracellular and extracellular proteins (1977) J. Mol. Evol., 10, pp. 155-160. , 1: CAS: 528: DyaE1cXjtlCmsQ%3D%3D 10. 1007/BF01751808
Hansen, R. E., Roth, D., Winther, J. R., Quantifying the global cellular thiol-disulfide status (2009) Proc. Natl. Acad. Sci. USA, 106, pp. 422-437. , 1: CAS: 528: DC%2BD1MXhtVelsb4%3D 10. 1073/pnas. 0812149106
Reaction of Hg2+ Insertion into Cysteine Pairs Within Bovine Insulin Crystals Followed via Raman Spectroscopy
Chemical modifications of protein crystals may be achieved via soaking of reactants from their precipitating solution, through the solvent channel, into the protein matrix. We describe a Raman microscopy approach to follow mercury insertion into cysteine pairs within protein single crystals, via soaking in an aqueous Hg2+ solution. The method has been developed using bovine insulin as the model system. Applying an efficient mercuration protocol, consisting of a first step of disulphide bridge TCEP-induced reduction within the crystal, followed by overnight reaction with a HgCl2 solution, we obtained Hg-derivative crystals. Raman spectra collected on these derivative crystals, kept in the mother liquor, reveal a characteristic Raman band at 335 cm(-1), which has been assigned to a -S-Hg-S- bridge. The analysis provides Raman-based markers of mercury binding to cysteines, and thus of mercury intoxication.
Reaction of Hg2+ Insertion into Cysteine Pairs Within Bovine Insulin Crystals Followed via Raman Spectroscopy
No results.
Reaction of Hg2+ Insertion into Cysteine Pairs Within Bovine Insulin Crystals Followed via Raman Spectroscopy