Abstract
The heme–imidazole–sodium dodecyl sulfate (SDS) ternary complex has been designed as a peroxidase-like nano-artificial enzyme, in which the imidazole moiety functions like the histidine ligand in the native horseradish peroxidase (HRP) and increases the reactivity and catalytic efficiency of the designed artificial enzyme by promoting the heterolytic cleavage of hydrogen peroxide. In the present study, three different ligands were used as the imidazole-based ligands in the heme–ligand–SDS ternary system: (1) 1-methylsulfonyl-1H-imidazole, (2) 1-(benzensulfonyl)-1H-imidazole, and (3) 1-tosyl-1H-imidazole (TsIm). The three different ligands gave variable reactivity in the system studied, and the enzymatic activation parameters, using spectrophotometric measurements, showed that the TsIm ligand had a higher catalytic efficiency at 26.38 % of the native HRP efficiency. To investigate the increase in catalytic activity, its mechanism was explored based on the original mechanism of HRP and the structure of its first catalytic intermediate (compound I). Based on the mechanism of HRP and the structure of compound I, a suggested mechanism for Tslm is as follows: the TsIm cation radical makes up part of the compound I structure, which is stabilized in the enzymatic process by charge distribution that is induced via phenyl and methyl groups. Suicide inactivation of heme–TsIm–SDS and heme–imidazole–SDS models was also compared to each other. Suicide inactivation was less exhibited in the presence of TsIm than imidazole in this system unless high concentrations of hydrogen peroxide were used.
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References
J. Bjerre, C. Rousseau, L. Marinescu, M. Bols, Appl. Microbiol. Biotechnol. 1, 81 (2008)
R. Breslow, Chem. Soc. Rev. 553, 1 (1972)
T. Kunitake, S. Shinkai, Adv. Phys. Org. Chem. 435, 17 (1980)
N. Kamiya, M. Goto, S. Furusaki, Biotechnol. Bioeng. 502, 64 (1999)
J.A. Laszlo, D.L. Compton, Mol. Catal. B Enzym. 109, 18 (2002)
M. Tohjo, Y. Nakamura, K. Kurihara, T. Samejima, Y. Hachimori, K. Shibat, Arch. Biochem. Biophys. 222, 99 (1962)
I. Bertini, A. Sigel, Handbook on Metalloproteins (Marcel and Dekker, New York, 2001), pp. 269–341
A.A. Moosavi-Movahedi, F. Semsarha, H. Heli, K. Nazari, H. Ghourchian, J. Hong, G.H. Hakimelahi, A.A. Saboury, Y. Sefidbakht, Colloids Surf. A Physicochem. Eng. Aspects. 213, 320 (2008)
H. Groger, J. Wilken, Angew. Chem. Int. Ed. Engl. 529, 40 (2001)
B. Meunier, Biomimetic Oxidations Catalyzed by Transition Metal Complexes (Imperial College Press, London, 2000), p. 171
W.B. Motherwell, M.J. Bingham, Y. Six, Tetrahedron 4663, 57 (2001)
Y. El Khoury, P. Hellwig, J. Biol. Inorg. Chem. 14, 23 (2009)
H. Gharibi, Z. Moosavi-Movahedi, S. Javadian, Kh Nazari, A.A. Moosavi-Movahedi, J. Phys. Chem. B. 4671, 115 (2011)
Y. Murakami, J-i Kikuchi, Y. Hisaeda, O. Hayashida, Chem. Rev. 721, 96 (1996)
S. Mazumdar, O.K. Medhi, S. Mitra, Inorg. Chem. 2541, 27 (1988)
H.M. Marques, Dalton Trans. 4371, 39 (2007)
T.L. Poulos, J. Kraut, Biol. Chem. 8199, 255 (1980)
M.N. Soltani Rad, A. Khalafi-Nezhad, S. Behrouz, M.A. Faghihi, A. Zare, A. Parhami, Tetrahedron 1778, 64 (2008)
J. Beck, J.S. Vartuli, J.C. Roth, W.J. Leonowicz, M.E. Kresge, C.T. Schmitt, K.D. Chu, C.T.W. Olson, D.H. Sheppard, E.W. McCullen, S.B. Higgins, J.B. Schlenker, J. Am. Chem. Soc. 10834, 114 (1992)
A.A. Moosavi-Movahedi, K. Nazari, M. Ghadermarzi, Ital. J. Biochem. 9, 48 (1999)
S. Mazumdar, S. Mitra, S. Struct, Bonding (Berlin) 116, 81 (1993)
F. Otón, A. Tárraga, P. Molina, Org. Biomol. Chem. 1711, 10 (2011)
J.H. Dowson, Science 434, 240 (1988)
P. Battioni, J.R. Renaud, J.F. Bartoli, M. Reina-Artiles, M. Fort, D. Mansuy, J. Am. Chem. Soc. 8462, 110 (1988)
J. Simplicio, Biochemistry 2525, 11 (1972)
DE Metzler, Biochemistry: The Chemical Reactions of Living Cells, 2nd edn (Academic Press, New York, 2003), p. 455
R. Quilez, S. de Lauzon, B. Desfosses, D. Mansuy, J.-P. Mahy, FEBS Lett. 73, 359 (1996)
A.N.P. Hiner, E.L. Raven, R.N.F. Thorneley, F. Garc′ıa-Ca′novas, J.N. Rodr′ıguez-Lo′pez, J. Inorg. Biochem. 91, 27 (2002)
M. Khosraneh, A. Mahmoudi, H. Rahimi, Kh Nazari, A.A. Moosavi-Movahedi, J. Enzyme Inhib, Med. Chem. 677, 22 (2007)
M. Ghadermarzi, A.A. Moosavi-Movahedi, Ital. J. Biochem. 197, 46 (1997)
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The financial supports of Research Council of University of Tehran, Iran National Science Foundation, Center of Excellence in Biothermodynamics (CEBiotherm) are gratefully are acknowledged.
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Ahmadzade Kermani, H., Shockravi, A., Moosavi-Movahedi, Z. et al. A surfactant–heme–sulfonyl imidazole system as a nano-artificial enzyme. J IRAN CHEM SOC 10, 961–968 (2013). https://doi.org/10.1007/s13738-013-0233-5
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DOI: https://doi.org/10.1007/s13738-013-0233-5