Abstract
The novel binucleating ligand, 6,6 prime-methylene-bis(5 prime-amino-3 prime,4 prime-benzo-2 prime-thiapentyl)-1,11-diamino-2,3:9,10-dibenzo-4,8-dithiaundecane (H4L) was prepared and reacted with copper(II) salts in dry MeOH to yield mixtures of copper(I) and copper(II) complexes with Cl- and ClO-4 counter ions. The amine functions on the ligand release protons to form copper(I) complexes: (Cu2L)X2, where X=Cl−, ClO4-. The complexes were oxidized to (Cu2L)X4 with H2O2 in DMF; Cu(NO3)2 gave a different complex, [Cu2(H4L)(NO3)2](NO3)2, as regards proton releasing ability, coordination and oxidation number. Evidence for the structures of this new tetraamino-tetrathioether ligand and its copper complexes is provided by 1H-, 13C-n.m.r., mass, u.v.–vis., i.r. spectra, elemental analyses, molar conductivities and magnetic moments.
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S. R. Collinson and D. E. Fenton, Coord. Chem. Rev., 148, 19 (1996).
H. A. Hill, Chem. Br., 12, 119 (1976).
J. A. Fee, Struct. Bonding, 23, 1 (1975).
A. C. Cope and F. Kagan, J. Am. Chem. Soc., 80, 5499 (1958).
D. E. Fenton, U. Casellato, P. A. Vigato and M. Vidali, Inorg. Chim. Acta, 62, 57 (1982).
L. Borer and E. Sinn, Inorg. Chim. Acta, 142, 197 (1988).
P. A. Vigato, S. Tamburini and D. E. Fenton, Coord. Chem. Rev., 106, 25 (1990).
J. Peisah, P. Alsen and W. E. Blumberg, in The Biochemistry of Copper, Academic Press, New York, 1966.
W. H. Vanneste and A. Zuberbühler in O. Hayaishi (Ed.), Molecular Mechanisms of Oxygen Activation, Academic Press, New York, 1974, p. 3.
R. Malkin In G. L. Eichhorn (Ed.), Inorganic Biochemistry, Elsevier, New York, 1973, p. 689.
W. S. Caughey, W. J. Wallace, J. A. Volpe and S. Yoshikawa, Enzymes, 12, 299 (1975).
O. Farver, M. Goldberg, D. Lancet and I. Pecht, Biochem. Biophys. Res. Commun., 73, 494 (1976).
G. McLendon and A. E. Martell, J. Inorg. Nucl. Chem., 39, 191 (1977).
H. A. O. Hill and B. E. Smith, Biochem. Biophys. Res. Commun., 81, 1201 (1978).
P. M. Coleman, H. C. Freeman, J. M. Guss, M. Murata, V. A. Norris, J. A. M. Ramshaw and M. P. Venkatappa, Nature, 272, 319 (1978).
E. T. Adam, R. E. Stenkamp, L. C. Seiker and L. H. Jensen, J. Mol. Biol., 125, 35 (1978).
R. Malkin and B. G. Malmstrom, Adv. Enzymol., 33, 177 (1970).
V. Sailasuta, F. C. Anson and H. B. Gray, J. Am. Chem. Soc., 101, 455 (1979).
M. Czugler and E. Weber, J. Chem. Soc., Chem. Commun., 472 (1981).
A. McAuley, G. Subramanian and T. W. Whitcombe, J. Chem. Soc., Chem. Commun., 539 (1987).
A. T. Philip, Aust. J. Chem., 21, 2301 (1968).
L. R. Gahan, K. E. Hart, C. H. L. Kennard, M. A. Kingston, G. Smith and T. C. W. Mak, Inorg. Chim. Acta, 116, 15 (1986).
T. M. Donlevy, L. R. Gahan, T. W. Hambley, G. R. Hanson, A. Markievicz, K. S. Murray, I. L. Swann and S. R. Pickering, Aust. J. Chem., 43, 1407 (1990).
S. Karaböcek, S. Güner and N. Karaböcek, J. Inorg. Biochem., 66, 57 (1997).
S. Kitagawa, M. Munakata and A. Higashie, Inorg. Chim. Acta, 84, 79 (1984).
W. K. Musker, M. M. Olmstead, R. M. Kessler, M. B. Murphy, C. H. Neagley, P. B. Roush, N. L. Hill, T. L. Wolford, H. Hope, G. Delker, K. Swanson and B. V. Gorewit, J. Am. Chem. Soc., 102, 1225 (1980).
J. R. Boehm, A. L. Birch, K. R. Bizot and R. Enemark, J. Am. Chem. Soc., 97, 501 (1975).
Y. Gök, S. Karaböcek and M. N. Misir, Transition Met. Chem., 21, 1 (1996).
M. T. H. Tarafter, M. A. Jalil Miah and R. N. Bose, J. Inorg, Nucl. Chem., 43, 3151 (1981).
M. R. Rosenthall, J. Chem. Educ., 50, 331 (1973).
N. F. Curtis and Y. M. Curtis, Inorg. Chem., 4, 804 (1965).
S. Pal, G. Mukherjee and S. N. Poddar, Transition Met. Chem., 19, 99 (1994).
K. A. Foster, D. R. Brown, M. D. Timken, D. G. van Derveer, R. L. Belford and E. K. Barefield, J. Coord. Chem., 19, 123 (1988).
R. E. Coffman and G. R. Buettner, J. Phys. Chem., 83, 2387 (1979).
K. Matsumoto, I. Fukutomi, I. Kinoshita and S. I. Ooi, Inorg. Chim. Acta, 158, 201 (1989).
J. T. Spence, M. Minelli and P. Kroneck, J. Am. Chem. Soc., 102, 4538 (1980).
H. Spies and H. J. Pietzch, Inorg. Chim. Acta, 161, 151 (1989).
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Karabocek, S., Guner, S. & Karabocek, N. Models for copper proteins. Copper(I) and (II) complexes of a novel binucleating tetraamino-tetrathioether ligand. Transition Metal Chemistry 23, 159–163 (1998). https://doi.org/10.1023/A:1006951211206
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DOI: https://doi.org/10.1023/A:1006951211206