An EPR and voltammetric study of simple and mixed copper(II) complexes with L- or D-glutamate and L-arginate in aqueous solution (380 views) (PDF restricted 186 views)
Inorganica Chimica Acta, 2016 Lug 19; 453(2016): 62-68.
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Paper type: Journal Article,
Impact factor: 0, 5-year impact factor: 0
Url: http://dx.doi.org/10.1016/j.ica.2016.07.031
Keywords: Cw Epr, Cu(ii) Complexes, Aminoacidate Ligands, Trans Copper Conformers, Electrostatic Interactions, Swv Formal Redox Potentials,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy
CNR, Istituto di Biostrutture e Bioimmagini, Via P. Gaifami 18, 95126 Catania, Italy
References:
[1] M.J. Kan, J.E. Lee, J.G. Wilson, A.L. Everheart, C.M. Brown, A.N. Hoofnagle, M. Jansen, M.P. Vitek, M.D. Gunn, C.A. Colton, J. Neurosci. 35 (2015) 5969–5982.
[2] L. Rossi, M.F. Lombardo, M.R. Ciriolo, G. Rotilio, Neurochem. Res. 29 (2004)
[3] N. Vassallo, J. Herms, J. Neurochem. 86 (2003) 538–544.
[4] G. Rotilio, M.T. Carri, L. Rossi, M.R. Ciriolo, IUBMB Life 50 (2000) 309–314.
[5] V. Desai, S.G. Kaler, Am. J. Clin. Nutr. 88 (2008) 855S–858S.
[6] P.M. Roos, O. Vesterberg, M. Nordberg, Exp. Biol. Med. 231 (2006) 1481–1487.
[7] S.R. Platt, Vet. J. 173 (2007) 278–286.
[8] L.D. Pettit, R.J.W. Hefford, Met. Ions Biol. Syst. 9 (1979) 173–212.
[9] Y. Shimazaki, T. Yaijma, O. Yamauchi, J. Inorg. Biochem. 148 (2015) 105–115.
[10] R.P. Bonomo, R. Calì, V. Cucinotta, G. Impellizzeri, E. Rizzarelli, Inorg. Chem. 25
[11] A.E. Martell, R.M. Smith, Critical Stability Constants, Amino Acids, vol. 1, Plenum Press, New York, 1974.
[12] O. Yamauchi, Y. Nakao, A. Nakahara, Bull. Chem. Soc. Japan 48 (1975) 2572–
[13] R.F.C. Claridge, J.J. Kilpatrick, H.K.J. Powell, Aust. J. Chem. 33 (1980) 2757–
[14] R. Bregier-Jarzebowska, J. Solution Chem. 43 (2014) 2144–2162.
[15] G. Brookes, L.D. Pettit, J. Chem. Soc., Dalton Trans. (1977) 1918–1924.
[16] T. Lund, J. Vanngard, Chem. Phys. 42 (1965) 2979–2980.
[17] T. Sakurai, O. Yamauchi, A. Nakahara, Bull. Chem. Soc. Japan 51 (1978) 3203–
[18] E. Kaifer, J. Bard, J. Phys. Chem. 89 (1985) 4876–4880.
[19] N. Ohata, H. Masuda, O. Yamauchi, Inorg. Chim. Acta 302 (2000) 749–761.
[20] L. Borer, D. Gallagher, J. Ready, ChemBio News 15 (1) (2005) 40.
[21] M.S. Bukharov, V.G. Shtyrlin, A.S. Mukhtarov, G.V. Mamin, S. Stapf, C. Mattea, A. A. Krutikov, A.N. Il’in, N.Y. Serov, Chem. Phys. 16 (2014) 9411–9421.
[22] R.P. Bonomo, F. Riggi, A.J. Di Bilio, Inorg. Chem. 27 (1988) 2510–2512.
[23] R.P. Bonomo, F. Riggi, Chem. Phys. Lett. 93 (1982) 99–102.
[24] B.J. Hathaway, D.E. Billing, Coord. Chem. Rev. 5 (1970) 143–207.
[25] J.E. Wertz, J.R. Bolton, Electron Spin Resonance. Elementary Theory and Practical Applications, Mac Graw Hill, New York, 1972.
[26] B.A. Goodman, D.B. McPhail, H. Kipton, J. Powell, J. Chem. Soc., Dalton Trans.
[27] H.A. Kuska, M.T. Rogers, Electron Spin Resonance of Transition Metal Complex Ions, Coordination Chemistry, in: A.E. Martell (Ed.), ACS Monograph, vol. 1, Van Nostrand Reinhold Company, New York, 1971.
[28] H. Masuda, A. Odani, T. Yamazaki, T. Yajima, O. Yamauchi, Inorg. Chem. 32
[29] P. Pary, L.N. Bengoa, W.A. Egli, J. Electrochem. Soc. 162 (2015) D275–D282.
[30] G. Tabbì, A. Giuffrida, R.P. Bonomo, J. Inorg. Biochem. 128 (2013) 137–145.
[31] T. Weiser, M. Wienrich, Brain Res. 742 (1996) 211–218.
Inorganica Chimica Acta, 2016 Lug 19; 453(2016): 62-68.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 0, 5-year impact factor: 0
Url: http://dx.doi.org/10.1016/j.ica.2016.07.031
Keywords: Cw Epr, Cu(ii) Complexes, Aminoacidate Ligands, Trans Copper Conformers, Electrostatic Interactions, Swv Formal Redox Potentials,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Università degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy
CNR, Istituto di Biostrutture e Bioimmagini, Via P. Gaifami 18, 95126 Catania, Italy
References:
[1] M.J. Kan, J.E. Lee, J.G. Wilson, A.L. Everheart, C.M. Brown, A.N. Hoofnagle, M. Jansen, M.P. Vitek, M.D. Gunn, C.A. Colton, J. Neurosci. 35 (2015) 5969–5982.
[2] L. Rossi, M.F. Lombardo, M.R. Ciriolo, G. Rotilio, Neurochem. Res. 29 (2004)
[3] N. Vassallo, J. Herms, J. Neurochem. 86 (2003) 538–544.
[4] G. Rotilio, M.T. Carri, L. Rossi, M.R. Ciriolo, IUBMB Life 50 (2000) 309–314.
[5] V. Desai, S.G. Kaler, Am. J. Clin. Nutr. 88 (2008) 855S–858S.
[6] P.M. Roos, O. Vesterberg, M. Nordberg, Exp. Biol. Med. 231 (2006) 1481–1487.
[7] S.R. Platt, Vet. J. 173 (2007) 278–286.
[8] L.D. Pettit, R.J.W. Hefford, Met. Ions Biol. Syst. 9 (1979) 173–212.
[9] Y. Shimazaki, T. Yaijma, O. Yamauchi, J. Inorg. Biochem. 148 (2015) 105–115.
[10] R.P. Bonomo, R. Calì, V. Cucinotta, G. Impellizzeri, E. Rizzarelli, Inorg. Chem. 25
[11] A.E. Martell, R.M. Smith, Critical Stability Constants, Amino Acids, vol. 1, Plenum Press, New York, 1974.
[12] O. Yamauchi, Y. Nakao, A. Nakahara, Bull. Chem. Soc. Japan 48 (1975) 2572–
[13] R.F.C. Claridge, J.J. Kilpatrick, H.K.J. Powell, Aust. J. Chem. 33 (1980) 2757–
[14] R. Bregier-Jarzebowska, J. Solution Chem. 43 (2014) 2144–2162.
[15] G. Brookes, L.D. Pettit, J. Chem. Soc., Dalton Trans. (1977) 1918–1924.
[16] T. Lund, J. Vanngard, Chem. Phys. 42 (1965) 2979–2980.
[17] T. Sakurai, O. Yamauchi, A. Nakahara, Bull. Chem. Soc. Japan 51 (1978) 3203–
[18] E. Kaifer, J. Bard, J. Phys. Chem. 89 (1985) 4876–4880.
[19] N. Ohata, H. Masuda, O. Yamauchi, Inorg. Chim. Acta 302 (2000) 749–761.
[20] L. Borer, D. Gallagher, J. Ready, ChemBio News 15 (1) (2005) 40.
[21] M.S. Bukharov, V.G. Shtyrlin, A.S. Mukhtarov, G.V. Mamin, S. Stapf, C. Mattea, A. A. Krutikov, A.N. Il’in, N.Y. Serov, Chem. Phys. 16 (2014) 9411–9421.
[22] R.P. Bonomo, F. Riggi, A.J. Di Bilio, Inorg. Chem. 27 (1988) 2510–2512.
[23] R.P. Bonomo, F. Riggi, Chem. Phys. Lett. 93 (1982) 99–102.
[24] B.J. Hathaway, D.E. Billing, Coord. Chem. Rev. 5 (1970) 143–207.
[25] J.E. Wertz, J.R. Bolton, Electron Spin Resonance. Elementary Theory and Practical Applications, Mac Graw Hill, New York, 1972.
[26] B.A. Goodman, D.B. McPhail, H. Kipton, J. Powell, J. Chem. Soc., Dalton Trans.
[27] H.A. Kuska, M.T. Rogers, Electron Spin Resonance of Transition Metal Complex Ions, Coordination Chemistry, in: A.E. Martell (Ed.), ACS Monograph, vol. 1, Van Nostrand Reinhold Company, New York, 1971.
[28] H. Masuda, A. Odani, T. Yamazaki, T. Yajima, O. Yamauchi, Inorg. Chem. 32
[29] P. Pary, L.N. Bengoa, W.A. Egli, J. Electrochem. Soc. 162 (2015) D275–D282.
[30] G. Tabbì, A. Giuffrida, R.P. Bonomo, J. Inorg. Biochem. 128 (2013) 137–145.
[31] T. Weiser, M. Wienrich, Brain Res. 742 (1996) 211–218.
An EPR and voltammetric study of simple and mixed copper(II) complexes with L- or D-glutamate and L-arginate in aqueous solution
EPR CW measurements at room and low temperature have been carried out on the systems containing
63copper(II) nitrate, L-Arg and L-or D-Glu or DL- racemic mixtures of both amino acids in aqueous solution
or in mixed solvents. For these copper(II) bis and ternary complexes, RT EPR spectra revealed that mixtures
of cis and trans conformers are really present in aqueous solution. In most cases, for these systems,
the cis conformer is more abundant at the lowest temperature (275 K). Increasing gradually the temperature
from 275 K to 305 K the cis/trans ratio tends towards the trans conformer. This latter is less abundant
in the case of [Cu(L-Glu)2], because of the possible interaction of negative side chain carboxylate
anions with the water molecules axially bound, and for [Cu(L-Arg)(D-Glu)], probably owing to a possible
electrostatic interaction between the two opposite charged side chains which are on the same side of the
CuN2O2 coordination plane. Low temperature frozen solution EPR spectra run on these systems show
the presence of only one absorbing specie thus giving reason to the stabilization of one conformer over
the other, in particular, the cis conformer. There are no evident differences in the anisotropic Spin
Hamiltonian parameters derived from the frozen EPR solution spectra of these systems, which are
characterized by a tetragonally elongated octahedral stereochemistry. SWV measurements confirmed
the EPR spectroscopic data, actually giving rise to the observation of slightly asymmetrical peaks, which
revealed two near formal redox potentials assigned to the two conformers.
EPR CW measurements at room and low temperature have been carried out on the systems containing
63copper(II) nitrate, L-Arg and L-or D-Glu or DL- racemic mixtures of both amino acids in aqueous solution
or in mixed solvents. For these copper(II) bis and ternary complexes, RT EPR spectra revealed that mixtures
of cis and trans conformers are really present in aqueous solution. In most cases, for these systems,
the cis conformer is more abundant at the lowest temperature (275 K). Increasing gradually the temperature
from 275 K to 305 K the cis/trans ratio tends towards the trans conformer. This latter is less abundant
in the case of [Cu(L-Glu)2], because of the possible interaction of negative side chain carboxylate
anions with the water molecules axially bound, and for [Cu(L-Arg)(D-Glu)], probably owing to a possible
electrostatic interaction between the two opposite charged side chains which are on the same side of the
CuN2O2 coordination plane. Low temperature frozen solution EPR spectra run on these systems show
the presence of only one absorbing specie thus giving reason to the stabilization of one conformer over
the other, in particular, the cis conformer. There are no evident differences in the anisotropic Spin
Hamiltonian parameters derived from the frozen EPR solution spectra of these systems, which are
characterized by a tetragonally elongated octahedral stereochemistry. SWV measurements confirmed
the EPR spectroscopic data, actually giving rise to the observation of slightly asymmetrical peaks, which
revealed two near formal redox potentials assigned to the two conformers.
An EPR and voltammetric study of simple and mixed copper(II) complexes with L- or D-glutamate and L-arginate in aqueous solution
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An EPR and voltammetric study of simple and mixed copper(II) complexes with L- or D-glutamate and L-arginate in aqueous solution
Other filter: ([btitle,keywords] "Cu(ii) Complexes" OR ...
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* Structural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability (526 views)
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Impact Factor: 4.882
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* Chemical Denaturation Of The Elongation Factor 1 Alpha Isolated From The Hyperthermophilic Archaeon Sulfolobus Solfataricus (343 views)
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Impact Factor: 3.633
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Tabbì G, Driessen WL, Reedijk J, Bonomo RP, Veldman N, Spek AL
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3 Records (3 excluding Abstracts).
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Total 5 year impact factor: 12.113 (12.113 excluding Abstracts).
Total impact factor: 11.251 (11.251 excluding Abstracts).
Total 5 year impact factor: 12.113 (12.113 excluding Abstracts).
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