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X-ray powder diffraction data of the novel copper and iron complexes as models for the active site in metalloproteins

Published online by Cambridge University Press:  06 March 2012

V. G. Vlasenko ,
A. T. Shuvaev ,
V. A. Shuvaeva  and
A. I. Uraev
V. G. Vlasenko*
Affiliation:
Institute of Physics, Rostov State University, 344090 Stachki Avenue 194, Rostov-on-Don, Russia
A. T. Shuvaev
Affiliation:
Institute of Physics, Rostov State University, 344090 Stachki Avenue 194, Rostov-on-Don, Russia
V. A. Shuvaeva
Affiliation:
Institute of Physics, Rostov State University, 344090 Stachki Avenue 194, Rostov-on-Don, Russia
A. I. Uraev
Affiliation:
Institute of Physical and Organic Chemistry, Rostov State University, 344090 Stachki Avenue 194/2, Rostov-on-Don, Russia
*
a)Electronic mail: [email protected]
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Abstract

Two novel copper and iron chelates have been studied by powder diffraction. The cell parameters for triclinic (space group P 1 (2)) C25H21CuN3SO4 are a=9.636(2) Å; b=11.014(1) Å; c=11.233(3) Å; α=83.55(2); β=82.45(6); γ=76.36(2); Z=2; Dx=1.456 g cm−3. The monoclinic cell parameters (space group P 21/c (14)) for C40H30Cl4Fe2N8S2 are a=11.464(8) Å; b=17.462(1) Å; c=20.550(6) Å; β=103.534(1); Z=2; Dx=1.356 g cm−3.

Keywords

X-ray powder diffractioncopper and iron complexesmetalloproteins
Type
New Diffraction Data
Information
Powder Diffraction , Volume 18 , Issue 2 , June 2003 , pp. 144 - 146
Copyright
Copyright © Cambridge University Press 2005

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References

Kraus, W. and Nolze, G. (1999). PowderCell for Windows, version 2.3 (Federal Institute for Materials Research and Testing, Berlin, Germany).Google Scholar
Nivorozhkin, A. L., Uraev, A. I., Bondarenko, G. I., Antsyshkina, A. S., Kurbatov, V. P., Garnovskii, A. D., Turta, C. I., and Brashoveanu, N. D. (1997). “Iron complexes with on N/S chromophore relevant to the active site of the hydrolytic metalloenzyme nitrile hydratase,” Chem. Commun. (Cambridge) CHCOFS 1997, 1711–1712. ccg, CHCOFS CrossRefGoogle Scholar
Vasilchenko, I. S., Antsyshkina, A. S., Burlov, A. S., Sadikov, G. G., Uraev, A. I., Nivorozhkin, A. L., Garnovskii, D. A., Sergienko, V. S., Kurbatov, V. P., Korshunov, O. Y., and Garnovskii, A. D. (1999). “Copper(II) Chelates with New Tridentate Ligand Systems, 2-(N-Tosylamino) benzylidene-and 2-Hydroxybenzylidene-Substituted 8-Aminoquinolines,” Russ. J. Inorg. Chem. RJICAQ 44 (8), 1278–1286. rji, RJICAQ Google Scholar