[Journal logo]

Volume 69 
Part 11 
Page m597  
November 2013  

Received 28 September 2013
Accepted 6 October 2013
Online 12 October 2013

Key indicators
Single-crystal X-ray study
T = 295 K
Mean [sigma](C-C) = 0.003 Å
R = 0.019
wR = 0.048
Data-to-parameter ratio = 23.1
Details
Open access

catena-Poly[[bis­(nitrato-[kappa]2O,O')barium]-bis­([mu]-L-histidine-[kappa]3O,O':O]

aDepartment of Physics, Presidency College, Chennai 600 005, India, and bDepartment of Physics, CPCL Polytechnic College, Chennai 600 068, India
Correspondence e-mail: chakkaravarthi_2005@yahoo.com, professormohan@yahoo.co.in

In the polymeric title compound, [Ba(NO3)2(C6H9N3O2)2]n, the BaII atom is located on a crystallographic twofold axis and is coordinated by ten O atoms. Six are derived from two zwitterionic L-histidine mol­ecules that simultaneously chelate one BaII atom and bridge to another. The remaining four O atoms are derived from two chelating nitrates. The mol­ecules assemble to form a chain along [010]. In the crystal, chains are linked via N-H...O and N-H...N hydrogen bonds, generating a three-dimensional network.

Related literature

For the biological activity of histidine, see: Eichler et al. (2005[Eichler, J. F., Cramer, J. C., Kirk, K. L. & Bann, J. G. (2005). ChemBioChem, 6, 2170-2173.]); Wimalasena et al. (2007[Wimalasena, D. S., Cramer, J. C., Janowiak, B. E., Juris, S. J., Melnyk, R. A., Anderson, D. E., Kirk, K. L., Collier, R. J. & Bann, J. G. (2007). Biochemistry, 46, 14928-14936.]). For standard bond lengths, see: Allen et al. (1987[Allen, F. H., Kennard, O., Watson, D. G., Brammer, L., Orpen, A. G. & Taylor, R. (1987). J. Chem. Soc. Perkin Trans. 2, pp. S1-19.]). For related structures, see: Andra et al. (2010[Andra, K. K., Bullinger, J. C., Bann, J. G. & Eichhorn, D. M. (2010). Acta Cryst. E66, o2713.]); Gokul Raj et al. (2006[Gokul Raj, S., Ramesh Kumar, G., Raghavalu, T., Mohan, R. & Jayavel, R. (2006). Acta Cryst. E62, o1178-o1180.]).

[Scheme 1]

Experimental

Crystal data
  • [Ba(NO3)2(C6H9N3O2)2]

  • Mr = 571.68

  • Monoclinic, C 2

  • a = 24.9063 (8) Å

  • b = 4.7226 (1) Å

  • c = 8.3180 (3) Å

  • [beta] = 105.432 (1)°

  • V = 943.11 (5) Å3

  • Z = 2

  • Mo K[alpha] radiation

  • [mu] = 2.18 mm-1

  • T = 295 K

  • 0.18 × 0.14 × 0.12 mm

Data collection
  • Bruker Kappa APEXII diffractometer

  • Absorption correction: multi-scan (SADABS; Sheldrick, 1996[Sheldrick, G. M. (1996). SADABS, University of Göttingen, Germany.]) Tmin = 0.695, Tmax = 0.780

  • 6598 measured reflections

  • 3281 independent reflections

  • 3281 reflections with I > 2[sigma](I)

  • Rint = 0.030

Refinement
  • R[F2 > 2[sigma](F2)] = 0.019

  • wR(F2) = 0.048

  • S = 1.15

  • 3281 reflections

  • 142 parameters

  • 2 restraints

  • H-atom parameters constrained

  • [Delta][rho]max = 1.40 e Å-3

  • [Delta][rho]min = -1.32 e Å-3

  • Absolute structure: Flack (1983[Flack, H. D. (1983). Acta Cryst. A39, 876-881.]), 1164 Friedel pairs

  • Absolute structure parameter: 0.004 (13)

Table 1
Hydrogen-bond geometry (Å, °)

D-H...A D-H H...A D...A D-H...A
N1-H1...O4i 0.86 2.29 2.854 (3) 123
N1-H1...O5ii 0.86 2.37 3.121 (3) 146
N3-H3B...O1iii 0.89 2.19 3.029 (2) 158
N3-H3C...O3iv 0.89 2.05 2.867 (3) 153
N3-H3A...N2v 0.89 1.94 2.827 (3) 174
Symmetry codes: (i) [-x+{\script{1\over 2}}, y+{\script{3\over 2}}, -z+1]; (ii) [-x+{\script{1\over 2}}, y+{\script{1\over 2}}, -z+1]; (iii) -x+1, y, -z+1; (iv) x, y+1, z-1; (v) x, y-1, z.

Data collection: APEX2 (Bruker, 2004[Bruker (2004). APEX2 and SAINT. Bruker AXS Inc., Madison, Wisconsin, USA.]); cell refinement: SAINT (Bruker, 2004[Bruker (2004). APEX2 and SAINT. Bruker AXS Inc., Madison, Wisconsin, USA.]); data reduction: SAINT; program(s) used to solve structure: SHELXS97 (Sheldrick, 2008[Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.]); program(s) used to refine structure: SHELXL97 (Sheldrick, 2008[Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.]); molecular graphics: PLATON (Spek, 2009[Spek, A. L. (2009). Acta Cryst. D65, 148-155.]); software used to prepare material for publication: SHELXL97.


Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: TK5259 ).


Acknowledgements

The authors wish to acknowledge the SAIF, IIT Madras, for the data collection.

References

Allen, F. H., Kennard, O., Watson, D. G., Brammer, L., Orpen, A. G. & Taylor, R. (1987). J. Chem. Soc. Perkin Trans. 2, pp. S1-19.
Andra, K. K., Bullinger, J. C., Bann, J. G. & Eichhorn, D. M. (2010). Acta Cryst. E66, o2713.  [CSD] [CrossRef] [IUCr Journals]
Bruker (2004). APEX2 and SAINT. Bruker AXS Inc., Madison, Wisconsin, USA.
Eichler, J. F., Cramer, J. C., Kirk, K. L. & Bann, J. G. (2005). ChemBioChem, 6, 2170-2173.  [Web of Science] [CrossRef] [PubMed] [ChemPort]
Flack, H. D. (1983). Acta Cryst. A39, 876-881.  [CrossRef] [IUCr Journals]
Gokul Raj, S., Ramesh Kumar, G., Raghavalu, T., Mohan, R. & Jayavel, R. (2006). Acta Cryst. E62, o1178-o1180.  [CSD] [CrossRef] [IUCr Journals]
Sheldrick, G. M. (1996). SADABS, University of Göttingen, Germany.
Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.  [CrossRef] [ChemPort] [IUCr Journals]
Spek, A. L. (2009). Acta Cryst. D65, 148-155.  [Web of Science] [CrossRef] [ChemPort] [IUCr Journals]
Wimalasena, D. S., Cramer, J. C., Janowiak, B. E., Juris, S. J., Melnyk, R. A., Anderson, D. E., Kirk, K. L., Collier, R. J. & Bann, J. G. (2007). Biochemistry, 46, 14928-14936.  [Web of Science] [CrossRef] [PubMed] [ChemPort]


Acta Cryst (2013). E69, m597  [ doi:10.1107/S1600536813027402 ]

This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.