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Volume 66 
Part 11 
Page m1450  
November 2010  

Received 5 September 2010
Accepted 16 October 2010
Online 23 October 2010

Key indicators
Single-crystal X-ray study
T = 150 K
Mean [sigma](C-C) = 0.005 Å
R = 0.057
wR = 0.153
Data-to-parameter ratio = 9.1
Details
Open access

Di-[mu]-hydroxido-bis[aqua(pyridine-2,6-dicarboxylato)iron(III)] monohydrate

aDepartment of Chemistry, School of Sciences, Ferdowsi University of Mashhad, Mashhad, Iran, and bDepartment of Chemistry, Purdue University, W. Lafayette, IN 47907, USA
Correspondence e-mail: heshtiagh@um.ac.ir, pfanwick@purdue.edu

In the dinuclear title complex, [Fe2(OH)2(C7H3NO4)2(H2O)2]·H2O, the two Fe atoms are separated by 3.063 (1) Å. Intermolecular O-H...O hydrogen bonds form an extensive three-dimensional hydrogen-bonding network, which consolidates the crystal packing.

Related literature

The crystal structure of the anhydrous form of the title dinuclear complex has been reported by Thich et al. (1976[Thich, J. A., Ou, C. C., Powers, D., Vasiliou, B., Mastropaolo, D., Potenza, J. A. & Schugar, H. J. (1976). J. Am. Chem. Soc. 98, 1425-1433. ]). For related structures, see: Aghabozorg et al. (2008[Aghabozorg, H., Manteghi, F. & Sheshmani, S. (2008). J. Iran. Chem. Soc. 5, 184-227.]); Eshtiagh-Hosseini et al. (2010[Eshtiagh-Hosseini, H., Yousefi, Z., Safiee, M. & Mirzaei, M. (2010). J. Coord. Chem. 63, 3187-3197.]).

[Scheme 1]

Experimental

Crystal data
  • [Fe2(OH)2(C7H3NO4)2(H2O2)2]·H2O

  • Mr = 529.97

  • Monoclinic, P 21 /c

  • a = 11.4786 (11) Å

  • b = 21.7080 (16) Å

  • c = 7.3291 (6) Å

  • [beta] = 90.099 (7)°

  • V = 1826.2 (3) Å3

  • Z = 4

  • Cu K[alpha] radiation

  • [mu] = 13.53 mm-1

  • T = 150 K

  • 0.20 × 0.20 × 0.14 mm

Data collection
  • Rigaku Rapid II diffractometer

  • Absorption correction: multi-scan (SCALEPACK; Otwinowski & Minor, 1997[Otwinowski, Z. & Minor, W. (1997). Methods in Enzymology, Vol. 276, Macromolecular Crystallography, Part A, edited by C. W. Carter Jr & R. M. Sweet, pp. 307-326. New York: Academic Press.]) Tmin = 0.120, Tmax = 0.150

  • 14275 measured reflections

  • 2831 independent reflections

  • 2695 reflections with I > 2[sigma](I)

  • Rint = 0.048

Refinement
  • R[F2 > 2[sigma](F2)] = 0.057

  • wR(F2) = 0.153

  • S = 1.07

  • 2831 reflections

  • 311 parameters

  • H atoms treated by a mixture of independent and constrained refinement

  • [Delta][rho]max = 0.97 e Å-3

  • [Delta][rho]min = -0.76 e Å-3

Table 1
Hydrogen-bond geometry (Å, °)

D-H...A D-H H...A D...A D-H...A
O1-H1...O1W 0.70 (5) 2.34 (5) 2.966 (3) 151 (5)
O2-H2...O1Wi 0.72 (5) 2.28 (5) 2.936 (3) 151 (5)
O15-H151...O12ii 0.83 (5) 1.78 (5) 2.611 (5) 173 (5)
O15-H152...O14iii 0.80 (4) 1.79 (4) 2.577 (4) 171 (5)
O25-H251...O24iv 0.78 (4) 1.80 (4) 2.577 (4) 176 (5)
O25-H252...O22v 0.71 (5) 1.87 (5) 2.576 (5) 173 (6)
O1W-H1W1...O23iii 0.87 (4) 2.10 (4) 2.962 (4) 176 (4)
O1W-H1W2...O13iii 0.87 (5) 2.22 (4) 3.072 (4) 169 (4)
Symmetry codes: (i) x, y, z+1; (ii) -x+1, -y, -z+1; (iii) [x, -y+{\script{1\over 2}}, z-{\script{1\over 2}}]; (iv) [x, -y+{\script{1\over 2}}, z+{\script{1\over 2}}]; (v) -x+2, -y, -z+2.

Data collection: CrystalClear (Rigaku, 2001[Rigaku (2001). CrystalClear. Rigaku Corporation, Tokyo, Japan.]); cell refinement: DENZO/SCALEPACK (Otwinowski & Minor, 1997[Otwinowski, Z. & Minor, W. (1997). Methods in Enzymology, Vol. 276, Macromolecular Crystallography, Part A, edited by C. W. Carter Jr & R. M. Sweet, pp. 307-326. New York: Academic Press.]); data reduction: DENZO/SCALEPACK; method used to solve structure: charge flipping (Oszlányi & Süto, 2004[Oszlányi, G. & Süto, A. (2004). Acta Cryst. A60, 134-141.]) implemented in PLATON (Spek, 2009[Spek, A. L. (2009). Acta Cryst. D65, 148-155.]); program(s) used to refine structure: SHELXL97 (Sheldrick, 2008[Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.]); molecular graphics: ORTEPII (Johnson, 1976[Johnson, C. K. (1976). ORTEP. Report ORNL-5138. Oak Ridge National Laboratory, Tennessee, USA.]) and PLATON; software used to prepare material for publication: SHELXL97.


Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: CV2763 ).


Acknowledgements

Financial support as well as provision of X-ray facilities from the Ferdowsi University of Mashhad and Purdue University, W. Lafayette, are gratefully acknowledged by the authors.

References

Aghabozorg, H., Manteghi, F. & Sheshmani, S. (2008). J. Iran. Chem. Soc. 5, 184-227.  [ChemPort]
Eshtiagh-Hosseini, H., Yousefi, Z., Safiee, M. & Mirzaei, M. (2010). J. Coord. Chem. 63, 3187-3197.  [ISI] [CrossRef] [ChemPort]
Johnson, C. K. (1976). ORTEP. Report ORNL-5138. Oak Ridge National Laboratory, Tennessee, USA.
Oszlányi, G. & Süto, A. (2004). Acta Cryst. A60, 134-141.  [CrossRef] [details]
Otwinowski, Z. & Minor, W. (1997). Methods in Enzymology, Vol. 276, Macromolecular Crystallography, Part A, edited by C. W. Carter Jr & R. M. Sweet, pp. 307-326. New York: Academic Press.
Rigaku (2001). CrystalClear. Rigaku Corporation, Tokyo, Japan.
Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.  [CrossRef] [details]
Spek, A. L. (2009). Acta Cryst. D65, 148-155.  [ISI] [CrossRef] [details]
Thich, J. A., Ou, C. C., Powers, D., Vasiliou, B., Mastropaolo, D., Potenza, J. A. & Schugar, H. J. (1976). J. Am. Chem. Soc. 98, 1425-1433.   [CrossRef] [ChemPort] [ISI]


Acta Cryst (2010). E66, m1450  [ doi:10.1107/S1600536810041966 ]

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