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Volume 68 
Part 12 
Page o3334  
December 2012  

Received 12 October 2012
Accepted 6 November 2012
Online 10 November 2012

Key indicators
Single-crystal X-ray study
T = 298 K
Mean [sigma](C-C) = 0.003 Å
R = 0.038
wR = 0.083
Data-to-parameter ratio = 13.6
Details
Open access

4-Methoxybenzamidinium nitrate

aChemistry Department, `Sapienza' University of Rome, P.le A. Moro, 5, I-00185 Rome, Italy
Correspondence e-mail: g.portalone@caspur.it

The title salt, C8H11N2O+·NO3-, was synthesized by a reaction between 4-methoxybenzamidine (4-amidinoanisole) and nitric acid. The asymmetric unit comprises a non-planar 4-methoxybenzamidinium cation and a nitrate anion. In the cation, the amidinium group has two similar C-N bond lengths [1.302 (3) and 1.313 (3) Å] and its plane forms a dihedral angle of 32.66 (5)° with the mean plane of the benzene ring. The nitrate-amidinium ion pair is not planar, as the dihedral angle between the planes defined by the CN2+ and NO3- units is 19.28 (6)°. The ionic components are associated in the crystal via N-H...O hydrogen bonds, resulting in a three-dimensional network.

Related literature

For the biological and pharmacological relevance of benzamidine, see: Powers & Harper (1999[Powers, J. C. & Harper, J. W. (1999). Proteinase Inhibitors, edited by A. J. Barrett & G. Salvesen, pp. 55-152. Amsterdam: Elsevier.]); Grzesiak et al. (2000[Grzesiak, A., Helland, R., Smalas, A. O., Krowarsch, D., Dadlez, M. & Otlewski, J. (2000). J. Mol. Biol. 301, 205-217.]). For structural analysis of proton-transfer adducts containing molecules of biological interest, see: Portalone (2011a[Portalone, G. (2011a). Chem. Centr. J. 5, 51.]); Portalone & Irrera (2011[Portalone, G. & Irrera, S. (2011). J. Mol. Struct. 991, 92-96.]). For the supramolecular association in proton-transfer adducts containing benzamidinium cations, see; Portalone (2010[Portalone, G. (2010). Acta Cryst. C66, o295-o301.], 2011b[Portalone, G. (2011b). Acta Cryst. E67, o3394-o3395.], 2012[Portalone, G. (2012). Acta Cryst. E68, o268-o269.]); Irrera & Portalone (2012[Irrera, S. & Portalone, G. (2012). Acta Cryst. E68, o3083.]); Irrera et al. (2012[Irrera, S., Ortaggi, G. & Portalone, G. (2012). Acta Cryst. C68, o447-o451.]). For hydrogen-bond motifs, see: Bernstein et al. (1995[Bernstein, J., Davis, R. E., Shimoni, L. & Chang, N.-L. (1995). Angew. Chem. Int. Ed. Engl. 34, 1555-1573.]).

[Scheme 1]

Experimental

Crystal data
  • C8H11N2O+·NO3-

  • Mr = 213.20

  • Orthorhombic, P 21 21 21

  • a = 7.1049 (7) Å

  • b = 10.3558 (8) Å

  • c = 13.4325 (9) Å

  • V = 988.32 (14) Å3

  • Z = 4

  • Mo K[alpha] radiation

  • [mu] = 0.12 mm-1

  • T = 298 K

  • 0.20 × 0.10 × 0.08 mm

Data collection
  • Oxford Diffraction Xcalibur S CCD diffractometer

  • Absorption correction: multi-scan (CrysAlis RED; Oxford Diffraction, 2006[Oxford Diffraction (2006). CrysAlis CCD and CrysAlis RED. Oxford Diffraction Ltd, Yarnton, England.]) Tmin = 0.977, Tmax = 0.991

  • 6206 measured reflections

  • 1253 independent reflections

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

  • Rint = 0.028

Refinement
  • R[F2 > 2[sigma](F2)] = 0.038

  • wR(F2) = 0.083

  • S = 0.98

  • 1253 reflections

  • 154 parameters

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

  • [Delta][rho]max = 0.12 e Å-3

  • [Delta][rho]min = -0.20 e Å-3

Table 1
Hydrogen-bond geometry (Å, °)

D-H...A D-H H...A D...A D-H...A
N1-H1A...O1 0.87 (2) 2.00 (2) 2.850 (3) 166 (2)
N1-H1B...O3i 0.91 (2) 2.10 (2) 3.008 (3) 170 (2)
N2-H2A...O2 0.87 (2) 2.05 (2) 2.920 (3) 175 (2)
N2-H2B...O1ii 0.84 (3) 2.43 (3) 3.030 (3) 129 (2)
N2-H2B...O3ii 0.84 (3) 2.33 (3) 3.174 (3) 177 (2)
Symmetry codes: (i) [-x+{\script{1\over 2}}, -y+1, z+{\script{1\over 2}}]; (ii) [-x+1, y-{\script{1\over 2}}, -z-{\script{1\over 2}}].

Data collection: CrysAlis CCD (Oxford Diffraction, 2006[Oxford Diffraction (2006). CrysAlis CCD and CrysAlis RED. Oxford Diffraction Ltd, Yarnton, England.]); cell refinement: CrysAlis CCD; data reduction: CrysAlis RED (Oxford Diffraction, 2006[Oxford Diffraction (2006). CrysAlis CCD and CrysAlis RED. Oxford Diffraction Ltd, Yarnton, England.]); program(s) used to solve structure: SIR97 (Altomare et al., 1999[Altomare, A., Burla, M. C., Camalli, M., Cascarano, G. L., Giacovazzo, C., Guagliardi, A., Moliterni, A. G. G., Polidori, G. & Spagna, R. (1999). J. Appl. Cryst. 32, 115-119.]); program(s) used to refine structure: SHELXL97 (Sheldrick, 2008[Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.]); molecular graphics: ORTEP-3 (Farrugia, 2012[Farrugia, L. J. (2012). J. Appl. Cryst. 45, 849-854.]); software used to prepare material for publication: WinGX (Farrugia, 2012[Farrugia, L. J. (2012). J. Appl. Cryst. 45, 849-854.]).


Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: FI2127 ).


References

Altomare, A., Burla, M. C., Camalli, M., Cascarano, G. L., Giacovazzo, C., Guagliardi, A., Moliterni, A. G. G., Polidori, G. & Spagna, R. (1999). J. Appl. Cryst. 32, 115-119.  [ISI] [CrossRef] [ChemPort] [details]
Bernstein, J., Davis, R. E., Shimoni, L. & Chang, N.-L. (1995). Angew. Chem. Int. Ed. Engl. 34, 1555-1573.  [CrossRef] [ChemPort] [ISI]
Farrugia, L. J. (2012). J. Appl. Cryst. 45, 849-854.  [ISI] [CrossRef] [ChemPort] [details]
Grzesiak, A., Helland, R., Smalas, A. O., Krowarsch, D., Dadlez, M. & Otlewski, J. (2000). J. Mol. Biol. 301, 205-217.  [ISI] [CrossRef] [PubMed] [ChemPort]
Irrera, S., Ortaggi, G. & Portalone, G. (2012). Acta Cryst. C68, o447-o451.  [CrossRef] [details]
Irrera, S. & Portalone, G. (2012). Acta Cryst. E68, o3083.  [CSD] [CrossRef] [details]
Oxford Diffraction (2006). CrysAlis CCD and CrysAlis RED. Oxford Diffraction Ltd, Yarnton, England.
Portalone, G. (2010). Acta Cryst. C66, o295-o301.  [CSD] [CrossRef] [details]
Portalone, G. (2011a). Chem. Centr. J. 5, 51.  [CSD] [CrossRef]
Portalone, G. (2011b). Acta Cryst. E67, o3394-o3395.  [CSD] [CrossRef] [details]
Portalone, G. (2012). Acta Cryst. E68, o268-o269.  [CSD] [CrossRef] [details]
Portalone, G. & Irrera, S. (2011). J. Mol. Struct. 991, 92-96.  [ISI] [CSD] [CrossRef] [ChemPort]
Powers, J. C. & Harper, J. W. (1999). Proteinase Inhibitors, edited by A. J. Barrett & G. Salvesen, pp. 55-152. Amsterdam: Elsevier.
Sheldrick, G. M. (2008). Acta Cryst. A64, 112-122.  [CrossRef] [details]


Acta Cryst (2012). E68, o3334  [ doi:10.1107/S1600536812045874 ]

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