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Volume 68 
Part 11 
Page o3244  
November 2012  

Received 23 October 2012
Accepted 25 October 2012
Online 31 October 2012

Key indicators
Single-crystal X-ray study
T = 298 K
Mean [sigma](C-C) = 0.003 Å
R = 0.039
wR = 0.114
Data-to-parameter ratio = 15.7
Details
Open access

4-Methoxybenzamidinium hydrogen sulfate

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+·HSO4-, has been synthesized by the reaction between 4-methoxybenzamidine and sulfuric acid. The asymmetric unit comprises a nonplanar 4-methoxybenzamidinium cation and one hydrogen sulfate anion. In the cation, the amidinium group has two identical C-N bonds [1.306 (2) and 1.308 (2) Å], and its plane forms a dihedral angle of 6.49 (8)° with the mean plane of the benzene ring. The ionic components are associated in the crystal via N-H+...O-, resulting in chains running approximately along the b-axis direction whicg are interconnected by O-H...O- hydrogen bonds.

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. Cent. 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+·HSO4-

  • Mr = 248.26

  • Monoclinic, P 21 /c

  • a = 14.2608 (14) Å

  • b = 10.1844 (9) Å

  • c = 7.5723 (9) Å

  • [beta] = 94.206 (10)°

  • V = 1096.83 (19) Å3

  • Z = 4

  • Mo K[alpha] radiation

  • [mu] = 0.30 mm-1

  • T = 298 K

  • 0.31 × 0.25 × 0.15 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, Oxfordshire, England.]) Tmin = 0.912, Tmax = 0.956

  • 16529 measured reflections

  • 2626 independent reflections

  • 2133 reflections with I > 2[sigma](I)

  • Rint = 0.036

Refinement
  • R[F2 > 2[sigma](F2)] = 0.039

  • wR(F2) = 0.114

  • S = 1.04

  • 2626 reflections

  • 167 parameters

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

  • [Delta][rho]max = 0.26 e Å-3

  • [Delta][rho]min = -0.34 e Å-3

Table 1
Hydrogen-bond geometry (Å, °)

D-H...A D-H H...A D...A D-H...A
O3-H3A...O2i 0.78 (3) 1.79 (3) 2.562 (2) 172 (3)
N1-H1A...O4 0.86 (2) 2.10 (2) 2.938 (2) 163 (2)
N1-H1B...O5ii 0.84 (2) 2.10 (2) 2.884 (2) 154 (2)
N2-H2A...O5 0.84 (2) 2.07 (3) 2.907 (2) 177 (2)
N2-H2B...O4iii 0.86 (3) 2.22 (3) 2.965 (2) 145 (3)
Symmetry codes: (i) [x, -y+{\script{1\over 2}}, z-{\script{1\over 2}}]; (ii) [-x, y+{\script{1\over 2}}, -z+{\script{3\over 2}}]; (iii) [-x, y-{\script{1\over 2}}, -z+{\script{3\over 2}}].

Data collection: CrysAlis CCD (Oxford Diffraction, 2006[Oxford Diffraction (2006). CrysAlis CCD and CrysAlis RED. Oxford Diffraction Ltd, Yarnton, Oxfordshire, England.]); cell refinement: CrysAlis RED (Oxford Diffraction, 2006[Oxford Diffraction (2006). CrysAlis CCD and CrysAlis RED. Oxford Diffraction Ltd, Yarnton, Oxfordshire, England.]); data reduction: CrysAlis RED; 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, 1997[Farrugia, L. J. (1997). J. Appl. Cryst. 30, 565.]); software used to prepare material for publication: WinGX (Farrugia, 1999[Farrugia, L. J. (1999). J. Appl. Cryst. 32, 837-838.]).


Supplementary data and figures for this paper are available from the IUCr electronic archives (Reference: RZ5020 ).


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. (1997). J. Appl. Cryst. 30, 565.  [CrossRef] [details]
Farrugia, L. J. (1999). J. Appl. Cryst. 32, 837-838.  [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.  [CrossRef] [details]
Oxford Diffraction (2006). CrysAlis CCD and CrysAlis RED. Oxford Diffraction Ltd, Yarnton, Oxfordshire, England.
Portalone, G. (2010). Acta Cryst. C66, o295-o301.  [CSD] [CrossRef] [details]
Portalone, G. (2011a). Chem. Cent. J. 5, 51.  [CrossRef] [PubMed]
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, o3244  [ doi:10.1107/S1600536812044327 ]

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