List of Publications

1979  1980 1982  1984  1985 1986  1987  1988  1989  1990  1991  1992  1993  1994  1995  1996  1997  1998  1999  2000  2001  2002  2003  2004  2005  2006  2007  2008  2009  2010  2011  2012  2013 

  1. L. Angeloni, G.Smulevich and M.P.Marzocchi
    Resonance Raman spectrum of crystal violet
    J. Raman Spectrosc. (1979) 8, 305-309.
  2. L.Angeloni, G. Smulevich and M.P. Marzocchi
    Resonance Raman spectra of conjugated chromophores. Evidence for electronic and vibrational couplings in crystal violet.
    J. Mol. Structure (1980) 61, 331-336.
  3. G. Smulevich, L. Angeloni and M.P. Marzocchi
    Raman excitation profiles of actinomycin D.
    Biochim. Biophys. Acta (1980) 610, 384-391.
  4. G. Smulevich, L. Angeloni and M.P. Marzocchi
    Raman excitation profiles of actinomycin-DNA complex.
    Spectrochim. Acta (1982) 38A, 219-221.
  5. G. Smulevich, L. Angeloni, S. Giovannardi and M.P. Marzocchi
    Resonance Raman and polarized light infrared spectra of 1.4-dihydroxyanthraquinone. Vibrational studies of the ground and excited states.
    Chem. Phys. (1982) 65, 313-322.
  6. L. Angeloni, G. Smulevich and M.P. Marzocchi
    Absorption, fluorescence and resonance Raman spectra of adriamycin and its complex with DNA.
    Spectrochim. Acta (1982) 38A, 213-217.
  7. L. Angeloni, G. Smulevich and M.P. Marzocchi
    Resonance Raman spectra of some ruthenium cluster compounds.
    J. Mol. Structure (1982) 79, 93-96.
  8. G. Smulevich, A. Amirav, U. Even and J. Jortner Electronic-vibrational excitations of a hydrogen-bonded molecule in supersonic expansions: 1.4-dihydroxyanthraquinone and its deuterated derivatives.
    Chem. Phys. (1982) 73, 1-18.
  9. L. Angeloni, M.P. Marzocchi and G. Smulevich
    Resonance Raman spectra and excitation profiles of some rifamycins.
    J. Raman Spectroscopy (1984) 15, 90-96.
  10. G. Smulevich and M.P. Marzocchi
    Energetics and intramolecular dynamics of 1.8-dihydroxyanthraquinone-d 0and -d2, as a model for anthracycline chromophores.
    Studia Biophysica (1984) 104, 105-110.
  11. G. Smulevich
    Resonance Raman and fluorescence spectra of 1.8-dihydroxyanthraquinone in n-alkanes at low temperature. Evidence for excited state proton transfer.
    J. Chem. Phys. (1985) 82, 14-21.
  12. G. Smulevich and M.P. Marzocchi
    Single crystal and polarized infrared spectra of two forms of 1.8- dihydroxyanthraquinone. Vibrational assignment and crystal structures.
    Chem. Phys. (1985) 94, 99-108.
  13. G. Smulevich and T. G. Spiro
    Nanosecond transient resonance Raman spectra of the FeII-CO and FeIII-NO photolysis products of horseradish peroxidase.
    Biochim. Biophys. Acta (1985) 830, 80-85.
  14. G. Smulevich and T. G. Spiro
    Surface Enhanced Raman Spectroscopy evidence that absorption on silver particles can denaturate heme proteins.
    J. Phys. Chem. (1985) 89, 5168-5173.
  15. G. Smulevich and M. P. Marzocchi
    Raman excitation profiles of 1.8-dihydroxyanthraquinone at 8K.
    Chem. Phys. (1986) 105, 159-171.
  16. G. Smulevich, R. Evangelista-Kirkup, A. English and T.G. Spiro
    Two CO binding modes for HRP-CO and CCP-CO: Raman evidence of CO pressure and pH dependence.
    J. Mol. Structure (1986) 141, 411-414.
  17. G. Smulevich and M. P. Marzocchi
    Raman excitation profiles, fluorescence spectra and excited state proton transfer of solid 1.8-dihydroxyanthraquinone at 8K.
    J. Mol. Structure (1986) 141, 429-432.
  18. R. Evangelista-Kirkup, G. Smulevich and T. G. Spiro
    Alternative CO binding modes for horseradish peroxidase studied by resonance Raman spectroscopy.
    Biochemistry (1986) 25, 4420-4425.
  19. G. Smulevich, R. Evangelista-Kirkup, A. English and T. G. Spiro
    Raman and infrared spectra of cytochrome c peroxidase CO adducts in an alternative conformational states.
    Biochemistry (1986) 25, 4426-4430.
  20. G. Smulevich, S. Dasgupta, A.M. English and T. G. Spiro
    Transient resonance Raman spectroscopy shows unrelaxed heme following CO photodissociation from cytocrome-c peroxidase.
    Biochim. Biophys. Acta (1986) 873, 88-91.
  21. F.F. Vincieri, S.A. Coran, M. Bambagiotti-Alberti, G. Smulevich and M.P. Marzocchi
    Second-derivative UV spectra of polyacetylene chromophores. Fingerprint of their geometrical isomers.
    Chem. Ber. (1986) 119, 2843-2847.
  22. G. Smulevich and A. Feis
    Surface Enhanced Resonance Raman Spectra of adriamycin, 11-deoxycarminomycin, their model chromophores and their complexes with DNA.
    J. Phys. Chem. (1986) 90, 6388-6392.
  23. G. Smulevich, G.G.T. Guarini and M.P. Marzocchi
    Infrared absorption and calorimetric evidence for the existence of two forms of 1.8-dihydroxyanthraquinone.
    Mol. Cryst. and Liq. Cryst. (1987) 142, 173-179.
  24. G. Smulevich, M.P. Marzocchi, F.F. Vincieri, S.A. Coran and M. Bambagiotti Alberti
    Vibronic absorption spectra of naturally occurring conjugated poly-ene-ynes. Evidence for localized excitation.
    J. Chem. Soc. Perkin Trans. II (1987), 1431-1437.
  25. G. Smulevich and P. Foggi
    Fluorescence excitation and emission spectra of 1.5-dihydroxyanthraquinone-d2 in n.hexane at 10 K.
    J. Chem. Phys. (1987) 87, 5657-5663.
  26. G. Smulevich, P. Foggi, A. Feis and M.P. Marzocchi
    Fluorescence excitation and emission spectra of 1.8-dihydroxyanthraquinone-d0 and -d2in n.octane at 10 K.
    J. Chem. Phys. (1987) 87, 5664-5669.
  27. G. Smulevich, A. Feis, A.R. Mantini and M.P. Marzocchi
    Resonance Raman and SERRS spectra of antitumour anthracyclines and their complexes with DNA.
    Indian J. Pure Appl. Phys. (1988) 26, 207-211. Raman Effect Diamond Jubilee Issue
  28. G. Smulevich, A. Feis, G. Mazzi and F.F. Vincieri
    Inclusion complex formation of 1.8-dihydroxyanthraquinone with cyclodextrins in aqueous solution and in solid state.
    J. Pharm. Sci. (1988) 77, 523
  29. G. Smulevich, J.M. Mauro, L.A. Fishel, A.M. English, J. Kraut and T.G. Spiro
    Heme pocket interactions in cytochrome c peroxidase studied by site directed mutagenesis and resonance Raman spectroscopy.
    Biochemistry (1988) 27, 5477-5485.
  30. G. Smulevich, J.M. Mauro, L.A. Fishel, A.M. English, J. Kraut and T.G. Spiro
    Cytochrome c peroxidase mutant active site structures probed by resonance Raman and infrared signatures of the CO adducts.
    Biochemistry (1988) 27, 5486-5492.
  31. A.R. Mantini, M.P. Marzocchi and G. Smulevich
    Raman excitation profiles and second-derivative absorption spectra of b-carotene.
    J. Chem. Phys. (1989), 91, 85-91.
  32. G. Smulevich, A.R. Mantini, A.M. English and J.M. Mauro
    Effects of temperature and glycerol on the resonance Raman spectra of cytochrome c peroxidase and selected mutants.
    Biochemistry (1989) 28, 5058-5064.
  33. G. Smulevich, M.A. Miller, D. Gosztola and T.G. Spiro
    Photodissociable endogeneous ligand in alkaline-reduced cytochrome c peroxidase implicates distal protein tension.
    Biochemistry (1989) 28, 9905-9908.
  34. G. Smulevich, A.R. Mantini and M.P. Marzocchi
    Surface-enhanced resonance Raman scattering excitation profiles of anthracyclines adsorbed onto silver particles.
    J. Phys. Chem. (1990) 94, 2540-2545.
  35. G. Smulevich, Y. Wang, S.L. Edwards, T.L. Poulos, A.M. English and T.G. Spiro
    Resonance Raman spectroscopy of cytochrome c peroxidase single crystals on a variable temperature microscope stage.
    Biochemistry (1990) 29, 2586-2592.
  36. T.G. Spiro, G. Smulevich and C. Su
    Probing protein structure and dynamics with resonance Raman spectroscopy: cytochrome peroxidase and hemoglobin.
    Biochemistry (1990) 29, 4497-4508.
  37. G. Smulevich, Y. Wang, J.M. Mauro, J. Wang, L. A. Fishel, J. Kraut and T. G. Spiro
    Single crystal resonance Raman spectroscopy of site directed mutants of cytochrome c peroxidase.
    Biochemistry (1990) 29, 7174-7180.
  38. M. A. Miller, J.M. Mauro, G. Smulevich, M. Coletta, J. Kraut and T. G. Traylor
    CO dissociation in cytochrome c peroxidase: site-directed mutagenesis shows that distal Arg48 influences CO dissociation rates.
    Biochemistry (1990) 29, 9978-9988.
  39. G. Smulevich, A.M. English and T.G. Spiro
    Structure and dynamics of the active site of peroxidases as revealed by resonance Raman spectroscopy.
    In "Laser Applications in Life Sciences" Vol. 1403, Part Two: Lasers in Biophysics and Biomedicine (N.I. Koroteev and B.N. Toleutaev, Eds) SPIE-The International Society for Optical Engineering (1990) pp. 440-447.
  40. G. Smulevich, A.M. English, A.R. Mantini and M.P. Marzocchi
    Resonance Raman investigation of ferric iron in horseradish peroxidase and its aromatic donor complexes at room and low temperatures.
    Biochemistry (1991) 30, 772-779.
  41. G. Smulevich, M. A. Miller, J. Kraut and T. G. Spiro
    Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: resonance Raman evidence from Leu-52 and Gly181 mutants of cytochrome c peroxidase.
    Biochemistry (1991) 30, 9546-9558.
  42. M. Coletta, P. Ascenzi, G. Smulevich, A.R. Mantini, R. Del Gaudio, M. Piscopo and G. Geraci
    Alteration of the proximal bond energy in the unligated form of the homodimeric myoglobin from Nassa mutabilis: kinetic and spectroscopic evidence.
    FEBS (1992) 296, 184-186.
  43. P. Hildebrandt, A.M. English and G. Smulevich
    The cytochrome c and cytochrome c peroxidase complex as studied by resonance Raman spectroscopy.
    Biochemistry (1992) 31, 2384-2393.
  44. Y. Wang and G. Smulevich
    A variable-temperature stage for Raman microprobing spectroscopy.
    Applied Spectroscopy (1992) 46, 1309-1311.
  45. R. Purrello, M. Molina, Y. Wang, G. Smulevich, J. Fossella, J. R. Fresco, and T. G. Spiro
    Keto-iminol tautomerism of protonated CMP characterized by ultraviolet resonance Raman spectroscopy; implications of C+ iminol tautomer for base mispairing.
    J. Am. Chem. Soc. (1993) 115, 760-767.
  46. G. Smulevich and T.G. Spiro
    Single Crystal micro-Raman Spectroscopy
    In Methods in Enzymology, Vol.226: Metallobiochemistry, part C (J.F. Riordan and B.L. Vallee, Eds.) Academic Press, Orlando, U.S.A., (1993) pp.397-408.
  47. G. Smulevich
    Structure-function relationship of peroxidases via resonance Raman spectroscopy and site directed mutagenesis:cytochrome c peroxidase.
    In "Advances in Spectroscopy" Vol. 20 : Biomolecular Spectroscopy (R.J.H. Clark and R.E. Hester, Eds.) John Wiley, England, (1993) pp. 163-193.
  48. G. Smulevich, M. Paoli, J.F. Burke, R.C. Bray, S.S. Sanders, R.N.F. Thorneley, and A.T. Smith
    Characterization of recombinant horseradish peroxidase C and its site directed mutants by resonance Raman spectroscopy.
    In: Plant peroxidases: Biochemistry and Physiology (K.G. Welinder, S.K. Rasmussen, C. Penel, and H. Greppin, Eds.) University of Geneva (1993) pp.65-68.
  49. Feis, M.P. Marzocchi, M. Paoli, and G. Smulevich
    Spin-state and axial ligand bonding in the hydroxy complexes of metmyoglobin, methemoglobin, and horseradish peroxidase at room and low temperatures.
    Biochemistry (1994), 33, 4577-4583.
  50. G. Smulevich, M. Paoli, J.F. Burke, R.C. Bray, S.A. Sanders, R.N.F. Thorneley, and A.T. Smith
    Characterisation of recombinant horseradish peroxidases (HRP-C*) and three site-directed mutants, F41V, F41W, and R38K by resonance Raman spectroscopy.
    Biochemistry (1994), 33, 7398-7407.
  51. G. Smulevich, M.J. Bjerrum, H.B. Gray, and T.G. Spiro
    Resonance Raman spectra and active site structure of semisynthetic Met80Cys horse heart cytochrome c.
    Inorg. Chem. (1994), 33, 4629-4634.
  52. G. Smulevich, A. Feis, C. Focardi, J. Tams, and K.G. Welinder
    Resonance Raman study of the active site of Coprinus cinereus peroxidase.
    Biochemistry (1994), 33, 15425-15432.
  53. G. Smulevich
    The functional role of the key residues in the active site of peroxidases.
    Biochemical Society Transactions (1995), 23, 240-244.
  54. G. Smulevich, A.R. Mantini, M. Paoli, M. Coletta, and G. Geraci
    Resonance Raman characterization of the heme active site of the homodimeric myoglobin from Nassa mutabilis.
    Biochemistry (1995), 34, 7507-7516.
  55. G. Smulevich, F. Neri, O. Willemsen, K. Choudhury, M.P. Marzocchi, and T.L. Poulos
    Effect of the H175 Glu mutation on the heme pocket architecture of cytochrome c peroxidase.
    Biochemistry (1995), 34, 13485-13490.
  56. G. Smulevich, F. Neri, M.P. Marzocchi, and K.G. Welinder
    Versatility of heme coordination demonstrated in a fungal peroxidase. Absorption and resonance Raman studies of Coprinus cinereus peroxidase and the Asp245® Asn mutant at various pH values.
    Biochemistry (1996), 35, 10576-10585.
  57. G. Smulevich, S. Hu, K.R. Rodgers, D.B. Goodin, K.M. Smith, and T.G. Spiro
    Heme protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance Raman spectra of isotopically labeled hemes.
    Biospectroscopy (1996), 2, 365-376.
  58. G. Smulevich
    Le spettroscopie UV-Vis. e Raman risonante per lo studio della relazione struttura-funzione delle emoproteine con particolare riferimento alle perossidasi.
    Biochimica in Italia (1996), 4, 26-36.
  59. G. Smulevich
    A comparative analysis of the structures of various peroxidases as defined by resonance Raman and electronic absorption spectroscopies.
    In: Plant peroxidases: Biochemistry and Physiology (C. Obinger, U. Burner, R. Ebermann, C. Penel, H. Greppin, Eds.) University of Geneva (1996) pp.13-19.
  60. M. Nissum, P.W. Jensen, and G. Smulevich
    Electronic absorption and resonance Raman characterization of a peroxidase isolated from soybean seed hulls.
    In: Plant peroxidases: Biochemistry and Physiology (C. Obinger, U. Burner, R. Ebermann, C. Penel, H. Greppin, Eds.) University of Geneva (1996) pp.20-22.
  61. M. Coletta, G. Smulevich, M. Paoli, G. De Sanctis, A.R. Mantini, F. Ascoli, and K.G. Welinder
    Proton-linked modulation of functional and structural properties in plant peroxidases.
    In: Plant peroxidases: Biochemistry and Physiology (C. Obinger, U. Burner, R. Ebermann, C. Penel, H. Greppin, Eds.) University of Geneva (1996) pp.23-26.
  62. G. Smulevich, M. Paoli, G. De Sanctis, A.R. Mantini, F. Ascoli and M. Coletta
    Spectroscopic evidence for a conformational transition in horseradish peroxidase at very low pH.
    Biochemistry (1997), 36, 640-649.
  63. D. Howes, J. N. Rodriguez-Lopez, A.T. Smith, and G. Smulevich
    Mutation of distal residues of horseradish peroxidase: influence on substrate binding and cavity properties.
    Biochemistry (1997), 36, 1532-1543.
  64. M. Nissum, J.-J. Karlsson, J. Ulstrup, P.W. Jensen, and G. Smulevich
    Resonance Raman characterization of the di-heme protein cytochrome c4 from Pseudomonas stutzeri.
    J. Biol. Inorg. Chem. (1997), 2, 302-307.
  65. F. Neri, D. Kok, M.A Miller, and G. Smulevich
    Fluoride binding in hemoproteins: the importance of the distal cavity structure.
    Biochemistry (1997), 36, 8947-8953.
  66. M. Coletta, H. Costa, G. De Sanctis, F. Neri, G. Smulevich, D. L. Turner, and H. Santos
    PH-dependence of structural and functional properties of oxidized cytochrome c" from Methylophilus methylotrophus.
    J. Biol. Chem. (1997), 272, 24800-24804.
  67. G. Smulevich, M. Possenti, R. D'Avino, G. di Prisco, and M. Coletta
    Spectroscopic studies of the heme active site of hemoglobin from Chelidonichthys kumu.
    J. Raman Spectrosc. (1998), 29, 57-65.
  68. M. P. Marzocchi, A. R. Mantini, M. Casu, and G. Smulevich
    Intramolecular hydrogen-bonding and excited state proton transfer in hydroxyanthraquinones as studied by electronic spectra, resonance Raman scattering, and trasform analysis.
    J. Chem. Phys (1998), 108, 534-549.
  69. F. Neri, C. Indiani, K. G. Welinder, and G. Smulevich
    Mutation of the distal ariginine in Coprinus cinereus peroxidase: structural implications.
    Eur. J. Biochem. (1998), 251, 830-838.
  70. M. Coletta, P. Ascenzi, F. Polizio, G. Smulevich, R. del Gaudio, M. Piscopo, and G.Geraci
    Cooperative mechanism in the homodimeric myoglobin from Nassa mutabilis.
    Biochemistry (1998), 37, 2873-2878.
  71. M. Nissum, F. Neri, D. Mandelman, T. L. Poulos, and G. Smulevich
    Spectroscopic characterization of recombinant pea cytosolic ascorbate peroxidase: similarities and differences with cytochrome c peroxidase.
    Biochemistry (1998), 37, 8080-8087.
  72. Feis, J. N. Rodriguez-Lopez, R. N. F. Thorneley, and G. Smulevich
    The distal cavity structure of carbonyl horseradish peroxidase as probed by the resonance Raman spectra of His42Leu and Arg38Leu mutants.
    Biochemistry (1998), 37, 13575-13581.
  73. G. Smulevich
    Understanding the heme cavity structure of peroxidases: comparison of electronic absorption and resonance Raman spectra with crystallographic results.
    Biospectroscopy (1998) 4, S3-S17.
  74. Feis, B. D. Howes, C. Indiani, and G. Smulevich
    Resonance Raman and electronic absorption spectra of horseradish peroxidase isozyme A2: evidence for a quantum-mixed spin species.
    J. Raman Spectrosc. (1998) 29, 933-938.
  75. M. Nissum, A. Feis, and G. Smulevich
    Characterization of soybean seed coat peroxidase: resonance Raman evidence for a structure based classification of plant peroxidases.
    Biospectroscopy (1998) 4, 355-364.
  76. G. Smulevich, A. Feis, C. Indiani, M. Becucci, and M.P. Marzocchi
    Peroxidase-benzhydroxamic acid complexes: spectroscopic evidence that a Fe-H2O distance of 2.6 Ã… can correspond to hexa-coordinate high-spin heme.
    J. Biol. Inorg. Chem. (1999) 4, 39-47.
  77. B. D. Howes, C. B. Schiødt, K.G. Welinder, M.P. Marzocchi, J.-G. Ma, J. Zhang, J. A. Shelnutt, and G. Smulevich
    The quantum mixed-spin heme state of barley peroxidase: a paradigm for class III peroxidases.
    Biophysical J. (1999) 77, 478-492.
  78. F. Neri, C. Indiani, B. Baldi, J. Vind, K.G. Welinder, and G. Smulevich
    Role of the distal phenilalanine54 on the structure, stability and ligand binding of Coprinus cinereus peroxidases.
    Biochemistry (1999) 38, 7819-7827.
  79. B. D. Howes, A. Feis. C. Indiani, M.P. Marzocchi, and G. Smulevich
    Formation of two types of low-spin heme in horseradish peroxidase isoenzyme A2 at low temperature
    J. Biol Inorg. Chem. (2000) 5, 227-235.
  80. A.M. Priori, C. Indiani, G. De Sanctis, S. Marini, R. Santucci, G. Smulevich, and M. Coletta
    Anion- and pH-linked conformational transition in horseradish peroxidase
    J. Inorg. Biochemistry (2000) 79, 25-31.
  81. C. Indiani, A. Feis, B. D. Howes, M.P. Marzocchi, and G. Smulevich
    Effect of low temperature on soybean peroxidase: spectroscopic characterization of the quantum-mechanically admixed spin state.
    J. Inorg. Biochemistry (2000) 79, 269-274.
  82. C. Indiani, G. De Sanctis, F. Neri. H. Santos, G. Smulevich, and M. Coletta
    Effect of pH on axial ligand coordination of cytochrome c" from Methylophilus methylotrophus and horse heart cytochrome c.
    Biochemistry (2000) 39, 8234-8242.
  83. C. Indiani, A. Feis, B. D. Howes, M.P. Marzocchi and, G. Smulevich
    Benzohydroxamic acid-peroxidase complexes: spectroscopic characterization of a novel heme spin species.
    J. Am. Chem. Soc. (2000) 122, 7368-7376.
  84. B. D. Howes, N. C. Veitch, A. T. Smith, C. G. White, and G. Smulevich
    Haem-linked interactions in horseradish peroxidase revealed by spectroscopic analysis of the Phe221Met mutant.
    Biochem. J. (2001) 353, 181-191.
  85. A. Henriksen, O. Mirza, C. Indiani, K. Teilum, G. Smulevich, K. G. Welinder, and M. Gajhede
    Structure of soybean seed coat peroxidases: a plant peroxidase with unusual stability and haem-apoprotein interactions.
    Protein Science (2001) 10, 108-115.
  86. G. Smulevich, A.R. Mantini, A. Feis, and M.P. Marzocchi
    Resonanace Raman spectra and transform analysis of anthracyclines and their complexes with DNA.
    J. Raman. Spectrosc. (2001) 32, 565-578.
  87. F. Pacello P.R. Langford, J.S. Kroll, C. Indiani, G. Smulevich, A. Desideri, G. Rotilio, and A. Battistoni
    A novel heme protein, the Cu-Zn-Superoxide Dismutase from Haemophilus ducreyi.
    J. Biol. Chem. (2001) 276, 30326-30334.
  88. H.A. Heering, M.A.K. Jansen, R.N.F. Thorneley, and G. Smulevich
    Cationic Ascorbate Peroxidase isoenzyme II from tea; structural insights into the heme pocket of a uniques Hybrid peroxidase.
    Biochemistry (2001) 40, 10360-10370.
  89. K.L. Nielsen, C. Indiani, A. Henriksen, A. Feis, M. Becucci, M. Gajhede, G. Smulevich, and K. G. Welinder
    Differential Activity and Structure of Highly Similar Peroxidases.Spectroscopic, Crystallographic, and Enzymatic Analyses of Lignifying Arabidopsis thaliana Peroxidase A2, and Horseradish Peroxidase A2.
    Biochemistry (2001) 40, 11013-11021.
  90. B. D. Howes, H.A. Heering, T.O. Roberts, F. Schneider-Belhadadd, A. T. Smith, and G. Smulevich
    Mutation of residues critical for benzohydroxamic acid binding to horseradish peroxidase isoenzyme c.
    Biospectroscopy (2001) 62, 261-267.
  91. B.D.Howes, A. Feis, L. Raimondi, C.Indiani, and G. Smulevich
    The critical role of the proximal calcium ion in the structural properties of horseradish peroxidase
    J. Biol. Chem. (2001) 276, 40704-40711.
  92. G. Smulevich
    Electronic Absorption and Resonance Raman Spectroscopies of Heme Proteins.
    In: Spectroscopic Techniques in Biophysics, Vol. 4 (G.M. Giacometti and G. Giacometti, Eds.), IOS Press, The Netherlands (2001) pp.11-37.
  93. H. A. Heering, A.T. Smith and G. Smulevich
    Spectroscopic charaterization of mutations at the Phe41 position in the distal heme pocket of horseradish peroxidase C: structural and functional consequences.
    Biochem. J. (2002) 363, 571-579.
  94. H. A. Heering, Chiara Indiani, Günther Regelsberger, Christa Jakopitsch, Christian Obinger, and Giulietta Smulevich
    New insights into the heme cavity structure of catalase-peroxidase: a spectroscopic approach to the recombinant synechocystis enzyme and selected distal cavity mutants.
    Biochemistry. (2002) 41, 9237-9247.
  95. A. Feis, E. Santoni,F. Neri, C. Ciaccio, G. De Sanctis, M. Coletta and Giulietta Smulevich
    Fine tuning of the binding and dissociation of CO by the amino acids of the heme pocket of Coprinus cinereus peroxidase.
    Biochemistry. (2002) 41, 13264-13273.
  96. E. Santoni, C. Jakopitsch, H.A. Heering, C. Indiani, G. Regelsberger, C. Obinger, and G. Smulevich
    Spectroscopic and kinetic investigations of selected mutants of recombinant catalase-peroxidase from Synechocystis.
    In: Plant peroxidases: Biochemistry and Physiology (M. Acosta, J.N. Rodriguez-Lopez, and M.A. Pedreno, Eds.) University of Murcia (2002) pp 40-46.
  97. D. López-Molina, H.A. Heering, G. Smulevich, J. Tudela, R.N.F. Thorneley, F. García-Cánovas, J.N. Rodríguez-López
    98. Purification and characterization of a new cationic peroxidase from fresh flowers of Cynara scolymus L..
    J. Inorg. Biochem. (2003) 94, 243-254.
  98. F. Sinibaldi, M.C. Piro, B.D. Howes, Giulietta Smulevich, F. Ascoli, nd R. Santucci
    Rupture of the H-bond limking two omega-loops induces the molten globule state at neutral pH in cytochrome c.
    Biochemistry (2003) 42, 7604-7610.
  99. F. Sinibaldi, B.D. Howes, Giulietta Smulevich, C. Ciaccio, M. Coletta, and R. Santucci
    Anion concentration modulates conformation and stability of the molten globule of cytochrome c.
    J. Biol. Inorg. Chem (2003) 8, 663-670.
  100. M. P. Marzocchi and G. Smulevich
    Relationship between heme vinyl conformation and the protein matrix in peroxidases.
    J. Raman Spectroscopy (2003) 34, 725-736.
  101. C. Indiani, E, Santoni, M. Becucci, A. Boffi, K. Fukuyama, and G. Smulevich
    New Insight into the Peroxidase-Hydroxamic Acid Interaction Revealed by the Combination of Spectroscopic and Crystallographic Studies.
    Biochemistry (2003) 42, 14066-14074.
  102. L. Vitagliano. G. Bonomi, A. Riccio, G. di Prisco, G. Smulevich, and L. Mazzarella
    The oxidation process of Antarctic fish hemoglobins.
    Eur. J. Biochem  (2004) 271, 1651-1659.
  103. E. Santoni, C. Jakopitsch, C. Obinger, and G. Smulevich
    Comparison between catalase-peroxidase and cytochrome c peroxidase. The role of the hydrogen bond networks for protein stability and catalysis.
    Biochemistry (2004) 43, 5792-5802.
  104. E. Santoni, C. Jakopitsch, C. Obinger, and G. Smulevich
    Manipulating the covalent link between distal side tryptophan, tyrosine and methionine in catalase-peroxidase: an electronic absorption and resonance Raman study.
    Biopolymers  (2004) 74, 46-50.
  105. E. Santoni, S. Scatragli, F. Sinibaldi,L. Fiorucci, R. Santucci, and G.Smulevich
    A model for the misfolded bis-His intermediate of cytochrome c: the 1-56 N fragment.
    J. Inorg. Biochem. (2004) 98, 1067-1077.
  106. P. D'Angelo, D. Lucarelli, S. della Longa, M. Benfatto, J.L.Hazemann, A. Feis, G.Smulevich, A. Ilari, A. Bonamore, and A. Boffi
    Unusual heme iron-lipid acyl chain coordination in Escherichia coli flavohemoglobin.
    Biophys. J. (2004) 86, 3882-3892.
  107. L. Tofani, A. Feis, R. E. Snoke, D. Berti, P. Baglioni, and G. Smulevich
    Spectroscopic and interfacial properties of myoglobin/surfactant complexes.
    Biophys. J. (2004) 87, 1186-1195.
  108. C. Verde, B.D. Howes, M.C. De Rosa, L. Raiola, G. Smulevich, R. Williams, B. Giardina, E. Parisi, and G. di Prisco
    Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes.
    Protein Science (2004) 13, 2766-2781.
  109. M. Fedurco, J. Augustynski, C. Indiani, G. Smulevich, M. Antalik, M. Bano, E. Sedlak, M.C. Glascock, and J.H. Dawson
    The heme iron coordination of unfolded ferric and ferrous cytochrome c in neutral and acidic urea solutions. Spectroscopic and electrochemical studies.
    Biochim. Biophys. Acta - Proteins and Proteomics (2004) 1703, 31-41.
  110. P. Caroppi, F. Sinibaldi, E. Santoni, B.D. Howes, L. Fiorucci, T. Ferri, F. Ascoli, G. Smulevich, and R. Santucci
    The 40's omega-loop plays a critical role in the stability and the alkaline conformational transition of cytochrome c.
    J. Biol. Inorg. Chem. (2004) 9, 997-1006.
  111. F. Sinibaldi, G. Mei, F. Polticelli, M. C. Piro, B. D. Howes, G. Smulevich, R. Santucci, F. Ascoli, and L. Fiorucci
    ATP specifically drives refolding of non native conformations of cytochrome c.
    Protein Science (2005) 14, 1049-1058.
  112. M. Fedurco, J. Augustynski, C. Indiani, G. Smulevich, M. Antalik, M. Bano, E. Sedlak, M.C. Glascock, and J.H. Dawson
    Electrochemistry of unfolded cytochrome c in neutral and acidic urea solutions.
    J. Am. Chem. Soc. (2005) 127, 7639-7646.
  113. G. Smulevich, A. Feis, and B.D. Howes
    Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: what have we learned?
    Acc. Chem. Res. (2005) 38, 433-440.
  114. B. D. Howes, N. C. Brissett, W. A. Doyle, A. T. Smith, and G. Smulevich
    Spectroscopic and kinetic properties of the horseradish peroxidase mutant T171S: evidence for selective effects on the reduced state of the enzyme.
    FEBS Journal (2005) 272, 5514-5521.
  115. E. Droghetti and G. Smulevich
    Effect of sol-gel encapsulation on the unfolding of ferric horse heart cytochrome c.
    J. Biol. Inorg. Chem. 10,(2005), 696-703.
  116. C. Jakopitsch, E. Droghetti, F. Schmuckenschlager, P.G. Furtmuller, G. Smulevich and C. Obinger
    Role of the Main Access Channel of Catalase-Peroxidase in Catalysis.
    J. Biol. Chem. (2005), 280, 42411-42422.
  117. F. Sinibaldi, B.D. Howes, M.C. Piro, P. Caroppi,G. Mei, F. Ascoli, G. Smulevich, and R. Santucci
    Insights into the role of the histidines in the structure and stability of cytochrome c.
    J. Biol. Inorg. Chem. 11, (2006), 52-62.
  118. S.Brogioni, A. Feis, M. P.Marzocchi, M. Zederbauer, P. G. Furtmuller, C. Obinger, and G. Smulevich
    Resonance Raman assignment of myeloperoxidase and the selected mutants Asp94Val and Met243Thr. Effects of the heme distortion.
    J. Raman Spectroscopy (2006), 37, 263-276.
  119. G. Smulevich, C. Jakopitsch, E. Droghetti, and C. Obinger
    Probing the structure and bifunctionality of catalase-peroxidase (KatG).
    J.Inorg. Biochem.(2006), 100, 568-585.
  120. B. D. Howes, S. Scatragli, M. P. Marzocchi and G. Smulevich
    Surface-enhanced resonance Raman spectroscopy of rifamycins on silver nanoparticles: insight into their adsorption mechanisms.
    J.Raman Spectrosc. 37 (2006) 900-909
  121. E. Droghetti, S. Oellerich, P. Hildebrandt, and G. Smulevich
    Heme coordination states of unfolded ferrous cytochrome c.
    Biophys J. 91 (2006) 3022-3031.
  122. G. Smulevich, E. Droghetti, C. Focardi, C.Ciaccio, M. Coletta, and M. Nocentini
    A rapid spectroscopic method to detect the fraudolent treatment of tuna fish with carbon monoxide.
    Food Chemistry 101 (2007) 1071-1077.
  123. S. Bruno, S. Faggiano, F. Spyrakis, A. Mozzarelli, S. Abbruzzetti, E. Grandi, C. Viappiani, A. Feis, S. Mackowiak, G.Smulevich, E. Cacciatori, P. Dominici
    The reactivity with CO of AHb1 and AHb2 from Arabidopsis thaliana is controlled by the distal His E7 and internal hydrophobic cavities.
    J. Am. Chem. Soc., 129 (2007) 2880-2889.
  124. M. Zederbauer, P. G. Furtmuller, S. Brogioni,C. Jakopitsch, G. Smulevich, and C. Obinger
    Heme to protein linkages in human peroxidases:Impact on spectroscopic, redox and catalytic properties.
    Nat.Prod. Rep., 2007, 24, 571-584.
  125. A. Feis, L. Tofani, G. De Sanctis, M. Coletta, and G. Smulevich
    Multiphasic Kinetics of Myoglobin/SDS Complex Formation.
    Biophys. J.(2007) 92, 4078-4087.
  126. G. De Sanctis, G. Petrella, C. Ciaccio, A. Feis, G. Smulevich, and M. Coletta
    A comparative study on axial coordination and ligand binding in ferric mini myoglobin and horse heart myoglobin.
    Biophys. J.(2007) 93, 2135-2142.
  127. E. Droghetti, B. D. Howes, A. Feis, P. Dominici, M. Fittipaldi and G. Smulevich
    The quantum mechanically mixed-spin state in a non symbiotic plant hemoglobin: the effect of distal mutation on AHb1 from Arabidopsis thaliana.
    J. Inorg. Biochem. (2007), 101, 1812-1819
  128. B.D. Howes, L. Guerrini, S. Sanchez-Cortes, M.P.Marzocchi, J.V. Garcia-Ramos, and G. Smulevich
    The influence of pH and anions on the adsorption mechanism of rifampicin on silver colloids.
    J. Raman Spectroscopy (2007), 38, 859-864.
  129. A. Feis, A. Lapini, B. Catacchio, S. Brogioni, P. Foggi, E. Chiancone, A. Boffi, and G.Smulevich
    Unusually Strong H-Bonding to the Heme Ligand and Fast Geminate Recombination Dynamics of the Carbon Monoxide Complex of Bacillus subtilis Truncated Hemoglobin.
    Biochemistry(2008), 47, 902-910.
  130. G. Bonente, B. D. Howes, S. Caffarri, G.Smulevich, and R. Bassi
    Interactions between the photosystem II subunit PsbS and xanthophylls studied in vivo and in vitro.
    J. Biol. Chem. (2008), 283, 8434-8445.
  131. S. Brogioni, J. Stampler, P.G. Furtmuller, A. Feis, C. Obinger and G.Smulevich
    The role of the sulfonium linkage in the stabilization of the ferrous form of myeloperoxidase: a comparison with lactoperoxidase.
    Biochim. Biophys. Acta, Proteins and Proteomics (2008), 1784,843-849.
  132. L. Vitagliano, A. Vergara, G. Bonomi, A. Merlino, C. Verde, G. di Prisco, B. D. Howes, G. Smulevich, L. Mazzarella
    Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate R/T state.
    J. Am Chem Soc. (2008), 130, 10527-10535.
  133. F. Nicoletti, B.D.Howes,M. Fittipaldi, G. Fanali, M. Fasano, P. Ascenzi and G. Smulevich
    Ibuprofen Induces an Allosteric Conformational Transition in the Heme Complex of Human Serum Albumin with Significant Effects on Heme Ligation.
    J. Am Chem Soc. (2008), 130 11677-11688.
  134. E. Droghetti, S. Sumithran, M. Sono, M. Antali­k, M. Fedurco,J. H. Dawson, G. Smulevich
    Effects of urea and acetic acid on the heme axial ligation structure of ferric myoglobin at very acidic pH.
    Arch. Biochem. Biophys.(2009), 489, 68-75.
  135. A. Merlino,L. Vitagliano, B. D. Howes, C.Verde, G. di Prisco, G. Smulevich, F. Sica, A.Vergara
    Combined Crystallographic and Spectroscopic Analysis of Trematomus bernacchii Hemoglobin Highlights Analogies and Differences in the Peculiar Oxidation Pathway of Antarctic Fish Hemoglobins.
    Biopolymers (2009), 91, 1117-1125.
  136. P. Ascenzi, A. di Masi, M. Coletta, C. Ciaccio, G. Fanali, F.P. Nicoletti, G. Smulevich, and M. Fasano
    Ibuprofen impairs allosterically peroxynitrite isomerization by ferric human serum heme-albumin.
    J. Biol. Chem. (2009) 284,31006-31017.
  137. S. Faggiano, S. Abbruzzetti, F. Spyrakis, E. Grandi, C. Viappiani, S. Bruno, A. Mozzarelli, P. Cozzini, A. Astegno, P. Dominici, S. Brogioni, A. Feis, G. Smulevich, O. Carrillo, P. Schmidtke, B. C. Axel, and F. J. Luque
    Structural Plasticity and Functional Implications of Internal Cavities in Distal Mutants of Type 1 Non-Symbiotic Hemoglobin AHb1 from Arabidopsis thaliana.
    J. Phys. Chem. B (2009), 113, 16028-16038.
  138. F.P. Nicoletti, M. Thompson, B.D. Howes, S. Franzen, and G. Smulevich
    New Insights into the role of distal histidine flexibility in ligand stabilization of dehaloperoxidase-hemoglobin from Amphitrite ornata.
    Biochemistry (2010), 49, 1903-1912.
  139. F.P. Nicoletti, A. Comandini, A. Bonamore, L. Boechi, F. M. Boubeta, A. Feis, G. Smulevich, and A. Boffi
    Sulfide binding properties of truncated hemoglobins.
    Biochemistry (2010), 49, 2269-2278.
  140. F. Sinibaldi, B.D. Howes, M.C. Piro, F. Polticelli, C. Bombelli, T. Ferri, M. Coletta, G. Smulevich, and R. Santucci
    Extended cardiolipin anchorage to cytochrome c: a model for protein-mitochondrial membrane binding.
    J. Biol. Inorg. Chem. (2010), 15, 689-700.
  141. G. Smulevich, A. Feis, B.D. Howes, and A. Ivancich
    Structure-Function Relationships Among Heme Peroxidases: New Insights from Electronic Absorption, Resonance Raman, and Multifrequency Electron Paramagnetic Resonance Spectroscopies .
    in HANDBOOK OF PORPHYRIN SCIENCE With Applications to Chemistry, Physics, Materials Science, Engineering, Biology and Medicine, Vol 6: NMR and EPR Techniques. (K. M Kadish, K. M Smith, R. Guilard, Eds), World Scientific, 2010, 367-455
  142. Matthew K. Thompson, Michael F. Davis, Vesna de Serrano, Francesco P. Nicoletti, Barry D. Howes, Giulietta Smulevich, and Stefan Franzen
    Internal Binding of Halogenated Phenols in Dehaloperoxidase-Hemoglobin Inhibits Peroxidase Function.
    Biophysical Journal (2010), 99, 1586-1595.
  143. Gianluca Bartolucci, Enrica Droghetti, Claudia Focardi, Massimo Bambagiotti-Alberti, Mila Nocentini, and Giulietta Smulevich
    High throughput headspace GC-MS quantitative method to measure the amount of carbon monoxide treated tuna fish.
    J. Mass. Spectrom. 2010, 45, 1041-1045
  144. Antonello Merlino, Luigi Vitagliano, Anna Balsamo, Francesco Nicoletti, Barry Howes, Daniela Giordano, Daniela Coppola, Guido di Prisco, Cinzia Verde, Giulietta Smulevich, Lelio Mazzarella and Alessandro Vergara
    Crystallization, preliminary X-ray diffraction studies and Raman microscopy of the major hemoglobin from the sub-Antarctic fish Eleginops maclovinus in the carbomonoxy form.
    Acta Cryst. (2010) F66, 1536-1540.
  145. Enrica Droghetti, Francesco Paolo Nicoletti, Alessandra Bonamore, Leonardo Boechi, Pau Arroyo Manez, Dario A. Estrin, Alberto Boffi, Giulietta Smulevich, and Alessandro Feis
    Heme pocket structural properties of a bacterial truncated hemoglobin from Thermobifida fusca.
    Biochemistry 2010, 49, 10394-10402
  146. Barry D. Howes, Daniela Giordano, Leonardo Boechi, Roberta Russo, Simona Mucciacciaro, Chiara Ciaccio, Federica Sinibaldi, Maria Fittipaldi, Marcelo A. Martí, Darío A. Estrin, Guido di Prisco, Massimo Coletta, Cinzia Verde, and Giulietta Smulevich
    The Peculiar Heme Pocket of the 2/2 Hemoglobin of Cold Adapted Pseudoalteromonas haloplanktis TAC125..
    J. Biol. Inorg. Chem. (2011), 16, 299-311
  147. F.P. Nicoletti, M. Thompson, S. Franzen, and G. Smulevich
    Degradation of sulfide by Dehaloperoxidase-Hemoglobin from Amphitrite Ornata.
    J. Biol. Inorg. Chem. (2011), 16, 611-619
  148. F. Spyrakis, S. Faggiano, S. Abbruzzetti, P. Dominici, E. Cacciatori, A. Astegno, E. Droghetti, A. Feis, G. Smulevich, S.Bruno, A. Mozzarelli, P. Cozzini, C. Viappiani, C. Bidon, A. Chanal, F.J. Luque
    Histidine E7 Dynamics Modulates Ligand Exchange between Distal Pocket and Solvent in AHb1 from Arabidopsis Thaliana.
    J. Phys. Chem. B (2011), 115, 4128-4137
  149. Enrica Droghetti, Gian Luca Bartolucci, Claudia Focardi, Massimo Bambagiotti-Alberti, Mila Nocentini and Giulietta Smulevich
    Development and validation of a quantitative spectrophotometric method to detect the amount of carbon monoxide in treated tuna fish.
    Food Chemistry (2011), 128, 1143-1151.
  150. A. Merlino, B.D. Howes, G. di Prisco, C. Verde, G. Smulevich, L. Mazzarella, A. Vergara
    Occurrence and formation of endogenous histidine hexa-coordination in cold-adapted hemoglobins.
    IUBMB Life (2011)  63, 295-303.
  151. Daniela Giordano, Roberta Russo, Chiara Ciaccio, Barry D. Howes, Guido di Prisco, Michael C. Marden, Gaston Hui Bon Hoa, Giulietta Smulevich, Massimo Coletta, and Cinzia Verde
    Ligand- and proton-linked conformational changes of the ferrous 2/2 hemoglobin of Pseudoalteromonas haloplanktis TAC125.
    IUBMB Life (2011) 63, 566-573.
  152. C. Iannuzzi, S. Adinolfi, B. D. Howes, R. Garcia-Serres, M. Clemancey, J.-M. Latour, G. Smulevich, A. Pastore
    The role of CyaY in iron sulfur cluster assembly on the E. coli IscU scaffold protein.
    PLoS ONE (2011) 6 (7), e21992.
  153. E Droghetti, F. P. Nicoletti, A. Bonamore, N. Sciamanna, A. Boffi, A. Feis, and G. Smulevich
    The optical spectra of fluoride complexes can effectively probe H-bonding interactions in the distal cavity of heme proteins.
    J. Inorg. Biochem. (2011), 105, 1338-1343.
  154. F. Sinibaldi, E. Droghetti, F. Polticelli, M.C. Piro, D. Di Pierro, T. Ferri, G. Smulevich, R. Santucci
    The effects of ATP and sodium chloride on the cytochrome c -cardiolipin interaction: the contrasting behaviour of the horse heart and yeast proteins.
    J. Inorg. Biochem. (2011), 105, 1365-1372
  155. F.P. Nicoletti, E. Droghetti, L. Boechi, A. Bonamore, N. Sciamanna, D. Estrin, A. Feis, A. Boffi, G. Smulevich
    Fluoride as a probe for H-bonding interactions in the active site of heme proteins: the case of Thermobifida fusca hemoglobin.
    J. Am. Chem. Soc. (2011) 133, 20970-20980.
  156. Y.Cao, F.P. Nicoletti, G. De Sanctis, A. Bocedi, C. Ciaccio, F. Gullotta, G. Fanali, G.R. Tundo, A. Di Masi, M. Fasano, G. Smulevich, P. Ascenzi, and M. Coletta
    Evidence for pH-dependent multiple Conformers in FE(II)-heme-human serum albumin: spectroscopic and kinetic investigation of carbon monoxide binding.
    J. Biol. Inorg. Chem. (2012) 17, 133-147.
  157. M. Zamocky, E. Droghetti,M. Bellei,B Gasselhuber, M. Pabst,P.G. Furtmueller,G. Battistuzzi, G. Smulevich, C. Obinger
    Eukaryotic Extracellular Catalase-Peroxidase from Magnaporthe grisea. Biophysical/Chemical Characterization of the First Representative from a Novel Phytopathogenic KatG Group.
    Biochemie (2012) 94, 673-683.
  158. Barry D. Howes, Signe Helbo, Angela Fago, Giulietta Smulevich
    Insights into the anomalous heme pocket of rainbow trout myoglobin.
    J. Inorg. Biochem. (2012) 109, 1-8.
  159. D.Giordano, I. Boron, S. Abbruzzetti,W. Van Leuven, F. P. Nicoletti, F. Forti, S. Bruno, C.-H. C. Cheng, L. Moens, G. di Prisco, A. Nadra,D. Estrin, G. Smulevich, S. Dewilde, C. Viappiani, C. Verde
    Biophysical characterisation of neuroglobin of the icefish, a natural knockout for hemoglobin and myoglobin. Comparison with human neuroglobin
    PLoS ONE (2012), 7(12), e44508.
  160. Daniela Coppola, Stefania Abbruzzetti, Francesco Nicoletti, Antonello Merlino, Alessandra Gambacurta, Daniela Giordano, Barry D. Howes, Giampiero De Sanctis, Luigi Vitagliano, Stefano Bruno, Guido di Prisco, Lelio Mazzarella, Giulietta Smulevich, Massimo Coletta, Cristiano Viappiani, Alessandro Vergara, Cinzia Verde
    ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus.
    Molecular BioSystems (2012), 8, 3295-3304.
  161. Enrica Droghetti, Claudia Focardi, Mila Nocentini, Giulietta Smulevich
    A spectrophotometric method for the detection of carboxymyoglobin in beef drip.
    International Journal of Food Science & Technology (2013), 48, 429-436.
  162. Alessio Bocedi, Giampiero De Sanctis, Chiara Ciaccio, Grazia R.Tundo, Alessandra Di Masi, Gabriella Fanali, Francesco P. Nicoletti, Mauro Fasani, Giulietta Smulevich, Paolo Ascenzi, and Massimo Coletta
    Reciprocal allosteric modulation of carbon monoxide and warfarin binding to ferrous human serum heme-albumin.
    PLoS ONE (2013),  8(3),  e58842
  163. Enrica Droghetti, Francesco P. Nicoletti, Luca Guandalini, Gianluca Bartolucci and Giulietta Smulevich
    SERS detection of benzophenones on viologen functionalized Ag nanoparticles: application to breakfast cereals.
    J. Raman Spectroscopy (2013) in press
  164. Francesco P. Nicoletti, Enrica Droghetti, Barry D Howes, Juan P Bustamante, Alessandra Bonamore, Natascia Sciamanna, Darío A Estrin, Alessandro Feis, Alberto Boffi, and Giulietta Smulevich
    H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin.
    BBA - Proteins and Proteomics (2013) in press
  165. Luciana Capece, Leonardo Boechi, Laura L Perissinotti, Pau Arroyo-Manez, Damian E Bikiel, Giulietta Smulevich, Marcelo A Marti, Dario Estrín
    Small ligand-globin interactions: Reviewing lessons derived from computer simulation.
    BBA - Proteins and Proteomics (2013) in press