R. G. Shulman, Spectroscopic Contributions to the Understanding of Hemoglobin Function: Implications for Structural Biology, IUBMB Life (International Union of Biochemistry and Molecular Biology: Life), vol.51, issue.6, pp.351-357, 2001.
DOI : 10.1080/152165401753366104

T. G. Spiro and I. H. Wasbotten, CO as a vibrational probe of heme protein active sites, Journal of Inorganic Biochemistry, vol.99, issue.1, pp.34-44, 2005.
DOI : 10.1016/j.jinorgbio.2004.09.026

S. Abbruzzetti, S. Bruno, S. Faggiano, E. Grandi, A. Mozzarelli et al., Time-resolved methods in Biophysics. 2. Monitoring haem proteins at work with nanosecond laser flash photolysis, Photochemical & Photobiological Sciences, vol.102, issue.12, pp.1109-1120, 2006.
DOI : 10.1039/b610236k

A. V. Soldatova, A. M. Ibrahim, J. S. Olson, R. S. Czernuszewicz, and T. G. Spiro, New Light on NO Bonding in Fe(III) Heme Proteins from Resonance Raman Spectroscopy and DFT Modeling, Journal of the American Chemical Society, vol.132, issue.13, pp.4614-4625, 2010.
DOI : 10.1021/ja906233m

J. Al-mustafa and J. R. Kincaid, Resonance Raman Study of Cyanide-Ligated Horseradish Peroxidase.Detection of Two Binding Geometries and Direct Evidence for the "Push-Pull" Effect, Biochemistry, vol.33, issue.8, pp.2191-2197, 1994.
DOI : 10.1021/bi00174a028

T. Egawa and S. R. Yeh, Structural and functional properties of hemoglobins from unicellular organisms as revealed by resonance Raman spectroscopy, Journal of Inorganic Biochemistry, vol.99, issue.1, pp.72-96, 2005.
DOI : 10.1016/j.jinorgbio.2004.10.017

M. Tsubaki, R. B. Srivastava, and N. T. Yu, Temperature dependence of resonance Raman spectra of metmyoglobin and methemoglobin azide. Detection of resonance-enhanced bound azide vibrations and iron-azide stretch, Biochemistry, vol.20, issue.4, pp.946-952, 1981.
DOI : 10.1021/bi00507a047

F. P. Nicoletti, A. Comandini, A. Bonamore, L. Boechi, F. M. Boubeta et al., Sulfide Binding Properties of Truncated Hemoglobins, Biochemistry, vol.49, issue.10, pp.2269-2278, 2010.
DOI : 10.1021/bi901671d

F. P. Nicoletti, M. K. Thompson, S. Franzen, and G. Smulevich, Degradation of sulfide by dehaloperoxidase-hemoglobin from Amphitrite ornata, JBIC Journal of Biological Inorganic Chemistry, vol.19, issue.42, pp.611-619, 2011.
DOI : 10.1007/s00775-011-0762-2

F. Neri, C. Indiani, K. G. Welinder, and G. Smulevich, Mutation of the distal arginine in Coprinus cinereus peroxidase . Structural implications, European Journal of Biochemistry, vol.251, issue.3, pp.830-838, 1998.
DOI : 10.1046/j.1432-1327.1998.2510830.x

. Fig, Resonance Raman spectra in the low-frequency region of fluoride adducts of TftrHb , HRPC and hhMb at pH 7, and hhMb at pH 5.2 and pD 5.1 (0.1 M MES) taken with excitation in resonance with the CT2 band

T. G. Spiro, 27 mW laser power at the sample, average of five spectra with 1800 s integration time (Tf-trHb-F), average of six spectra with 600 s integration time (HRPC-F), average of seventeen spectra with 300 s integration time (hhMb-F at pH and pD 7.0), average of fifteen spectra with 300 s integration time (hhMb-F at pH 5.2 and pD 5.1). A baseline has been subtracted from the spectra of Tf-trHb-F and Mb-F, Experimental conditions, 1 cm ? 1 spectral resolution Iron Porphirins, Part II, pp.89-152, 1983.

A. Desbois, M. Lutz, and R. Banerjee, Low-frequency vibrations in resonance Raman spectra of horse heart myoglobin. Iron-ligand and iron-nitrogen vibrational modes, Biochemistry, vol.18, issue.8, pp.1510-1518, 1979.
DOI : 10.1021/bi00575a019

J. B. Wittenberg, M. Bolognesi, B. A. Wittenberg, and M. Guertin, Truncated Hemoglobins: A New Family of Hemoglobins Widely Distributed in Bacteria, Unicellular Eukaryotes, and Plants, Journal of Biological Chemistry, vol.277, issue.2, pp.871-874, 2002.
DOI : 10.1074/jbc.R100058200

G. Wu, L. M. Wainwright, and R. K. Poole, Microbial globins, Adv. Microb. Physiol, vol.47, pp.255-310, 2003.
DOI : 10.1016/S0065-2911(03)47005-7

A. Bonamore, A. Ilari, L. Giangiacomo, A. Bellelli, V. Morea et al., A novel thermostable hemoglobin from the actinobacterium Thermobifida fusca, FEBS Journal, vol.84, issue.16, pp.4189-4201, 2005.
DOI : 10.1111/j.1742-4658.2005.04831.x

B. A. Springer, S. G. Sligar, J. O. Olson, and J. G. Phillips, Mechanisms of Ligand Recognition in Myoglobin, Chemical Reviews, vol.94, issue.3, pp.699-714, 1994.
DOI : 10.1021/cr00027a007

G. Smulevich, A. Feis, and B. D. Howes, Fifteen Years of Raman Spectroscopy of Engineered Heme Containing Peroxidases:?? What Have We Learned?, Accounts of Chemical Research, vol.38, issue.5, pp.433-440, 2005.
DOI : 10.1021/ar020112q

S. A. Asher, M. L. Adams, and T. M. Schuster, Resonance Raman and absorption spectroscopic detection of distal histidine-fluoride interactions in human methemoglobin fluoride and sperm whale metmyoglobin fluoride: measurements of distal histidine ionization constants, Biochemistry, vol.20, issue.12, pp.3339-3346, 1981.
DOI : 10.1021/bi00515a004

M. Tamura, Optical and magnetic measurements of horseradish peroxidase II. pH dependence of peroxidase, Biochimica et Biophysica Acta (BBA) - Protein Structure, vol.243, issue.2, pp.249-258, 1971.
DOI : 10.1016/0005-2795(71)90082-1

L. Vickery, T. Nozawa, and K. Sauer, Magnetic circular dichroism studies of myoglobin complexes. Correlations with heme spin state and axial ligation, Journal of the American Chemical Society, vol.98, issue.2, pp.343-350, 1976.
DOI : 10.1021/ja00418a005

A. E. Pond, M. Sono, E. A. Elenkova, D. B. Goodin, A. M. English et al., Influence of protein environment on magnetic circular dichroism spectral properties of ferric and ferrous ligand complexes of yeast cytochromec peroxidase, Biospectroscopy, vol.386, issue.276, pp.42-52, 1999.
DOI : 10.1002/(SICI)1520-6343(1999)5:5+<S42::AID-BSPY5>3.0.CO;2-9

S. A. Asher and T. M. Schuster, Resonance Raman examination of axial ligand bonding and spin-state equilibriums in metmyoglobin hydroxide and other heme derivatives, Biochemistry, vol.18, issue.24, pp.5377-5387, 1979.
DOI : 10.1021/bi00591a019

S. A. Asher, L. E. Vickery, T. M. Schuster, and K. Sauer, Resonance Raman spectra of methemoglobin derivatives. Selective enhancement of axial ligand vibrations and lack of an effect of inositol hexaphosphate, Biochemistry, vol.16, issue.26, pp.5849-5856, 1977.
DOI : 10.1021/bi00645a032

M. Tachikawa and M. Shiga, Geometrical H/D Isotope Effect on Hydrogen Bonds in Charged Water Clusters, Journal of the American Chemical Society, vol.127, issue.34, pp.11908-11909, 1909.
DOI : 10.1021/ja053135j

A. Feis, M. P. Marzocchi, M. Paoli, and G. Smulevich, Spin State and Axial Ligand Bonding in the Hydroxide Complexes of Metmyoglobin, Methemoglobin, and Horseradish Peroxidase at Room and Low Temperatures, Biochemistry, vol.33, issue.15, pp.4577-4583, 1994.
DOI : 10.1021/bi00181a019