A. D. Adler, F. R. Longo, F. Kampas, K. , and J. , On the preparation of metalloporphyrins, Journal of Inorganic and Nuclear Chemistry, vol.32, issue.7, p.2443, 1970.
DOI : 10.1016/0022-1902(70)80535-8

S. L. Alam, B. F. Volkman, J. L. Markley, and J. D. Satterlee, Detailed NMR analysis of the heme-protein interactions in component IV Glycera dibranchiata monomeric hemoglobin-CO, Journal of Biomolecular NMR, vol.11, issue.2, pp.119-133, 1998.
DOI : 10.1023/A:1008202621725

P. Arnoux, R. Haser, N. Izadi, A. Lecroisey, M. Delepierre et al., The crystal structure of HasA, a hemophore secreted by Serratia marcescens, Nat. Struct. Biol, vol.6, pp.516-520, 1999.
URL : https://hal.archives-ouvertes.fr/hal-00313557

P. Arnoux, R. Haser, N. Izadi-pruneyre, A. Lecroisey, and M. Czjzek, Functional aspects of the heme bound hemophore HasA by structural analysis of various crystal forms, Proteins: Structure, Function, and Genetics, vol.8, issue.2, pp.202-210, 2000.
DOI : 10.1002/1097-0134(20001101)41:2<202::AID-PROT50>3.0.CO;2-8

URL : https://hal.archives-ouvertes.fr/hal-00313554

A. Bax and M. Summer, Proton and carbon-13 assignments from sensitivity-enhanced detection of heteronuclear multiple-bond connectivity by 2D multiple quantum NMR, Journal of the American Chemical Society, vol.108, issue.8, pp.2093-2094, 1986.
DOI : 10.1021/ja00268a061

S. Bhattacharya, S. Sukits, K. Maclaughlin, and J. Lecomte, The tautomeric state of histidines in myoglobin, Biophysical Journal, vol.73, issue.6, pp.3230-3240, 1997.
DOI : 10.1016/S0006-3495(97)78348-6

F. Blomberg, W. Maurer, R. , and H. , Nuclear magnetic resonance investigation of nitrogen-15-labeled histidine in aqueous solution, Journal of the American Chemical Society, vol.99, issue.25, pp.8149-8159, 1977.
DOI : 10.1021/ja00467a005

L. Bodenhausen and D. J. Ruben, Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy, Chemical Physics Letters, vol.69, issue.1, pp.185-189, 1980.
DOI : 10.1016/0009-2614(80)80041-8

URL : https://zenodo.org/record/45375

V. Braun and H. Killmann, Bacterial solutions to the iron-supply problem, Trends in Biochemical Sciences, vol.24, issue.3, pp.104-109, 1999.
DOI : 10.1016/S0968-0004(99)01359-6

J. M. Ghigo, S. Létoffé, and C. Wandersman, A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli., Journal of Bacteriology, vol.179, issue.11, pp.3572-3579, 1997.
DOI : 10.1128/jb.179.11.3572-3579.1997

R. D. Guiles, J. Altman, I. D. Kuntz, and L. Waskell, Structural studies of cytochrome b5: complete sequence-specific resonance assignments for the trypsin-solubilized microsomal ferrocytochrome b5 obtained from pig and calf, Biochemistry, vol.29, issue.5, pp.1276-1289, 1990.
DOI : 10.1021/bi00457a025

N. Izadi-pruneyre, N. Wolff, C. Castagne, M. Czisch, C. Wandersman et al., Backbone NMR assignment and secondary structure of the 19 kDa hemophore HasA, Journal of Biomolecular NMR, vol.14, issue.2, pp.193-194, 1999.
DOI : 10.1023/A:1008308802821

URL : https://hal.archives-ouvertes.fr/pasteur-00370459

N. Izadi-pruneyre, N. Wolff, V. Redeker, C. Wandersman, M. Delepierre et al., NMR studies of the C-terminal secretion signal of the haem-binding protein, HasA, European Journal of Biochemistry, vol.31, issue.2, pp.562-568, 1999.
DOI : 10.1093/emboj/17.4.936

URL : https://hal.archives-ouvertes.fr/pasteur-00370437

S. Létoffé, J. M. Ghigo, and C. Wandersman, Secretion of the Serratia marcescens HasA protein by an ABC transporter., Journal of Bacteriology, vol.176, issue.17, pp.5372-5377, 1994.
DOI : 10.1128/jb.176.17.5372-5377.1994

S. Létoffé, J. M. Ghigo, and C. Wandersman, Iron acquisition from heme and hemoglobin by a Serratia marcescens extracellular protein., Proc. Natl. Acad. Sci, pp.9876-9880, 1994.
DOI : 10.1073/pnas.91.21.9876

S. Létoffé, C. Deniau, N. Wolff, E. Dassa, P. Delepelaire et al., Haemophore-mediated bacterial haem transport: evidence for a common or overlapping site for haem-free and haem-loaded haemophore on its specific outer membrane receptor, Molecular Microbiology, vol.389, issue.2, pp.439-450, 2001.
DOI : 10.1046/j.1365-2958.2001.02530.x

R. B. Martin, Bioinorganic chemistry of aluminium, Met. Ions Biol. Syst, vol.24, pp.1-57, 1988.

R. Maurus, R. Bogumil, Y. Luo, H. L. Tang, M. Smith et al., Structural characterization of heme ligation in the His64?Tyr variant of myoglobin, J. Biol. Chem, vol.269, pp.12606-12610, 1994.

M. Nagai, Y. Yoneyama, and T. Kitagawa, Characteristics in tyrosine coordinations of four hemoglobins M probed by resonance Raman spectroscopy, Biochemistry, vol.28, issue.6, pp.2418-2422, 1989.
DOI : 10.1021/bi00432a012

Y. Nozaki and C. Tanford, [84] Examination of titration behavior, Methods Enzymol, vol.11, pp.715-734, 1967.
DOI : 10.1016/S0076-6879(67)11088-4

J. G. Pelton, D. A. Torchia, N. D. Meadow, and S. And-roseman, Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from escherichia coli, using two-dimensional heteronuclear NMR techniques, Protein Science, vol.88, issue.4, pp.543-558, 1993.
DOI : 10.1002/pro.5560020406

D. G. Rousseau and D. L. Rousseau, Hydrogen bonding of iron-coordinated histidine in heme proteins, J. Struct. Biol, vol.109, pp.13-17, 1992.

V. Sklenar, R. D. Peterson, M. R. Rejante, and J. And-feigon, Correlation of nucleotide base and sugar protons in a 15N-labeled HIV-1 RNA oligonucleotide by 1H-15N HSQC experiments, J. Biomol. NMR, vol.4, pp.117-122, 1994.

E. Steensma, E. Gordon, L. Öster, S. J. Ferguson, and J. Hajdu, Heme Ligation and Conformational Plasticity in the Isolatedc Domain of Cytochrome cd 1 Nitrite Reductase, Journal of Biological Chemistry, vol.276, issue.8, pp.5846-5855, 2001.
DOI : 10.1074/jbc.M007345200

I. Stojiljkovic, V. Kumar, and N. Srinivasan, Non-iron metalloporphyrins: potent antibacterial compounds that exploit haem/Hb uptake systems of pathogenic bacteria, Molecular Microbiology, vol.62, issue.2, pp.429-442, 1999.
DOI : 10.1046/j.1365-2958.1997.2641628.x

M. Tanokura, 1H-NMR study on the tautomerism of the imidazole ring of histidine residues, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol.742, issue.3, pp.576-585, 1983.
DOI : 10.1016/0167-4838(83)90276-5

A. A. Van-dijk, R. M. Scheek, K. Dijkstra, G. K. Wolters, and G. T. Robillard, Characterization of the protonation and hydrogen bonding state of the histidine residues in IIAmtl, a domain of the phosphoenolpyruvate-dependent mannitol-specific transport protein, Biochemistry, vol.31, issue.37, pp.9063-9072, 1992.
DOI : 10.1021/bi00152a050

Y. Yamamoto, T. Nakashima, E. Kawano, C. , and R. , 1H-NMR investigation of the influence of the heme orientation on functional properties of myoglobin, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol.1388, issue.2, pp.349-362, 1998.
DOI : 10.1016/S0167-4838(98)00193-9

L. P. Yu and G. M. Smith, Characterization of pH-dependent conformation heterogeneity in Rhodospirillum rubrum cytochrome c2 using nitrogen-15 and proton NMR, Biochemistry, vol.29, issue.12, pp.2920-2925, 1990.
DOI : 10.1021/bi00464a005