C. Wandersman and P. Delepelaire, Bacterial Iron Sources: From Siderophores to Hemophores, Annual Review of Microbiology, vol.58, issue.1, pp.611-647, 2004.
DOI : 10.1146/annurev.micro.58.030603.123811

S. Letoffe, J. M. Ghigo, and C. Wandersman, Iron acquisition from heme and hemoglobin by a Serratia marcescens extracellular protein., Proceedings of the National Academy of Sciences, vol.91, issue.21, pp.9876-9880, 1994.
DOI : 10.1073/pnas.91.21.9876

S. Letoffe, V. Redeker, and C. Wandersman, Isolation and characterization of an extracellular haem-binding protein from Pseudomonas aeruginosa that shares function and sequence similarities with the Serratia marcescens HasA haemophore, Molecular Microbiology, vol.16, issue.6, pp.1223-1234, 1998.
DOI : 10.1046/j.1365-2958.1997.2641628.x

S. Letoffe, K. Omori, and C. Wandersman, Functional Characterization of the HasAPF Hemophore and Its Truncated and Chimeric Variants: Determination of a Region Involved in Binding to the Hemophore Receptor, Journal of Bacteriology, vol.182, issue.16, pp.4401-4405, 2000.
DOI : 10.1128/JB.182.16.4401-4405.2000

M. S. Rossi, J. D. Fetherston, S. Letoffe, E. Carniel, R. D. Perry et al., Identification and Characterization of the Hemophore-Dependent Heme Acquisition System of Yersinia pestis, Infection and Immunity, vol.69, issue.11, pp.6707-6717, 2001.
DOI : 10.1128/IAI.69.11.6707-6717.2001

J. M. Ghigo, S. Letoffe, 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

J. T. Lecomte, J. D. Smit, K. H. Winterhalter, L. Mar, and G. N. , Structural and electronic properties of the liver fluke heme cavity by nuclear magnetic resonance and optical spectroscopy, Journal of Molecular Biology, vol.209, issue.2, pp.235-247, 1989.
DOI : 10.1016/0022-2836(89)90275-1

T. Uchida, J. M. Stevens, O. Daltrop, E. M. Harvat, L. Hong et al., Maturation Protein CcmE, Journal of Biological Chemistry, vol.279, issue.50, pp.51981-51988, 2004.
DOI : 10.1074/jbc.M408963200

S. Nagatomo, Y. Jin, M. Nagai, H. Hori, and T. Kitagawa, Changes in the abnormal ??-subunit upon CO-binding to the normal ??-subunit of Hb M Boston: resonance Raman, EPR and CD study, Biophysical Chemistry, vol.98, issue.1-2, pp.217-232, 2002.
DOI : 10.1016/S0301-4622(02)00103-5

N. Wolff, C. Deniau, S. Letoffe, C. Simenel, V. Kumar et al., Histidine pKa shifts and changes of tautomeric states induced by the binding of gallium-protoporphyrin IX in the hemophore HasASM, Protein Science, vol.11, issue.4, pp.757-765, 2002.
DOI : 10.1110/ps.3630102

URL : https://hal.archives-ouvertes.fr/pasteur-00164701

C. Caillet-saguy, M. Delepierre, A. Lecroisey, I. Bertini, M. Piccioli et al., C NMR to Investigate the Iron(III) Hemophore HasA, Journal of the American Chemical Society, vol.128, issue.1, pp.150-158, 2006.
DOI : 10.1021/ja054902h

URL : https://hal.archives-ouvertes.fr/pasteur-00367136

S. Letoffe, 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

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

N. Izadi-pruneyre, F. Huche, G. S. Lukat-rodgers, A. Lecroisey, R. Gilli et al., The Heme Transfer from the Soluble HasA Hemophore to Its Membrane-bound Receptor HasR Is Driven by Protein-Protein Interaction from a High to a Lower Affinity Binding Site, Journal of Biological Chemistry, vol.281, issue.35, pp.25541-25550, 2006.
DOI : 10.1074/jbc.M603698200

URL : https://hal.archives-ouvertes.fr/pasteur-00366583

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. Perrakis, T. K. Sixma, K. S. Wilson, and V. S. Lamzin, : Improvement and Extension of Crystallographic Phases by Weighted Averaging of Multiple-Refined Dummy Atomic Models, Acta Crystallographica Section D Biological Crystallography, vol.53, issue.4, pp.448-455, 1997.
DOI : 10.1107/S0907444997005696

R. A. Laskowski, M. W. Macarthur, D. S. Moss, T. , and J. M. , PROCHECK: a program to check the stereochemical quality of protein structures, Journal of Applied Crystallography, vol.26, issue.2, pp.283-291, 1993.
DOI : 10.1107/S0021889892009944

S. Adachi, S. Nagano, K. Ishimori, Y. Watanabe, I. Morishima et al., Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase, Biochemistry, vol.32, issue.1, pp.241-252, 1993.
DOI : 10.1021/bi00052a031

G. S. Lukat-rodgers and K. R. Rodgers, Spin-state equilibria and axial ligand bonding in FixL hydroxide: a resonance raman study, Journal of Biological Inorganic Chemistry, vol.3, issue.3, pp.274-281, 1998.
DOI : 10.1007/s007750050232

S. H. Song, . Boffi, E. Chiancone, and D. L. Rousseau, Protein-heme interactions in hemoglobin from the mollusk Scapharca inaequivalvis: Evidence from resonance Raman scattering, Biochemistry, vol.32, issue.25, pp.6330-6336, 1993.
DOI : 10.1021/bi00076a005

S. R. Yeh, M. Couture, Y. Ouellet, M. Guertin, and D. L. Rousseau, A Cooperative Oxygen Binding Hemoglobin from Mycobacterium tuberculosis: STABILIZATION OF HEME LIGANDS BY A DISTAL TYROSINE RESIDUE, Journal of Biological Chemistry, vol.275, issue.3, pp.1679-1684, 2000.
DOI : 10.1074/jbc.275.3.1679

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, Journal of the American Chemical Society, vol.122, issue.30, pp.7368-7376, 2000.
DOI : 10.1021/ja000587h

I. Bertini, P. Turano, and A. J. Vila, Nuclear magnetic resonance of paramagnetic metalloproteins, Chemical Reviews, vol.93, issue.8, pp.2833-2932, 1993.
DOI : 10.1021/cr00024a009

L. Mar, G. N. Budd, D. L. Smith, K. M. Langry, and K. C. , Nuclear magnetic resonance of high-spin ferric hemoproteins. Assignment of proton resonances in met-aquo myoglobins using deuterium-labeled hemes, Journal of the American Chemical Society, vol.102, issue.6, pp.1822-1827, 1980.
DOI : 10.1021/ja00526a011

J. Z. Wu, L. Mar, G. N. Yu, L. P. Lee, K. B. Walker et al., Proton NMR study of the solution molecular and electronic structure of Escherichia coli ferricytochrome b562: evidence for S = 1/2 .dblarw. S = 5/2 spin equilibrium for intact His/Met ligation, Biochemistry, vol.30, issue.8, pp.2156-2165, 1991.
DOI : 10.1021/bi00222a020

I. Bertini and C. Luchinat, NMR of Paramagnetic Molecules in Biological Systems, 1986.

G. C. Chu, T. Tomita, F. D. Sonnichsen, T. Yoshida, and M. Ikeda-saito, The Heme Complex of Hmu O, a Bacterial Heme Degradation Enzyme from Corynebacterium diphtheriae: STRUCTURE OF THE CATALYTIC SITE, Journal of Biological Chemistry, vol.274, issue.35, pp.24490-24496, 1999.
DOI : 10.1074/jbc.274.35.24490

U. Pande, L. Mar, G. N. Lecomte, J. T. Ascoli, F. Brunori et al., NMR study of the molecular and electronic structure of the heme cavity of Aplysia metmyoglobin. Resonance assignments based on isotope labeling and proton nuclear Overhauser effect measurements, Biochemistry, vol.25, issue.19, pp.5638-5646, 1986.
DOI : 10.1021/bi00367a044

I. Bertini, B. Jimenez, M. Piccioli, and L. Poggi, C COSY Spectra Provides Information on Ligand Geometry in Paramagnetic Proteins, Journal of the American Chemical Society, vol.127, issue.35, pp.12216-12217, 2005.
DOI : 10.1021/ja051058m

F. Arnesano, L. Banci, and M. Piccioli, NMR structures of paramagnetic metalloproteins, Quarterly Reviews of Biophysics, vol.38, issue.02, pp.167-219, 2005.
DOI : 10.1017/S0033583506004161

B. W. Matthews, Solvent content of protein crystals, Journal of Molecular Biology, vol.33, issue.2, pp.491-497, 1968.
DOI : 10.1016/0022-2836(68)90205-2

Y. Yamamoto, T. Suziki, and H. Hori, Dynamics and thermodynamics of acid-alkaline transitions in metmyoglobins lacking the usual distal histidine residue, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol.1203, issue.2, pp.267-275, 1993.
DOI : 10.1016/0167-4838(93)90093-7

T. Iizuka and M. Kotani, Analysis of thermal equilibrium between high-spin and low-spin states in ferrihemoglobin complexes, Biochimica et Biophysica Acta (BBA) - Protein Structure, vol.194, issue.2, pp.351-363, 1969.
DOI : 10.1016/0005-2795(69)90096-8

T. Iizuka and M. Kotani, Analysis of thermal equilibrium between high-spin and low-spin states in ferrimyoglobin complexes, Biochimica et Biophysica Acta (BBA) - Protein Structure, vol.181, issue.1, pp.275-286, 1969.
DOI : 10.1016/0005-2795(69)90250-5

E. Antonini, M. Brunori, C. Greenwood, B. G. Malmstrom, R. et al., The Interaction of Cyanide with Cytochrome Oxidase, European Journal of Biochemistry, vol.189, issue.2, pp.396-400, 1971.
DOI : 10.1111/j.1432-1033.1971.tb01633.x

L. Banci, I. Bertini, K. L. Bren, H. B. Gray, and P. Turano, pH-dependent equilibria of yeast Met80Ala-iso-1-cytochrome c probed by NMR spectroscopy: a comparison with the wild-type protein, Chemistry & Biology, vol.2, issue.6, pp.377-383, 1995.
DOI : 10.1016/1074-5521(95)90218-X

L. Banci, I. Bertini, L. D. Eltis, and R. Pierattelli, Spectroscopic characterization of a newly isolated cytochrome P450 from Rhodococcus rhodochrous, Biophysical Journal, vol.65, issue.2, pp.806-813, 1993.
DOI : 10.1016/S0006-3495(93)81122-6

R. M. Keller, K. Wuthrich, and P. G. Debrunner, Proton Magnetic Resonance Reveals High-Spin Iron (II) in Ferrous Cytochrome P450cam from Pseudomonas putida, Proceedings of the National Academy of Sciences, vol.69, issue.8, pp.2073-2075, 1972.
DOI : 10.1073/pnas.69.8.2073

I. Bertini, F. Briganti, R. Monnanni, A. Scozzafava, P. Carlozzi et al., 1H NMR studies of Chromatium vinosum cytochrome c???, Archives of Biochemistry and Biophysics, vol.282, issue.1, pp.84-90, 1990.
DOI : 10.1016/0003-9861(90)90090-L

M. Motie, R. J. Kassner, T. E. Meyer, and M. A. Cusanovich, Kinetics of cyanide binding to Chromatium vinosum ferricytochrome c', Biochemistry, vol.29, issue.7, pp.1932-1936, 1990.
DOI : 10.1021/bi00459a038

S. Letoffe, L. Debarbieux, N. Izadi, P. Delepelaire, and C. Wandersman, Ligand delivery by haem carrier proteins: the binding of Serratia marcescens haemophore to its outer membrane receptor is mediated by two distinct peptide regions, Molecular Microbiology, vol.179, issue.1, pp.77-88, 2003.
DOI : 10.1046/j.1365-2958.2003.03686.x

URL : https://hal.archives-ouvertes.fr/pasteur-00366306