S. Vinogradov, D. Hoogewijs, X. Bailly, R. Arredondo-peter, M. Guertin et al., Three globin lineages belonging to two structural classes in genomes from the three kingdoms of life, Proceedings of the National Academy of Sciences, vol.102, issue.32, pp.11385-11389, 2005.
DOI : 10.1073/pnas.0502103102

R. Weber and S. Vinogradov, Nonvertebrate hemoglobins: functions and molecular adaptations, Physiol Rev, vol.81, pp.569-628, 2001.

T. Freitas, J. Saito, S. Hou, and M. Alam, Globin-coupled sensors, protoglobins, and the last universal common ancestor, Journal of Inorganic Biochemistry, vol.99, issue.1, pp.23-33, 2005.
DOI : 10.1016/j.jinorgbio.2004.10.024

S. Vinogradov and L. Moens, Diversity of Globin Function: Enzymatic, Transport, Storage, and Sensing, Journal of Biological Chemistry, vol.283, issue.14, pp.8773-8777, 2008.
DOI : 10.1074/jbc.R700029200

M. Blaxter, Nemoglobins: Divergent nematode globins, Parasitology Today, vol.9, issue.10, pp.353-360, 1993.
DOI : 10.1016/0169-4758(93)90082-Q

T. Hankeln, H. Friedl, I. Ebersberger, J. Martin, and E. Schmidt, A variable intron distribution in globin genes of Chironomus: evidence for recent intron gain, Gene, vol.205, issue.1-2, pp.151-160, 1997.
DOI : 10.1016/S0378-1119(97)00518-0

H. Baumgarthl, K. Kritzler, W. Zimelka, and D. Zinkler, Local PO 2 measurements in the environment of submerged soil microarthroods, Acta Oecologica, vol.15, pp.781-789, 1994.

T. Paget, M. Fry, and D. Lloyd, Effects of inhibitors on the oxygen kinetics of Nippostrongylus brasiliensis, Molecular and Biochemical Parasitology, vol.22, issue.2-3, pp.125-134, 1987.
DOI : 10.1016/0166-6851(87)90042-9

H. Atkinson, Respiration in nematodes. Nematodes as biological models 1980, pp.101-142

J. Gray, D. Karow, H. Lu, A. Chang, J. Chang et al., Oxygen sensation and social feeding mediated by a C. elegans guanylate cyclase homologue, Nature, vol.33, issue.6997, pp.317-322, 2004.
DOI : 10.1146/annurev.micro.57.030502.090938

V. Voorhies, W. Ward, and S. , Broad oxygen tolerance in the nematode Caenorhabditis elegans, J Exp Biol, vol.203, pp.2467-2478, 2000.

R. Engh and R. Huber, Accurate bond and angle parameters for X-ray protein structure refinement, Acta Crystallographica Section A Foundations of Crystallography, vol.47, issue.4, pp.392-400, 1991.
DOI : 10.1107/S0108767391001071

R. Laskowski, M. Macarthur, D. Moss, and J. Thornton, 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

L. Holm and C. Sander, Structural alignment of globins, phycocyanins and colicin A, FEBS Letters, vol.8, issue.3, pp.301-306, 1993.
DOI : 10.1016/0014-5793(93)81183-Z

M. Bolognesi, D. Bordo, M. Rizzi, C. Tarricone, and P. Ascenzi, Nonvertebrate hemoglobins: Structural bases for reactivity, Progress in Biophysics and Molecular Biology, vol.68, issue.1, pp.29-68, 1997.
DOI : 10.1016/S0079-6107(97)00017-5

M. Perutz, Regulation of Oxygen Affinity of Hemoglobin: Influence of Structure of the Globin on the Heme Iron, Annual Review of Biochemistry, vol.48, issue.1, pp.327-386, 1979.
DOI : 10.1146/annurev.bi.48.070179.001551

E. Krissinel and K. Henrick, Detection of Protein Assemblies in Crystals, Complife 2005, LNBI 3695 Edited by: Berthold, pp.163-174
DOI : 10.1007/11560500_15

W. Royer, . Jr, W. Hendrickson, and E. Chiancone, The 2.4-? crystal structure of Scapharca dimeric hemoglobin Cooperativity based on directly communicating hemes at a novel subunit interface, J Biol Chem, vol.264, pp.21052-21061, 1989.
URL : https://hal.archives-ouvertes.fr/ujm-01378510

D. Mitchell, G. Kitto, and M. Hackert, Structural Analysis of Monomeric Hemichrome and Dimeric Cyanomet Hemoglobins fromCaudina arenicola, Journal of Molecular Biology, vol.251, issue.3, pp.421-431, 1995.
DOI : 10.1006/jmbi.1995.0445

D. Hoogewijs, D. Henau, S. Dewilde, S. Moens, L. Couvreur et al., The Caenorhabditis globin gene family reveals extensive nematode-specific radiation and diversification, BMC Evolutionary Biology, vol.8, issue.1, p.279, 2008.
DOI : 10.1186/1471-2148-8-279

M. Brunori, A. Giuffre, K. Nienhaus, G. Nienhaus, and F. Scandurra, Neuroglobin, nitric oxide, and oxygen: Functional pathways and conformational changes, Proceedings of the National Academy of Sciences, vol.102, issue.24, pp.8483-8488, 2005.
DOI : 10.1073/pnas.0408766102
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1150806

A. Fago, C. Hundahl, H. Malte, and R. Weber, Functional Properties of Neuroglobin and Cytoglobin. Insights into the Ancestral Physiological Roles of Globins, IUBMB Life, vol.56, issue.11, pp.689-696, 2004.
DOI : 10.1080/15216540500037299

E. Geuens, I. Brouns, D. Flamez, S. Dewilde, and J. Timmermans, A Globin in the Nucleus!, Journal of Biological Chemistry, vol.278, issue.33, pp.30417-30420, 2003.
DOI : 10.1074/jbc.C300203200

J. Murray, O. Delumeau, and R. Lewis, Structure of a nonheme globin in environmental stress signaling, Proceedings of the National Academy of Sciences, vol.102, issue.48, pp.17320-17325, 2005.
DOI : 10.1073/pnas.0506599102

W. Zhang, G. Phillips, and . Jr, Structure of the Oxygen Sensor in Bacillus subtilis, Structure, vol.11, issue.9, pp.1097-1110, 2003.
DOI : 10.1016/S0969-2126(03)00169-2

J. Sage, D. Morikis, and P. Champion, Spectroscopic studies of myoglobin at low pH: heme structure and ligation, Biochemistry, vol.30, issue.5, pp.1227-1237, 1991.
DOI : 10.1021/bi00219a010

S. Huang, J. Huang, A. Kloek, D. Goldberg, and J. Friedman, Hydrogen Bonding of Tyrosine B10 to Heme-bound Oxygen in Ascaris Hemoglobin: DIRECT EVIDENCE FROM UV RESONANCE RAMAN SPECTROSCOPY, Journal of Biological Chemistry, vol.271, issue.2, pp.958-962, 1996.
DOI : 10.1074/jbc.271.2.958

A. Pesce, M. Nardini, P. Ascenzi, E. Geuens, S. Dewilde et al., Thr-E11 Regulates O2 Affinity in Cerebratulus lacteus Mini-hemoglobin, Journal of Biological Chemistry, vol.279, issue.32, pp.33662-33672, 2004.
DOI : 10.1074/jbc.M403597200

S. Dewilde, L. Kiger, T. Burmester, T. Hankeln, V. Baudin-creuza et al., Biochemical Characterization and Ligand Binding Properties of Neuroglobin, a Novel Member of the Globin Family, Journal of Biological Chemistry, vol.276, issue.42, pp.38949-38955, 2001.
DOI : 10.1074/jbc.M106438200

H. Sawai, M. Makino, Y. Mizutani, T. Ohta, H. Sugimoto et al., Structural Characterization of the Proximal and Distal Histidine Environment of Cytoglobin and Neuroglobin, Biochemistry, vol.44, issue.40, pp.13257-13265, 2005.
DOI : 10.1021/bi050997o

A. Fago, A. Mathews, S. Dewilde, L. Moens, and T. Brittain, The reactions of neuroglobin with CO: Evidence for two forms of the ferrous protein, Journal of Inorganic Biochemistry, vol.100, issue.8, pp.1339-1343, 2006.
DOI : 10.1016/j.jinorgbio.2006.03.009

M. Brunori and B. Vallone, Neuroglobin, seven years after, Cellular and Molecular Life Sciences, vol.64, issue.10, pp.1259-1268, 2007.
DOI : 10.1007/s00018-007-7090-2

A. Fago, C. Hundahl, S. Dewilde, K. Gilany, L. Moens et al., Allosteric Regulation and Temperature Dependence of Oxygen Binding in Human Neuroglobin and Cytoglobin, Journal of Biological Chemistry, vol.279, issue.43, pp.44417-44426, 2004.
DOI : 10.1074/jbc.M407126200

J. Fraser, L. De-mello, D. Ward, H. Rees, D. Williams et al., From The Cover: Hypoxia-inducible myoglobin expression in nonmuscle tissues, Proceedings of the National Academy of Sciences, vol.103, issue.8, pp.2977-2981, 2006.
DOI : 10.1073/pnas.0508270103

E. Fordel, E. Geuens, S. Dewilde, P. Rottiers, P. Carmeliet et al., Cytoglobin expression is upregulated in all tissues upon hypoxia: an in vitro and in vivo study by quantitative real-time PCR, Biochemical and Biophysical Research Communications, vol.319, issue.2, pp.342-348, 2004.
DOI : 10.1016/j.bbrc.2004.05.010

M. Schmidt, F. Gerlach, A. Avivi, T. Laufs, S. Wystub et al., Cytoglobin Is a Respiratory Protein in Connective Tissue and Neurons, Which Is Up-regulated by Hypoxia, Journal of Biological Chemistry, vol.279, issue.9, pp.8063-8069, 2004.
DOI : 10.1074/jbc.M310540200

A. Roesner, T. Hankeln, and T. Burmester, Hypoxia induces a complex response of globin expression in zebrafish (Danio rerio), Journal of Experimental Biology, vol.209, issue.11, pp.2129-2137, 2006.
DOI : 10.1242/jeb.02243

C. Awenius, T. Hankeln, and T. Burmester, Neuroglobins from the Zebrafish Danio rerio and the Pufferfish Tetraodon nigroviridis, Biochemical and Biophysical Research Communications, vol.287, issue.2, pp.418-421, 2001.
DOI : 10.1006/bbrc.2001.5614

A. Roesner, S. Mitz, T. Hankeln, and T. Burmester, Globins and hypoxia adaptation in the goldfish, Carassius???auratus, FEBS Journal, vol.72, issue.14, pp.3633-3643, 2008.
DOI : 10.1111/j.1742-4658.2008.06508.x

T. Gorr, J. Cahn, H. Yamagata, and H. Bunn, Hypoxia-induced Synthesis of Hemoglobin in the Crustacean Daphnia magna Is Hypoxia-inducible Factor-dependent, Journal of Biological Chemistry, vol.279, issue.34, pp.36038-36047, 2004.
DOI : 10.1074/jbc.M403981200

T. Farazi, G. Waksman, and J. Gordon, The Biology and Enzymology of ProteinN-Myristoylation, Journal of Biological Chemistry, vol.276, issue.43, pp.39501-39504, 2001.
DOI : 10.1074/jbc.R100042200

A. Leslie and . Mosflm-user-guide, Msoflm Version 6.2.3 Cambridge, 1993.

P. Evans, Proceedings of the CCP4 study weekend on data collection and processing UK: CLRC Daresbury Laboratory, 1993.

T. Terwilliger and J. Berendzen, Automated MAD and MIR structure solution, Acta Crystallographica Section D Biological Crystallography, vol.55, issue.4, pp.849-861, 1999.
DOI : 10.1107/S0907444999000839

A. Perrakis, R. Morris, and V. Lamzin, Automated protein model building combined with iterative structure refinement, Nature Structural Biology, vol.6, issue.5, pp.458-463, 1999.
DOI : 10.1038/8263

P. Emsley and K. Cowtan, : model-building tools for molecular graphics, Acta Crystallographica Section D Biological Crystallography, vol.60, issue.12, pp.2126-2132, 2004.
DOI : 10.1107/S0907444904019158

G. Murshudov, A. Vagin, and E. Dodson, Refinement of Macromolecular Structures by the Maximum-Likelihood Method, Acta Crystallographica Section D Biological Crystallography, vol.53, issue.3, pp.240-255, 1997.
DOI : 10.1107/S0907444996012255

A. Vagin and A. Teplyakov, : an Automated Program for Molecular Replacement, Journal of Applied Crystallography, vol.30, issue.6, pp.1022-1025, 1997.
DOI : 10.1107/S0021889897006766

R. Laskowski, SURFNET: A program for visualizing molecular surfaces, cavities, and intermolecular interactions, Journal of Molecular Graphics, vol.13, issue.5, pp.323-328, 1995.
DOI : 10.1016/0263-7855(95)00073-9

H. Berman, J. Westbrook, Z. Feng, G. Gilliland, T. Bhat et al., The Protein Data Bank, Nucleic Acids Research, vol.28, issue.1, pp.235-242, 2000.
DOI : 10.1093/nar/28.1.235

J. Uzan, S. Dewilde, T. Burmester, T. Hankeln, L. Moens et al., Neuroglobin and Other Hexacoordinated Hemoglobins Show a Weak Temperature Dependence of Oxygen Binding, Biophysical Journal, vol.87, issue.2, pp.1196-1204, 2004.
DOI : 10.1529/biophysj.104.042168

R. Weber, W. Voelter, A. Fago, H. Echner, E. Campanella et al., Modulation of red cell glycolysis: interactions between vertebrate hemoglobins and cytoplasmic domains of band 3 red cell membrane proteins, AJP: Regulatory, Integrative and Comparative Physiology, vol.287, issue.2, pp.454-464, 2004.
DOI : 10.1152/ajpregu.00060.2004

A. Hayashi, T. Suzuki, and M. Shin, An enzymic reduction system for metmyoglobin and methemoglobin, and its application to functional studies of oxygen carriers, Biochimica et Biophysica Acta (BBA) - Protein Structure, vol.310, issue.2, pp.309-316, 1973.
DOI : 10.1016/0005-2795(73)90110-4

D. Hoogewijs, K. Houthoofd, F. Matthijssens, J. Vandesompele, and J. Vanfleteren, Selection and validation of a set of reliable reference genes for quantitative sod gene expression analysis in C. elegans, BMC Molecular Biology, vol.9, issue.1, p.9, 2008.
DOI : 10.1186/1471-2199-9-9

J. Hellemans, G. Mortier, D. Paepe, A. Speleman, F. Vandesompele et al., qBase relative quantification framework and software for management and automated analysis of real-time quantitative PCR data, Genome Biology, vol.8, issue.2, p.19, 2007.
DOI : 10.1186/gb-2007-8-2-r19

J. Vandesompele, D. Preter, K. Pattyn, F. Poppe, B. Van-roy et al., Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes, Genome Biol, vol.311, pp.34-35, 2002.

O. Hobert, PCR fusion-based approach to create reporter gene constructs for expression analysis in transgeni c C. elegans, Biotechniques, vol.82, pp.728-730, 2002.

P. Kraulis, MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, Journal of Applied Crystallography, vol.24, issue.5, pp.946-950, 2006.
DOI : 10.1107/S0021889891004399

J. Olson and G. Philips, Myoglobin discriminates between O 2 , NO, and CO by electrostatic interactions with the bound ligand, Journal of Biological Inorganic Chemistry, vol.2, issue.4, pp.544-552, 1997.
DOI : 10.1007/s007750050169

I. De-baere, L. Liu, L. Moens, J. Van-beeumen, C. Gielens et al., Polar zipper sequence in the high-affinity hemoglobin of Ascaris suum: amino acid sequence and structural interpretation., Proceedings of the National Academy of Sciences, vol.89, issue.10, pp.4638-4642, 1992.
DOI : 10.1073/pnas.89.10.4638