Ligand- and proton-linked conformational changes of the ferrous 2/2 hemoglobin of Pseudoalteromonas haloplanktis TAC125

IUBMB Life

Volumn 63, Issue 7, 2011, Pages 566-573

  Giordano, Daniela ^a   Russo, Roberta ^a   Ciaccio, Chiara ^b,c   Howes, Barry D ^d   Di Prisco, Guido ^a   Marden, Michael C ^e   Hui Bon Hoa, Gaston ^e   Smulevich, Giulietta ^d   Coletta, Massimo ^b,c   Verde, Cinzia ^a  

^a INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

^b UNIVERSITY OF ROME TOR VERGATA   (Italy)

^c Interuniversity Consortium for the Research on the Chemistry of Metals in Biological Systems   (Italy)

^d UNIVERSITY OF FLORENCE   (Italy)

^e INSERM   (France)

Author keywords

Antarctic; hemoglobin; ligand binding; resonance Raman

Indexed keywords

CARBON MONOXIDE; HEMOGLOBIN;

ALKALINITY; ANTARCTICA; ARTICLE; CONFORMATIONAL TRANSITION; DYNAMICS; EQUILIBRIUM CONSTANT; IRON KINETICS; LIGAND BINDING; NONHUMAN; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PSEUDOALTEROMONAS; PSEUDOALTEROMONAS HALOPLANKTIS; SPECTROSCOPY; TEMPERATURE;

BACTERIA (MICROORGANISMS); PSEUDOALTEROMONAS HALOPLANKTIS;

EID: 79959575656     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.492     Document Type: Article

References (32)

1. Vinogradov, S. N., Hoogewijs, D., Bailly, X., Arredondo-Peter, R., Guertin, M., Gough, J., Dewilde S., Moens, L., and, Vanfleteren J. R., (2005) Three globin lineages belonging to two structural classes in genomes from the three kingdoms of life. Proc. Natl. Acad. Sci. USA 102, 11385-11389. (Pubitemid 41153829)
2. Pesce, A., Couture, M., Dewilde, S., Guertin, M., Yamauchi, K., Ascenzi, P., Moens, L., and, Bolognesi, M., (2000) A novel two-over-two alpha-helical sandwich fold is characteristic of the truncated hemoglobin family. EMBO J. 19, 2424-2434. (Pubitemid 30323532)
3. Wittenberg, J. B., Bolognesi, M., Wittenberg, B. A., and, Guertin, M., (2002) Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants. J. Biol. Chem. 227, 871-874. (Pubitemid 34968827)
4. Wu, G., Wainwright, L. M., and, Poole, R. K., (2003) Microbial globins. Adv. Microb. Physiol. 47, 255-310. (Pubitemid 37214152)
5. Nicoletti, F. P., Comandini, A., Bonamore, A., Boechi, L., Boubeta, F., Feis, A., Smulevich, G., and, Boffi, A., (2010) Sulfide binding properties of truncated hemoglobins. Biochemistry 49, 2269-2278.
6. Giangiacomo, L., Ilari, A., Boffi, A., Morea, V., and, Chiancone, E., (2005) The truncated oxygen-avid hemoglobin from Bacillus subtilis. J. Biol. Chem. 280, 9192-9202.
7. Bonamore, A., Ilari, A., Giangiacomo, L., Bellelli, A., Morea, V., and, Boffi, A., (2005) A novel thermostable hemoglobin from the actinobacterium Thermobifida fusca. FEBS J. 272, 4189-4201. (Pubitemid 41160925)
8. Ilari, A., Kjelgaard, P., von Wachenfeldt, C., Catacchio, B., Chiancone, E., and, Boffi, A., (2007) Crystal structure and ligand binding properties of the truncated hemoglobin from Geobacillus stearothermophilus. Arch. Biochem. Biophys. 457, 85-94. (Pubitemid 44969279)
9. Milani, M., Savard, P. Y., Ouellet, H., Ascenzi, P., Guertin, M., and, Bolognesi, M., (2003) A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O. Proc. Natl. Acad. Sci. USA 100, 5766-5771. (Pubitemid 36576882)
10. Milani, M., Pesce, A., Nardini, M., Ouellet, H., Ouellet, Y., Dewilde, S., Bocedi, A., Ascenzi, P., Guertin, M., Moens, L., Friedman, J. M., Wittenberg, J. B., and, Bolognesi, M., (2005) Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins. J. Inorg. Biochem. 99, 97-109. (Pubitemid 39642973)
11. Médigue, C., Krin, E., Pascal, G., Barbe, V., Bernsel, A., Bertin, P. N., Cheung, F., Cruveiller, S., D'Amico, S., Duilio, A., Fang, G., Feller, G., Ho, C., Mangenot, S., Marino, G., Nilsson, J., Parrilli, E., Rocha, E. P., Rouy, Z., Sekowska, A., Tutino, M. L., Vallenet, D., von Heijne, G., and, Danchin, A., (2005) Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125. Genome Res. 15, 1325-1335. (Pubitemid 41400898)
12. Giordano, D., Parrilli, E., Dettaî, A., Russo, R., Barbiero, G., Marino, G., Lecointre, G., di Prisco, G., Tutino, M. L., and, Verde, C., (2007) The truncated hemoglobins in the Antarctic psychrophilic bacterium Pseudoalteromonas haloplanktis TAC125. Gene 398, 69-77. (Pubitemid 47078996)
13. Parrilli, E., Giuliani, M., Giordano, D., Russo, R., Marino, G., Verde, C., and, Tutino, M. L., (2010) The role of a 2-on-2 haemoglobin in oxidative and nitrosative stress resistance of Antarctic Pseudoalteromonas haloplanktis TAC125. Biochimie 92, 1003-1009.
14. Howes, B. D., Giordano, D., Boechi, L., Russo, R., Mucciacciaro, S., Ciaccio, C., Sinibaldi, F., Fittipaldi, M., MartÃ, M. A., Estrin, D. A., di Prisco, G., Coletta, M., Verde, C., and, Smulevich, G., (2011) The peculiar heme pocket of the 2/2 hemoglobin of cold adapted Pseudoalteromonas haloplanktis TAC125. J. Biol. Inorg. Chem. 16, 299-311
15. Droghetti, E., Nicoletti, F. P., Bonamore, A., Boechi, L., Mañez, P. A., Estrin, D. A., Boffi, A., Smulevich, G., and, Feis, A., (2010) Heme pocket structural properties of a bacterial truncated hemoglobin from Thermobifida fusca. Biochemistry 49, 10394-10402.
16. Antonini, E., and, Brunori, M., (1971) Hemoglobin and Myoglobin in Their Reactions with Ligands. North-Holland, Amsterdam.
17. Uzan, J., Dewilde, S., Burmester, T., Hankeln, T., Moens, L., Hamdane, D., Marden, M. C., and, Kiger, L., (2004) Neuroglobin and other hexa-coordinated hemoglobins show a weak temperature dependence of oxygen binding. Biophys. J. 2, 1196-1204. (Pubitemid 39095096)
18. Hori, H., and, Kitagawa, T., (1980) Iron-ligand stretching band in the resonance Raman spectra of ferrous iron porphyrin derivatives. Importance as a probe band for quaternary structure of hemoglobin. J. Am. Chem. Soc. 102, 3608-3613.
19. Stein, P., and, Spiro, T. G., (1980) Hydrogen-bond and deprotonation effects on the resonance Raman iron-imidazole mode in deoxy hemoglobin models: implication for hemoglobin cooperativity. J. Am. Chem. Soc. 102, 7795-7797.
20. Razzera, G., Vernal, J., Baruh, D., Serpa, V. I., Tavares, C., Lara, F., Souza, E. M., Pedrosa, F. O., Almeida, F. C., Terenzi, H., and, Valente, A. P., (2008) Spectroscopic characterization of a truncated haemoglobin from the nitrogen-fixing bacterium Herbaspirillum seropedicae. J. Biol. Inorg. Chem. 13, 1085-1096.
21. Couture, M., Das, T. K., Lee, H. C., Peisach, J., Rousseau, D. L., Wittenberg, B. A., Wittenberg, J. B., and, Guertin, M., (1999) Chlamydomonas chloroplast ferrous hemoglobin. Heme pocket structure and reaction with ligands. J. Biol. Chem. 274, 6898-6910.
22. Spiro, T. G., and, Wasbotten, I. H., (2005) CO as a vibrational probe of heme protein active sites. J. Inorg. Biochem. 99, 34-44. (Pubitemid 39642970)
23. Phillips, G. N. Jr., Teodoro, M. L., Li, T., Smith, B., and, Olson, J. S., (1999) Bound CO is a molecular probe of electrostatic potential in the distal pocket of myoglobin. J. Phys. Chem. B 103, 8817-8829. (Pubitemid 129613930)
24. Cameron, A. D., Smerdon, S. J., Wilkinson, A. J., Habash, J., Helliwell, J. R., Li, T., and, Olson, J. S., (1993) Distal pocket polarity in ligand binding to myoglobin: deoxy and carbonmonoxy forms of a threonine 68(E11) mutant investigated by X-ray crystallography and infrared spectroscopy. Biochemistry 32, 13061-13070. (Pubitemid 24005913)
25. Coletta, M., Ascenzi, P., and, Brunori, M., (1988) Kinetic evidence for a role of heme geometry on the modulation of carbon monoxide reactivity in human hemoglobin. J. Biol. Chem. 263, 18286-18289. (Pubitemid 19005105)
26. Ouellet, H., Juszczak, L., Dantsker, D., Samuni, U., Ouellet, Y. H., Savard, P.Y., Wittenberg, J.B., Wittenberg, B. A., Friedman, J. M., and, Guertin, M., (2003) Reactions of Mycobacterium tuberculosis truncated hemoglobin O with ligands reveal a novel ligand-inclusive hydrogen bond network. Biochemistry 42, 5764-5774. (Pubitemid 36582868)
27. Thijs, L., Vinck, E., Bolli, A., Trandafir, F., Wan, X., Hoogewijs, D., Coletta, M., Fago, A., Weber, R. E., van Doorslaer, S., Ascenzi, P., Alam, M., Moens, L., and, Dewilde, S., (2007) Characterization of a globin-coupled sensor with a gene-regulating function. J. Biol. Chem. 282, 37325-37340.
28. Pesce, A., Thijs, L., Nardini, M., Desmet, F., Sisinni, L., Gourlay, L., Bolli, A., Coletta, M., van Doorslaer, S., Wan, X., Alam, M., Ascenzi, P., Moens, L., Bolognesi, M., and, Dewilde, S., (2009) HisE11 and HisF8 provide bis-histidyl heme hexa-coordination in the globin domain of Geobacter sulfurreducens globin-coupled sensor. J. Mol. Biol. 386, 246-260.
29. Visca, P., Fabozzi, A., Petrucca, C., Ciaccio, C., Coletta, M., De Sanctis, G., Bolognesi, M., Milani, M., and, Ascenzi, P., (2002) The truncated hemoglobin from Mycobacterium lepre. Biochem. Biophys. Res. Commun. 294, 1064-1070.
30. Springer, B. A., Sligar, S. G., Olson, J. S., and, Phillips, G. N. Jr., (1994) Mechanisms of ligand recognition in myoglobin. Chem. Rev. 94, 699-714. (Pubitemid 24987707)
31. Wyman, J., Gill, S. J., Noll, L., Giardina, B., Colosimo, A., and, Brunori, M., (1977). The balance sheet of hemoglobin. Thermodynamics of CO binding by hemoglobin trout I. J. Mol. Biol. 109, 195-205. (Pubitemid 8027699)
32. Wittenberg, J. B., (1966) The molecular mechanism of hemoglobin- facilitated oxygen diffusion. J. Biol. Chem. 241, 104-114.