Engineering, expression and biochemical characterization of the hemoglobin domain of a Erwinia chrysanthemi flavohemoprotein

European Journal of Biochemistry

Volumn 253, Issue 3, 1998, Pages 751-759

  Labesse, Gilles ^a   Craescu, Constantin T ^b   Mispelter, Joël ^b   Chottard, Geneviève ^c   Marden, Michael C ^d   Pin, Serge ^e   Forest, Eric ^f   Mornon, Jean Paul ^a   Boccara, Martine ^g  

^a UNIVERSITÉ PIERRE ET MARIE CURIE   (France)

^b INSTITUT CURIE   (France)

^c CNRS   (France)

^d BICÊTRE HOSPITAL   (France)

^e UNIVERSITÉ PARIS DESCARTES   (France)

^f INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^g AGROPARISTECH   (France)

Author keywords

1H NMR; Electron transfer; Heme cavity structure; Homology modelling; Structure function analysis

Indexed keywords

BACTERIAL PROTEIN; HEMOGLOBIN; HEMOPROTEIN;

ARTICLE; ERWINIA; ESCHERICHIA COLI; HEMOGLOBIN DETERMINATION; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS;

BACTERIA (MICROORGANISMS); ERWINIA; ERWINIA CHRYSANTHEMI; ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0032079717     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2530751.x     Document Type: Article

References (36)

1. Altschul, S., Gish, W., Miller, W., Myers, E. & Lipman, D. (1990) Basic Local Alignment Search Tool, J. Mol. Biol. 215, 403-410.
2. + reductase, FEBS Lett. 32, 247-252.
3. Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. & Struhl, K. (1987) Current protocols in molecular biology, Greene Publishing Assoc. and Wiley-Interscience, New York.
4. Bashford, D., Chothia, C. & Lesk, A. M. (1987) Determinants of protein fold unique features of globin amino acid sequences, J. Mol. Biol. 196, 199-216.
5. Bolognesi, M., Bordo, D., Rizzi, M., Tarricone, C. & Ascenzi, P. (1997) Nonvertebrate hemoglobins: structural bases for reactivity, Prog. Biophys. Molec. Biol. 68, 29-68.
6. Callebaut, I., Labesse, G., Durand, P., Poupon, A., Canard, L., Chomilier, J., Henrissat, B. & Mornon, J.-P. (1997) Deciphering protein sequence information through hydrophobic cluster (HCA): current status and perspectives, Cell. Mol. Life Sci. 53, 621-645.
7. Cooke, R. M., Dalvit, C., Narula, S. S. & Wright, P. E. (1987) NMR studies of the heme pocket conformations of monomeric hemoglobins from Glycera dibranchiata. Implications for ligand binding, Eur. J. Biochem. 166, 399-408.
8. Craescu, C. T. & Mispelter, J. (1989) Resonance assignments in the proton NMR spectrum of carbonmonoxy hemoglobin by two-dimensional methods, Eur. J. Biochem. 181, 87-96.
9. De Baere, I., Liu, L., Moens, L., van Beumen, J., Gielens, C., Richelle, J., Trotman, C., Finch, J., Gerstien, M. & Perutz, M. F. (1992) Polar zipper sequence in the high-affinity hemoglobin of Ascaris: amino acid sequence and structural interpretation, Proc. Natl Acad. Sci. USA 89, 4638-4642.
10. De Baere, I., Perutz, M. F., Kiger, L., Marden, M. C. & Poyart, C. (1994) Formation of two hydrogen bonds from the globin to the heme-linked oxygen molecule in Ascaris hemoglobin, Proc. Natl Acad. Sci. USA 91, 1594-1597.
11. Dikshit, R. P., Dikshit, K. L., Liu, Y. & Webster, D. A. (1992) The bacterial hemoglobin from Vitreoscilla can support the aerobic growth of Escherichia coli lacking terminal oxidases, Arch. Biochem. Biophys. 292, 29-33.
12. Ermler, U., Siddiqui, R. A., Cramm, R. & Friedrich, B. (1995) Crystal structure of the flavohemoglobin from Alcaligenes eutrophus at 1.75 Å resolution, EMBO J. 14, 6067-6077.
13. Favey, S., Labesse, G., Vouille, V. & Boccara, M. (1995) Flavohaemoglobin HmpX: a new pathogenicity determinant in Erwinia chrysanthemi strain 3937, Microbiology 141, 863-871.
14. Fülöp, V., Phizackerley, R. P., Soltis, S. M., Clifton, I. J., Wakatsuki, S., Erman, J., Hajdu, J. & Edwards, S. L. (1994) Laue diffraction study on the strcture of cytochrome c peroxidase compound I, Structure 2, 201-208.
15. Gabbianelli, R., Santroni, A. M., Fedeli, D., Kantar, A. & Falcioni, G. (1998) Antioxidant activities of different hemoglobin derivatives, Biochem. Biophys. Res. Commun. 242, 560-564.
16. Gaspard, S., Chottard, G., Mathy, J.-P. & Mansuy, D. (1996) Study of the coordination chemistry of prostaglandin H synthase by Resonance Raman spectroscopy, Eur. J. Biochem. 238, 529-537.
17. Iwaasa, H., Takagi, T. & Shikama, K. (1992) Amino acid sequence of yeast hemoglobin a two domain structure, J. Mol. Biol. 227, 948-954.
18. LaCelle, M., Kumano, M., Kurita K., Yamane, K., Zuber, P. & Nakano, M. M. (1996) Oxygen-controlled regulation of the flavohemoglobin gene in Bacillus subtilis, J. Bacteriol. 178, 3803-3808.
19. Maniatis, T., Fritsch, E. F. & Sambrook, J. (1982) Molecular cloning: a laboratory manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY.
20. Martineau, L. & Craescu, C. T. (1992) Sequential assignment of the proton NMR spectrum of isolated alpha(CO) chains from human adult hemoglobin, Eur. J. Biochem. 205, 661-670.
21. Mieyal, J. J. & Starke, D. W. (1994) Hydroxylation and dealkylation reactions catalyzed by hemoglobin, Methods Enzymol. 231, 573-598.
22. Morikis, D., Champion, P. M., Springer, B. A., Egebey, K. D. & Sligar, S. G. (1990) Resonance Raman studies of iron spin and axial coordination in distal pocket mutants of ferric myoglobin, J. Biol. Chem. 265, 12143-12145.
23. Morikis, D., Lepre, C. A. & Wright, P. E. (1994) 1H resonance assignments and secondary structure of the carbon monoxide complex of soybean leghemoglobin determined by homonuclear two-dimensional and three-dimensional NMR spectroscopy, Eur. J. Biochem. 219, 611-626.
24. Osapay, K., Thierault, Y., Wright, P. E. & Case, D. A. (1994) Solution structure of carbonmonoxy myoglobin determined from nuclear resonance distance and chemical shift constraints, J. Mol. Biol. 244, 183-197.
25. Oshino, R., Asakura, T., Takio, K., Oshino, N. & Chance, B. (1973) Purification and molecular properties of yeast hemoglobin, Eur. J. Biochem. 39, 581-590.
26. Perutz, M. F. (1986) A bacterial haemoglobin, Nature 322, 405.
27. Poulos, T. L. & Raag, R. (1992) Cytochrome P450cam: crystallography, oxygen activation, and electron transfer, FASEB J. 6, 674-679.
28. Rizzi, M., Wittenberg, J. B., Coda, A., Fasano, M., Ascenzi, P. & Bolognesi, M. (1994) Structure of the sulfide-reactive hemoglobin from the clam Lucina pectinata, J. Mol. Biol. 244, 86-99.
29. Tarricone, C., Galizzi, A., Coda, A., Ascenzi, P. & Bolognesi, M. (1997) Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp, Structure 5, 497-507.
30. Tuffery, P. (1995) XmMol: an X11 and motif program for macromolecular visualization and modeling, J. Mol. Graphics 13, 67-72.
31. Vasudevan, S. G., Armarego, W. L. F., Shaw, D. C., Lilley, P. E., Dixon, N. E. & Poole, R. K. (1991) Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K12, Mol. Gen. Genet. 226, 49-58.
32. Wakabayashi, S., Matsubara, H. & Webster, D. A. (1986) Primary sequence of a dimeric bacterial haemoglobin from Vitreoscilla, Nature 322, 481-483.
33. Wishart, D. S., Sykes, B. D. & Richards, F. M. (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure, J. Mol. Biol. 222, 311-333.
34. Yang, J., Kloek, A. P., Goldberg, D. E. & Mathews, F. S. (1995) The structure of Ascaris hemoglobin domain I at 2.2 A resolution: molecular features of oxygen avidity, Proc. Natl Acad. Sci. USA 92, 4224-4228.
35. Yu, N. T. (1986) Resonance Raman studies of ligand binding, Methods Enzymol. 130, 351-409.
36. Zhu, H. & Riggs, A. F. (1992) Yeast flavohemoglobin is an ancient protein related to globins and a reductase family, Proc. Natl Acad. Sci. USA 89, 5015-5019.