Oxygen binding and NO scavenging properties of truncated hemoglobin, HbN, of Mycobacterium smegmatis

FEBS Letters

Volumn 580, Issue 17, 2006, Pages 4031-4041

  Lama, Amrita ^a   Pawaria, Sudesh ^a   Dikshit, Kanak L ^a  

^a INSTITUTE OF MICROBIAL TECHNOLOGY   (India)

Author keywords

Acidified nitrite; HbN; HbO; Hemoglobin; Mycobacterium smegmatis; Nitric oxide; Nitrosative stress; Oxygen uptake

Indexed keywords

DIOXYGENASE; HEMOGLOBIN; HEMOPROTEIN; NITRIC OXIDE; NITRITE; REACTIVE NITROGEN SPECIES;

AMINO TERMINAL SEQUENCE; ARTICLE; AUTOOXIDATION; BACTERIAL STRAIN; BINDING AFFINITY; CELL METABOLISM; CELL SURVIVAL; CIRCULAR DICHROISM; COMPARATIVE STUDY; DETOXIFICATION; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE EXPRESSION; GENE SEQUENCE; GENOMICS; METABOLISM; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NITROGEN UPTAKE; NONHUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL; SCAVENGING SYSTEM; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS; TOXICITY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; ESCHERICHIA COLI; HEMEPROTEINS; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NITRIC OXIDE; OXIDATION-REDUCTION; OXYGEN; OXYGENASES; PROTEIN BINDING; RECOMBINANT PROTEINS; SEQUENCE DELETION; SPECIES SPECIFICITY; STRUCTURAL HOMOLOGY, PROTEIN;

BACTERIA (MICROORGANISMS); CORYNEBACTERINEAE; MYCOBACTERIUM; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS;

EID: 33745812343     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.06.037     Document Type: Article

References (31)

1. Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., Gordon S.V., Eiglmeier K., Gas S., Barry C.E., Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., Mclean J., Moule S., Murphy L., Oliver K., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutters S., Seeger K., Skelton J., Squares R., Squares S., Sulston J.E., Taylor K., Whitehead S., and Barrell B.G. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393 (1998) 537-544
2. Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C., Harris D., Mungall K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy I., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., and Barrel B.G. Massive gene decay in the leprosy bacillus. Nature 409 (2001) 1007-1011
3. Wittenberg J.B., Bolognesi M., Wittenberg B.A., and Guertin M. Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants. J. Biol. Chem. 277 (2001) 871-874
4. Couture M., Yeh S.R., Wittenberg B.A., Wittenberg J.B., Ouellet Y., Rousseau D.L., and Guertin M. A cooperative oxygen-binding hemoglobin from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 96 (1999) 11223-11228
5. 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. Reaction of Mycobacterium tuberculosis truncated hemoglobin O with ligand reveal a novel ligand inclusive hydrogen bond network. Biochemistry 42 (2003) 5764-5774
6. Pathania R., Navani N.K., Rajamohan G., and Dikshit K.L. Mycobacterium tuberculosis Hemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant E. coli. J. Biol. Chem. 277 (2002) 15293-15302
7. Pathania R., Navani N.K., Gardner A.M., Gardner P.R., and Dikshit K.L. Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli. Mol. Microbiol. 45 (2002) 1303-1314
8. Ouellet H., Ouellet Y., Richard C., Labarre M., Wittenberg B., Wittenberg J., and Guertin M. Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide. Proc. Natl. Acad. Sci. USA 99 (2002) 5902-5907
9. 2 diffusion to the heme. EMBO J. 20 (2001) 3902-3909
10. Milani M., Pesce A., Ouellet Y., Dewilde S., Friedman J., Ascenzi P., Guertin M., and Bolgnesi M. Heme-ligand tunneling in group I truncated hemoglobins. J. Biol. Chem. 279 (2004) 21520-21525
11. Yeh S.R., Couture M., Ouellet Y., Guertin M., and Rousseau D.L. A cooperative oxygen binding hemoglobin from Mycobacterium tuberculosis. Stabilization of heme ligands by a distal tyrosine residue. J. Biol. Chem. 275 (2000) 1679-1684
12. Samuni U., Ouellet Y., Guertin M., Friedman J.M., and Yeh S.R. The absence of proximal strain in the truncated hemoglobins from Mycobacterium tuberculosis. J. Am. Chem. Soc. 126 (2004) 2682-2683
13. Poole R.K., and Hughes M.N. New functions for the ancient globin family,bacterial response to nitric oxide and nitrosative stress. Mol. Microbiol. 36 (2000) 775-783
14. Gardner P.R. Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myogloin and their associated reductases. J. Inorg. Biochem. 99 (2005) 247-266
15. Hernandez-Urzua E., Mills C.E., White G.P., Contreras-Zentella M.L., Escamilla E., Vasudevan S.G., Membrillo-Hernandez J., and Poole R.K. Flavohemoglobin Hmp, but not its individual domains, confers protection from respiratory inhibition by nitric oxide in Escherichia coli. J. Biol. Chem. 278 (2003) 34975-34982
16. MacMicking J.D., North R.J., LaCourse R., Mudgett J.S., Shah S.K., and Nathan C.F. Identification of nitric oxide synthase as a protective locus against tuberculosis. Proc. Natl. Acad. Sci. USA 94 (1997) 5243-5248
17. Turenne C.Y., Suchak A.A., Wolfe J.N., Kabani A., and Nicolle L.E. Soft tissue infection caused by a novel pigmented, rapidly growing mycobacterium species. J. Clin. Microbiol. 41 (2003) 2779-2782
18. Snapper S.B., Melton R.E., Mustafa S., Kieser T., and Jacobs Jr. W.R. Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol. Microbiol. 4 (1990) 1911-1919
19. Dikshit K.L., and Webster D.A. Cloning, characterization and expression of the bacterial globin gene from Vitreoscilla in Escherichia coli. Gene 70 (1988) 377-386
20. Kaur R., Pathania R., Sharma V., Mande S.C., and Dikshit K.L. Chimeric Vitreoscilla hemoglobin (VHb) carrying a flavoreductase domain relieves nitrosative stress in Escherichia coli: new insight into the functional role of VHb. Appl. Environ. Microbiol. 68 (2002) 152-160
21. Poole R.K., Anjum M.F., Membrillo-Hernandez J., Kim S.O., Hughes M.N., and Stewart V. Nitric oxide, nitrite and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12. J. Bacteriol. 178 (1996) 5487-5492
22. Appleby C.A. Purification of Rhizobium cytochromes P-450. Methods Enzymol. 52 (1978) 157-166
23. Thorsteinsson M.V., Bevan D.R., Ebel R.E., Weber R.E., and Potts M. Spectroscopical and functional characterization of the hemoglobin of Nostoc commune UTEX 584 (Cyanobacteria). Biochim. Biophys. Acta 1292 (1996) 133-139
24. Hausladen A., Gow A.J., and Stamler J.S. Nitrosative stress: metabolic pathway involving the flavohemoglobin. Proc. Natl. Acad. Sci. USA 95 (1998) 14100-14105
25. Liu J., Zeng M., Hausladen A., Heitman J., and Stamler J.S. Protection from nitrosative stress by yeast flavohemoglobin. Proc. Natl. Acad. Sci. USA 97 (2000) 4672-4676
26. Stevanin T.M., Ioannidis N., Mills C.E., Kim S.O., Hughes M.N., and Poole R.K. Flavohemoglobin Hmp affords inducible protection for Escherichia coli respiration, catalyzed by cytochromes bo′ or bd, from nitric oxide. J. Biol. Chem. 275 (2000) 35868-35875
27. Yamauchi K., Tada H., and Usuki I. Structure and evolution of Paramecium hemoglobin genes. Biochim. Biophys. Acta 1264 (1995) 53-62
28. Couture M., Das T.K., Lee H.C., Peisach J., Rousseau D.L., Wittenberg B.A., Wittenberg J.B., and Guertin M. Chlamydomonas chloroplast ferrous hemoglobin: heme pocket structure and reactions with ligands. J. Biol. Chem. 274 (1999) 6898-6910
29. Das T.K., Weber R.E., Dewilde S., Wittenberg J.B., Wittenberg B.A., Yamauchi K., VanHauwaert M.L., Moens L., and Rousseau D.L. Ligand binding in the ferric and ferrous states of Paramecium hemoglobin. Biochemistry 39 (2000) 14330-14340
30. Springer B.A., Egeberg K.D., Sligar S.G., Rohlfs R.J., Mathews A.J., and Olson J.S. Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. site directed mutagenesis of the distal histidine. J. Biol. Chem. 264 (1989) 3057-3060
31. Brantley Jr. R.E., Smerdon S.J., Wilkinson A.J., Singleton E.W., and Olson J.S. The mechanism of autooxidation of myoglobin. J. Biol. Chem. 268 (1993) 6995-7010