메뉴 건너뛰기




Volumn 436, Issue , 2008, Pages 317-337

Scavenging of Reactive Nitrogen Species by Mycobacterial Truncated Hemoglobins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARBONIC ACID DERIVATIVE; HEMOGLOBIN; MYCOBACTERIAL TRUNCATED HEMOGLOBIN; NITRIC OXIDE; OXIDIZING AGENT; PEROXYNITRITE; REACTIVE NITROGEN SPECIES; RECOMBINANT PROTEIN; SCAVENGER; UNCLASSIFIED DRUG; HEMOGLOBIN O, MYCOBACTERIUM TUBERCULOSIS; PEROXYNITROUS ACID; TRUNCATED HEMOGLOBIN; TRUNCATED HEMOGLOBIN, MYCOBACTERIUM LEPRAE;

EID: 35148877224     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(08)36018-2     Document Type: Chapter
Times cited : (38)

References (85)
  • 1
    • 0031396678 scopus 로고    scopus 로고
    • Comparison of the roles of reactive oxygen and nitrogen intermediates in the host response to Mycobacterium tuberculosis using transgenic mice
    • Adams L.B., Dinauer M.C., Morgenstern D.E., and Krahenbuhl J.L. Comparison of the roles of reactive oxygen and nitrogen intermediates in the host response to Mycobacterium tuberculosis using transgenic mice. Tuberc. Lung. Dis. 78 (1997) 237-246
    • (1997) Tuberc. Lung. Dis. , vol.78 , pp. 237-246
    • Adams, L.B.1    Dinauer, M.C.2    Morgenstern, D.E.3    Krahenbuhl, J.L.4
  • 3
    • 33845750255 scopus 로고    scopus 로고
    • Abacavir modulates peroxynitrite-mediated oxidation of ferrous nitrosylated human serum heme-albumin
    • Ascenzi P., and Fasano M. Abacavir modulates peroxynitrite-mediated oxidation of ferrous nitrosylated human serum heme-albumin. Biochem. Biophys. Res. Commun. 353 (2007) 469-474
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , pp. 469-474
    • Ascenzi, P.1    Fasano, M.2
  • 4
    • 33750503195 scopus 로고    scopus 로고
    • Peroxynitrite scavenging by ferrous truncated hemoglobin GlbO from Mycobacterium leprae
    • Ascenzi P., Milani M., and Visca P. Peroxynitrite scavenging by ferrous truncated hemoglobin GlbO from Mycobacterium leprae. Biochem. Biophys. Res. Commun. 351 (2006) 528-533
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 528-533
    • Ascenzi, P.1    Milani, M.2    Visca, P.3
  • 5
    • 33845995064 scopus 로고    scopus 로고
    • Reductive nitrosylation and peroxynitrite-mediated oxidation of heme-hemopexin
    • Ascenzi P., Bocedi A., Antonini G., Bolognesi M., and Fasano M. Reductive nitrosylation and peroxynitrite-mediated oxidation of heme-hemopexin. FEBS J. 274 (2007) 551-562
    • (2007) FEBS J. , vol.274 , pp. 551-562
    • Ascenzi, P.1    Bocedi, A.2    Antonini, G.3    Bolognesi, M.4    Fasano, M.5
  • 7
    • 34447509223 scopus 로고    scopus 로고
    • Mycobacterial truncated hemoglobins: From genes to functions
    • Ascenzi P., Bolognesi M., Milani M., Guertin M., and Visca P. Mycobacterial truncated hemoglobins: From genes to functions. Gene 398 (2007) 42-51
    • (2007) Gene , vol.398 , pp. 42-51
    • Ascenzi, P.1    Bolognesi, M.2    Milani, M.3    Guertin, M.4    Visca, P.5
  • 8
    • 28144440256 scopus 로고    scopus 로고
    • Nitric oxide scavenging by Mycobacterium leprae GlbO involves the formation of the ferric heme-bound peroxynitrite intermediate
    • Ascenzi P., Bocedi A., Bolognesi M., Fabozzi G., Milani M., and Visca P. Nitric oxide scavenging by Mycobacterium leprae GlbO involves the formation of the ferric heme-bound peroxynitrite intermediate. Biochem. Biophys. Res. Commun. 339 (2006) 448-454
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 448-454
    • Ascenzi, P.1    Bocedi, A.2    Bolognesi, M.3    Fabozzi, G.4    Milani, M.5    Visca, P.6
  • 9
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly
    • Beckman J.S., and Koppenol W.H. Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly. Am. J. Physiol. 271 (1996) C1424-C1437
    • (1996) Am. J. Physiol. , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 10
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide
    • Beckman J.S., Beckman T.W., Chen J., Marshall P.A., and Freeman B.A. Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide. Proc. Natl. Acad. Sci. USA 87 (1990) 1620-1624
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1620-1624
    • Beckman, J.S.1    Beckman, T.W.2    Chen, J.3    Marshall, P.A.4    Freeman, B.A.5
  • 12
    • 11144298023 scopus 로고    scopus 로고
    • Mechanistic studies of the oxidation of oxyhemoglobin by peroxynitrite
    • Boccini F., and Herold S. Mechanistic studies of the oxidation of oxyhemoglobin by peroxynitrite. Biochemistry 43 (2004) 16393-16404
    • (2004) Biochemistry , vol.43 , pp. 16393-16404
    • Boccini, F.1    Herold, S.2
  • 13
    • 0029688736 scopus 로고    scopus 로고
    • Syntheses of pure tetramethylammonium peroxynitrite
    • Bohle D.S., Glassbrenner P.A., and Hansert B. Syntheses of pure tetramethylammonium peroxynitrite. Methods Enzymol. 269 (1996) 302-311
    • (1996) Methods Enzymol. , vol.269 , pp. 302-311
    • Bohle, D.S.1    Glassbrenner, P.A.2    Hansert, B.3
  • 15
    • 0035312317 scopus 로고    scopus 로고
    • Nitric oxide moves myoglobin centre stage
    • Brunori M. Nitric oxide moves myoglobin centre stage. Trends Biochem. Sci. 26 (2001) 209-210
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 209-210
    • Brunori, M.1
  • 16
    • 0034867130 scopus 로고    scopus 로고
    • Cavities and packing defects in the structural dynamics of myoglobin
    • Brunori M., and Gibson Q.H. Cavities and packing defects in the structural dynamics of myoglobin. EMBO Rep. 2 (2001) 674-679
    • (2001) EMBO Rep. , vol.2 , pp. 674-679
    • Brunori, M.1    Gibson, Q.H.2
  • 20
    • 0037099165 scopus 로고    scopus 로고
    • Analysis of nitric oxide synthase and nitrotyrosine expression in human pulmonary tuberculosis
    • Choi H.S., Rai P.R., Cool C., Chu H.W., and Chan E.D. Analysis of nitric oxide synthase and nitrotyrosine expression in human pulmonary tuberculosis. Am. J. Respir. Crit. Care Med. 166 (2002) 178-186
    • (2002) Am. J. Respir. Crit. Care Med. , vol.166 , pp. 178-186
    • Choi, H.S.1    Rai, P.R.2    Cool, C.3    Chu, H.W.4    Chan, E.D.5
  • 21
    • 26644471251 scopus 로고    scopus 로고
    • Nitric oxide and mitochondrial biogenesis: A key to long-term regulation of cellular metabolism
    • Clementi E., and Nisoli E. Nitric oxide and mitochondrial biogenesis: A key to long-term regulation of cellular metabolism. Comp. Biochem. Physiol. 142 (2005) 102-110
    • (2005) Comp. Biochem. Physiol. , vol.142 , pp. 102-110
    • Clementi, E.1    Nisoli, E.2
  • 23
    • 0030432481 scopus 로고    scopus 로고
    • Purification and spectroscopic characterization of a recombinant chloroplastic hemoglobin from the green unicellular alga Chlamydomonas eugametos
    • Couture M., and Guertin M. Purification and spectroscopic characterization of a recombinant chloroplastic hemoglobin from the green unicellular alga Chlamydomonas eugametos. Eur. J. Biochem. 242 (1996) 779-787
    • (1996) Eur. J. Biochem. , vol.242 , pp. 779-787
    • Couture, M.1    Guertin, M.2
  • 25
    • 13244281710 scopus 로고    scopus 로고
    • Peroxynitrite and drug-dependent toxicity
    • Denicola A., and Radi R. Peroxynitrite and drug-dependent toxicity. Toxicology 208 (2005) 273-288
    • (2005) Toxicology , vol.208 , pp. 273-288
    • Denicola, A.1    Radi, R.2
  • 27
    • 33646240586 scopus 로고    scopus 로고
    • Truncated hemoglobin GlbO from Mycobacterium leprae alleviates nitric oxide toxicity
    • Fabozzi G., Ascenzi P., Di Renzi S., and Visca P. Truncated hemoglobin GlbO from Mycobacterium leprae alleviates nitric oxide toxicity. Microb. Pathog. 40 (2006) 211-220
    • (2006) Microb. Pathog. , vol.40 , pp. 211-220
    • Fabozzi, G.1    Ascenzi, P.2    Di Renzi, S.3    Visca, P.4
  • 30
    • 0141783647 scopus 로고    scopus 로고
    • Bacterial hemoglobins and flavohemoglobins: Versatile proteins and their impact on microbiology and biotechnology
    • Frey A.D., and Kallio P.T. Bacterial hemoglobins and flavohemoglobins: Versatile proteins and their impact on microbiology and biotechnology. FEMS Microbiol. Rev. 27 (2003) 525-545
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 525-545
    • Frey, A.D.1    Kallio, P.T.2
  • 31
    • 12344266500 scopus 로고    scopus 로고
    • Nitric oxide detoxification: A new era for bacterial globins in biotechnology?
    • Frey A.D., and Kallio P.T. Nitric oxide detoxification: A new era for bacterial globins in biotechnology?. Trends Biotechnol. 23 (2005) 69-73
    • (2005) Trends Biotechnol. , vol.23 , pp. 69-73
    • Frey, A.D.1    Kallio, P.T.2
  • 32
    • 0041806720 scopus 로고    scopus 로고
    • Myoglobin: The hydrogen atom of biology and a paradigm of complexity
    • Frauenfelder H., McMahon B.H., and Fenimore P.W. Myoglobin: The hydrogen atom of biology and a paradigm of complexity. Proc. Natl. Acad. Sci. USA 100 (2003) 8615-8617
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8615-8617
    • Frauenfelder, H.1    McMahon, B.H.2    Fenimore, P.W.3
  • 33
    • 0034724887 scopus 로고    scopus 로고
    • Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin): The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis
    • Gardner A.M., Martin L.A., Gardner P.R., Dou Y., and Olson J.S. Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin): The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis. J. Biol. Chem. 275 (2000) 12581-12589
    • (2000) J. Biol. Chem. , vol.275 , pp. 12581-12589
    • Gardner, A.M.1    Martin, L.A.2    Gardner, P.R.3    Dou, Y.4    Olson, J.S.5
  • 34
    • 21944443058 scopus 로고    scopus 로고
    • Chemistry of peroxynitrites and peroxynitrates
    • Goldstein S., Lind J., and Merényi G. Chemistry of peroxynitrites and peroxynitrates. Chem. Rev. 105 (2005) 2457-2470
    • (2005) Chem. Rev. , vol.105 , pp. 2457-2470
    • Goldstein, S.1    Lind, J.2    Merényi, G.3
  • 36
    • 0033046163 scopus 로고    scopus 로고
    • Kinetic and spectroscopic characterization of an intermediate peroxynitrite complex in the nitrogen monoxide induced oxidation of oxyhemoglobin
    • Herold S. Kinetic and spectroscopic characterization of an intermediate peroxynitrite complex in the nitrogen monoxide induced oxidation of oxyhemoglobin. FEBS Lett. 443 (1999) 81-84
    • (1999) FEBS Lett. , vol.443 , pp. 81-84
    • Herold, S.1
  • 37
    • 1242293624 scopus 로고    scopus 로고
    • Nitrotyrosine, dityrosine, and nitrotryptophan formation from metmyoglobin, hydrogen peroxide, and nitrite
    • Herold S. Nitrotyrosine, dityrosine, and nitrotryptophan formation from metmyoglobin, hydrogen peroxide, and nitrite. Free Radic. Biol. Med. 36 (2004) 565-579
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 565-579
    • Herold, S.1
  • 38
    • 2942756048 scopus 로고    scopus 로고
    • The outer-sphere oxidation of nitrosyliron(II)hemoglobin by peroxynitrite leads to the release of nitrogen monoxide
    • Herold S. The outer-sphere oxidation of nitrosyliron(II)hemoglobin by peroxynitrite leads to the release of nitrogen monoxide. Inorg. Chem. 43 (2004) 3783-3785
    • (2004) Inorg. Chem. , vol.43 , pp. 3783-3785
    • Herold, S.1
  • 39
    • 33748615158 scopus 로고    scopus 로고
    • • release from MbFe(II)NO and HbFe(II)NO after oxidation by peroxynitrite
    • • release from MbFe(II)NO and HbFe(II)NO after oxidation by peroxynitrite. Inorg. Chem. 45 (2006) 6933-6943
    • (2006) Inorg. Chem. , vol.45 , pp. 6933-6943
    • Herold, S.1    Boccini, F.2
  • 40
    • 26644473174 scopus 로고    scopus 로고
    • Reactions of peroxynitrite with globin proteins and their possible physiological role
    • Herold S., and Fago A. Reactions of peroxynitrite with globin proteins and their possible physiological role. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 142 (2005) 124-129
    • (2005) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.142 , pp. 124-129
    • Herold, S.1    Fago, A.2
  • 41
    • 27944466057 scopus 로고    scopus 로고
    • Kinetics and mechanistic studies of the reactions of metleghemoglobin, ferrylleghemoglobin, and nitrosylleghemoglobin with reactive nitrogen species
    • Herold S., and Puppo A. Kinetics and mechanistic studies of the reactions of metleghemoglobin, ferrylleghemoglobin, and nitrosylleghemoglobin with reactive nitrogen species. J. Biol. Inorg. Chem. 10 (2005) 946-957
    • (2005) J. Biol. Inorg. Chem. , vol.10 , pp. 946-957
    • Herold, S.1    Puppo, A.2
  • 42
    • 27944457196 scopus 로고    scopus 로고
    • Oxyleghemoglobin scavenges nitrogen monoxide and peroxynitrite: A possible role in functioning nodules?
    • Herold S., and Puppo A. Oxyleghemoglobin scavenges nitrogen monoxide and peroxynitrite: A possible role in functioning nodules?. J. Biol. Inorg. Chem. 10 (2005) 935-945
    • (2005) J. Biol. Inorg. Chem. , vol.10 , pp. 935-945
    • Herold, S.1    Puppo, A.2
  • 43
    • 0037348406 scopus 로고    scopus 로고
    • The mechanism of the peroxynitrite-mediated oxidation of myoglobin in the absence and presence of carbon dioxide
    • Herold S., Exner M., and Boccini F. The mechanism of the peroxynitrite-mediated oxidation of myoglobin in the absence and presence of carbon dioxide. Chem. Res. Toxicol. 16 (2003) 390-402
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 390-402
    • Herold, S.1    Exner, M.2    Boccini, F.3
  • 44
    • 0035916922 scopus 로고    scopus 로고
    • •-mediated oxidation of oxymyoglobin and oxyhemoglobin
    • •-mediated oxidation of oxymyoglobin and oxyhemoglobin. Biochemistry 40 (2001) 3385-3395
    • (2001) Biochemistry , vol.40 , pp. 3385-3395
    • Herold, S.1    Exner, M.2    Nauser, T.3
  • 45
    • 2542447171 scopus 로고    scopus 로고
    • Reactivity studies of the Fe(III) and Fe(II)NO forms of human neuroglobin reveal a potential role against oxidative stress
    • Herold S., Fago A., Weber R.E., Dewilde S., and Moens L. Reactivity studies of the Fe(III) and Fe(II)NO forms of human neuroglobin reveal a potential role against oxidative stress. J. Biol. Chem. 279 (2004) 22841-22847
    • (2004) J. Biol. Chem. , vol.279 , pp. 22841-22847
    • Herold, S.1    Fago, A.2    Weber, R.E.3    Dewilde, S.4    Moens, L.5
  • 46
    • 0344417899 scopus 로고    scopus 로고
    • Regulation of hmp gene transcription in Mycobacterium tuberculosis: Effects of oxygen limitation and nitrosative and oxidative stress
    • Hu Y., Butcher P.D., Mangan J.A., Rajandream M.A., and Coates A.R. Regulation of hmp gene transcription in Mycobacterium tuberculosis: Effects of oxygen limitation and nitrosative and oxidative stress. J. Bacteriol. 181 (1999) 3486-3493
    • (1999) J. Bacteriol. , vol.181 , pp. 3486-3493
    • Hu, Y.1    Butcher, P.D.2    Mangan, J.A.3    Rajandream, M.A.4    Coates, A.R.5
  • 47
    • 34247340991 scopus 로고    scopus 로고
    • Leprosy and tuberculosis: An insight-review
    • Hussain T. Leprosy and tuberculosis: An insight-review. Crit. Rev. Microbiol. 33 (2007) 15-66
    • (2007) Crit. Rev. Microbiol. , vol.33 , pp. 15-66
    • Hussain, T.1
  • 48
    • 0036912721 scopus 로고    scopus 로고
    • Nitric oxide as a unique signaling molecule in the vascular system: A historical overview
    • Ignarro L.J. Nitric oxide as a unique signaling molecule in the vascular system: A historical overview. J. Physiol. Pharmacol. 53 (2002) 503-514
    • (2002) J. Physiol. Pharmacol. , vol.53 , pp. 503-514
    • Ignarro, L.J.1
  • 49
    • 0029834589 scopus 로고    scopus 로고
    • Syntheses of peroxynitrite: To go with the flow or on solid grounds?
    • Koppenol W.H., Kissner R., and Beckman J.S. Syntheses of peroxynitrite: To go with the flow or on solid grounds?. Methods Enzymol. 269 (1996) 296-302
    • (1996) Methods Enzymol. , vol.269 , pp. 296-302
    • Koppenol, W.H.1    Kissner, R.2    Beckman, J.S.3
  • 50
    • 33745812343 scopus 로고    scopus 로고
    • Oxygen binding and NO scavenging properties of truncated hemoglobin, HbN, of Mycobacterium smegmatis
    • Lama A., Pawaria S., and Dikshit K.L. Oxygen binding and NO scavenging properties of truncated hemoglobin, HbN, of Mycobacterium smegmatis. FEBS Lett. 580 (2006) 4031-4041
    • (2006) FEBS Lett. , vol.580 , pp. 4031-4041
    • Lama, A.1    Pawaria, S.2    Dikshit, K.L.3
  • 51
    • 0031914824 scopus 로고    scopus 로고
    • The role of phagocytic respiratory burst in host defense against Mycobacterium tuberculosis
    • Lau Y.L., Chan G.C.F., Ha S.Y., Hui Y.F., and Yuen K.Y. The role of phagocytic respiratory burst in host defense against Mycobacterium tuberculosis. Clin. Infect. Dis. 26 (1998) 226-227
    • (1998) Clin. Infect. Dis. , vol.26 , pp. 226-227
    • Lau, Y.L.1    Chan, G.C.F.2    Ha, S.Y.3    Hui, Y.F.4    Yuen, K.Y.5
  • 52
    • 1642327485 scopus 로고    scopus 로고
    • Truncated hemoglobin O of Mycobacterium tuberculosis: The oligomeric state change and the interaction with membrane components
    • Liu C., He Y., and Chang Z. Truncated hemoglobin O of Mycobacterium tuberculosis: The oligomeric state change and the interaction with membrane components. Biochem. Biophys. Res. Commun. 316 (2004) 1163-1172
    • (2004) Biochem. Biophys. Res. Commun. , vol.316 , pp. 1163-1172
    • Liu, C.1    He, Y.2    Chang, Z.3
  • 56
    • 0038624089 scopus 로고    scopus 로고
    • A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O
    • Milani M., Savard P.Y., Ouellet H., Ascenzi P., Guertin M., and Bolognesi M. 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 (2003) 5766-5771
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5766-5771
    • Milani, M.1    Savard, P.Y.2    Ouellet, H.3    Ascenzi, P.4    Guertin, M.5    Bolognesi, M.6
  • 60
    • 0035831479 scopus 로고    scopus 로고
    • Flavohemoglobin, a globin with a peroxidase-like catalytic site
    • Mukai M., Mills C.E., Poole R.K., and Yeh S.R. Flavohemoglobin, a globin with a peroxidase-like catalytic site. J. Biol. Chem. 276 (2001) 7272-7277
    • (2001) J. Biol. Chem. , vol.276 , pp. 7272-7277
    • Mukai, M.1    Mills, C.E.2    Poole, R.K.3    Yeh, S.R.4
  • 61
    • 1542297723 scopus 로고    scopus 로고
    • NO binding induced conformational changes in a truncated hemoglobin from Mycobacterium tuberculosis
    • Mukai M., Ouellet Y., Ouellet H., Guertin M., and Yeh S.R. NO binding induced conformational changes in a truncated hemoglobin from Mycobacterium tuberculosis. Biochemistry 43 (2004) 2764-2770
    • (2004) Biochemistry , vol.43 , pp. 2764-2770
    • Mukai, M.1    Ouellet, Y.2    Ouellet, H.3    Guertin, M.4    Yeh, S.R.5
  • 62
    • 0037177162 scopus 로고    scopus 로고
    • Unique ligand-protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis
    • Mukai M., Savard P.Y., Ouellet H., Guertin M., and Yeh S.R. Unique ligand-protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis. Biochemistry 41 (2002) 3897-3905
    • (2002) Biochemistry , vol.41 , pp. 3897-3905
    • Mukai, M.1    Savard, P.Y.2    Ouellet, H.3    Guertin, M.4    Yeh, S.R.5
  • 63
    • 0034255209 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens
    • Nathan C., and Shiloh M.U. Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens. Proc. Natl. Acad. Sci. USA 97 (2000) 8841-8848
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8841-8848
    • Nathan, C.1    Shiloh, M.U.2
  • 64
    • 0041827138 scopus 로고    scopus 로고
    • The effects of reactive nitrogen intermediates on gene expression in Mycobacterium tuberculosis
    • Ohno H., Zhu G., Mohan V.P., Chu D., Kohno S., Jacobs Jr. W.R., and Chan J. The effects of reactive nitrogen intermediates on gene expression in Mycobacterium tuberculosis. Cell Microbiol. 5 (2003) 637-648
    • (2003) Cell Microbiol. , vol.5 , pp. 637-648
    • Ohno, H.1    Zhu, G.2    Mohan, V.P.3    Chu, D.4    Kohno, S.5    Jacobs Jr., W.R.6    Chan, J.7
  • 66
    • 34147154024 scopus 로고    scopus 로고
    • Reaction of Mycobacterium tuberculosis truncated hemoglobin O with hydrogen peroxide: Evidence for peroxidatic activity and formation of protein-based radicals
    • in press
    • Ouellet H., Ranguelova K., Labarre M., Wittenberg J.B., Wittenberg B.A., Magliozzo R.S., and Guertin M. Reaction of Mycobacterium tuberculosis truncated hemoglobin O with hydrogen peroxide: Evidence for peroxidatic activity and formation of protein-based radicals. J. Biol. Chem. (2007) in press
    • (2007) J. Biol. Chem.
    • Ouellet, H.1    Ranguelova, K.2    Labarre, M.3    Wittenberg, J.B.4    Wittenberg, B.A.5    Magliozzo, R.S.6    Guertin, M.7
  • 68
    • 33746224034 scopus 로고    scopus 로고
    • Ligand interactions in the distal heme pocket of Mycobacterium tuberculosis truncated hemoglobin N: Roles of TyrB10 and GlnE11 residues
    • Ouellet Y., Milani M., Couture M., Bolognesi M., and Guertin M. Ligand interactions in the distal heme pocket of Mycobacterium tuberculosis truncated hemoglobin N: Roles of TyrB10 and GlnE11 residues. Biochemistry 45 (2006) 8770-8781
    • (2006) Biochemistry , vol.45 , pp. 8770-8781
    • Ouellet, Y.1    Milani, M.2    Couture, M.3    Bolognesi, M.4    Guertin, M.5
  • 69
    • 0037013274 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis hemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli
    • Pathania R., Navani N.K., Rajamohan G., and Dikshit K.L. Mycobacterium tuberculosis hemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli. J. Biol. Chem. 277 (2002) 15293-15302
    • (2002) J. Biol. Chem. , vol.277 , pp. 15293-15302
    • Pathania, R.1    Navani, N.K.2    Rajamohan, G.3    Dikshit, K.L.4
  • 70
    • 0036049852 scopus 로고    scopus 로고
    • Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli
    • 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
    • (2002) Mol. Microbiol. , vol.45 , pp. 1303-1314
    • Pathania, R.1    Navani, N.K.2    Gardner, A.M.3    Gardner, P.R.4    Dikshit, K.L.5
  • 71
    • 14644387541 scopus 로고    scopus 로고
    • Nitric oxide and nitrosative stress tolerance in bacteria
    • Poole R.K. Nitric oxide and nitrosative stress tolerance in bacteria. Biochem. Soc. Trans. 33 (2005) 176-180
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 176-180
    • Poole, R.K.1
  • 73
    • 1542287658 scopus 로고    scopus 로고
    • The absence of proximal strain in the truncated hemoglobins from Mycobacterium tuberculosis
    • 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
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2682-2683
    • Samuni, U.1    Ouellet, Y.2    Guertin, M.3    Friedman, J.M.4    Yeh, S.R.5
  • 74
    • 33646137117 scopus 로고    scopus 로고
    • Expression profiling of host pathogen interactions: How Mycobacterium tuberculosis and the macrophage adapt to one another
    • Schnappinger D., Schoolnik G.K., and Ehrt S. Expression profiling of host pathogen interactions: How Mycobacterium tuberculosis and the macrophage adapt to one another. Microbes Infect. 8 (2006) 1132-1140
    • (2006) Microbes Infect. , vol.8 , pp. 1132-1140
    • Schnappinger, D.1    Schoolnik, G.K.2    Ehrt, S.3
  • 81
    • 33646341657 scopus 로고    scopus 로고
    • A phylogenetic and structural analysis of truncated hemoglobins
    • Vuletich D.A., and Lecomte J.T. A phylogenetic and structural analysis of truncated hemoglobins. J. Mol. Evol. 62 (2006) 196-210
    • (2006) J. Mol. Evol. , vol.62 , pp. 196-210
    • Vuletich, D.A.1    Lecomte, J.T.2
  • 82
    • 0037059826 scopus 로고    scopus 로고
    • Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants
    • 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 (2002) 871-874
    • (2002) J. Biol. Chem. , vol.277 , pp. 871-874
    • Wittenberg, J.B.1    Bolognesi, M.2    Wittenberg, B.A.3    Guertin, M.4
  • 84
    • 0034695445 scopus 로고    scopus 로고
    • A cooperative oxygen binding hemoglobin from Mycobacterium tuberculosis: Stabilization of heme ligands by a distal tyrosine residue
    • 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
    • (2000) J. Biol. Chem. , vol.275 , pp. 1679-1684
    • Yeh, S.R.1    Couture, M.2    Ouellet, Y.3    Guertin, M.4    Rousseau, D.L.5
  • 85
    • 0036200214 scopus 로고    scopus 로고
    • Reactive nitrogen and oxygen intermediates and bacterial defenses: Unusual adaptation in Mycobacterium tuberculosis
    • Zahrt T.C., and Deretic V. Reactive nitrogen and oxygen intermediates and bacterial defenses: Unusual adaptation in Mycobacterium tuberculosis. Antioxid. Redox Signal. 4 (2002) 141-159
    • (2002) Antioxid. Redox Signal. , vol.4 , pp. 141-159
    • Zahrt, T.C.1    Deretic, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.