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Volumn 48, Issue 5, 2009, Pages 863-872

Reaction of Mycobacterium tuberculosis Cytochrome P450 enzymes with nitric oxide

Author keywords

[No Author keywords available]

Indexed keywords

ANAEROBIC REDUCTIONS; CYTOCHROME OXIDASE; CYTOCHROME P-450; HEME PROTEINS; INHIBITORY EFFECTS; MYCOBACTERIUM TUBERCULOSIS; N-O COMPLEXES; PHYSIOLOGICAL CONCENTRATIONS; RESONANCE RAMAN; SODIUM DITHIONITE; STOPPED FLOWS; UV-VISIBLE ABSORPTIONS;

EID: 61449218869     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801595t     Document Type: Article
Times cited : (40)

References (53)
  • 2
    • 0035185373 scopus 로고    scopus 로고
    • What is the role of nitric oxide in murine and human host defense against tuberculosis? Current knowledge
    • Chan, E. D., Chan, J., and Schluger, N. W. (2001) What is the role of nitric oxide in murine and human host defense against tuberculosis? Current knowledge. Am. J. Respir. Cell Mol. Biol. 25, 606-612.
    • (2001) Am. J. Respir. Cell Mol. Biol , vol.25 , pp. 606-612
    • Chan, E.D.1    Chan, J.2    Schluger, N.W.3
  • 3
    • 0041402773 scopus 로고    scopus 로고
    • Immune evasion by Mycobacterium tuberculosis: Living with the enemy
    • Flynn, J. L., and Chan, J. (2003) Immune evasion by Mycobacterium tuberculosis: living with the enemy. Curr. Opin. Immunol. 15, 450-455.
    • (2003) Curr. Opin. Immunol , vol.15 , pp. 450-455
    • Flynn, J.L.1    Chan, J.2
  • 4
    • 0033033929 scopus 로고    scopus 로고
    • Mycobacteriocidal action of exogenous nitric oxide
    • Long, R., Light, B., and Talbot, J. A. (1999) Mycobacteriocidal action of exogenous nitric oxide. Antimicrob. Agents Chemother. 43, 403-405.
    • (1999) Antimicrob. Agents Chemother , vol.43 , pp. 403-405
    • Long, R.1    Light, B.2    Talbot, J.A.3
  • 6
    • 0035146934 scopus 로고    scopus 로고
    • Nitric oxide, cytochrome-c oxidase and myoglobin
    • Brunori, M. (2001) Nitric oxide, cytochrome-c oxidase and myoglobin. Trends Biochem. Sci. 26, 21-23.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 21-23
    • Brunori, M.1
  • 7
    • 0031023654 scopus 로고    scopus 로고
    • Metabolic fate of peroxynitrite in aqueous solution. Reaction with nitric oxide and pH-dependent decomposition to nitrite and oxygen in a 2:1 stoichiometry
    • Pfeiffer, S., Gorren, A. C., Schmidt, K., Werner, E. R., Hansert, B., Bohle, D. S., and Mayer, B. (1997) Metabolic fate of peroxynitrite in aqueous solution. Reaction with nitric oxide and pH-dependent decomposition to nitrite and oxygen in a 2:1 stoichiometry. J. Biol. Chem. 272, 3465-3470.
    • (1997) J. Biol. Chem , vol.272 , pp. 3465-3470
    • Pfeiffer, S.1    Gorren, A.C.2    Schmidt, K.3    Werner, E.R.4    Hansert, B.5    Bohle, D.S.6    Mayer, B.7
  • 8
    • 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. (2000) Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens. Proc. Natl. Acad. Sci. U.S.A. 97, 8841-8848.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 8841-8848
    • Nathan, C.1    Shiloh, M.U.2
  • 9
    • 0032054683 scopus 로고    scopus 로고
    • The role of nitric oxide in hepatic metabolism
    • Alexander, B. (1998) The role of nitric oxide in hepatic metabolism. Nutrition 14, 376-390.
    • (1998) Nutrition , vol.14 , pp. 376-390
    • Alexander, B.1
  • 10
    • 0031007899 scopus 로고    scopus 로고
    • Nitric oxide-mediated inhibition of cytochrome P450 by interferon-gamma in human hepatocytes
    • Donato, M. T., Guillen, M. I., Jover, R., Castell, J. V., and Gomez-Lechon, M. J. (1997) Nitric oxide-mediated inhibition of cytochrome P450 by interferon-gamma in human hepatocytes. J. Pharmacol. Exp. Ther. 281, 484-490.
    • (1997) J. Pharmacol. Exp. Ther , vol.281 , pp. 484-490
    • Donato, M.T.1    Guillen, M.I.2    Jover, R.3    Castell, J.V.4    Gomez-Lechon, M.J.5
  • 11
    • 0032508046 scopus 로고    scopus 로고
    • Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., III, 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., Rutter, S., Seeger, K., Skelton, J., Squares, R., Squares, S., Sulston, J. E., Taylor, K., Whitehead, S., and Barrell, B. G (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393, 537-544.
    • Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., III, 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., Rutter, S., Seeger, K., Skelton, J., Squares, R., Squares, S., Sulston, J. E., Taylor, K., Whitehead, S., and Barrell, B. G (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393, 537-544.
  • 12
    • 47649089787 scopus 로고    scopus 로고
    • Structural biology and biochemistry of cytochrome P450 systems in Mycobacterium tuberculosis
    • McLean, K. J., and Munro, A. W. (2008) Structural biology and biochemistry of cytochrome P450 systems in Mycobacterium tuberculosis. Drug Metab. Rev. 40, 427-446.
    • (2008) Drug Metab. Rev , vol.40 , pp. 427-446
    • McLean, K.J.1    Munro, A.W.2
  • 13
    • 0033529797 scopus 로고    scopus 로고
    • Characterization and catalytic properties of the sterol 14alpha-demethylase from Mycobacterium tuberculosis
    • Bellamine, A., Mangla, A. T., Nes, W. D., and Waterman, M. R. (1999) Characterization and catalytic properties of the sterol 14alpha-demethylase from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U.S.A. 96, 8937-8942.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 8937-8942
    • Bellamine, A.1    Mangla, A.T.2    Nes, W.D.3    Waterman, M.R.4
  • 15
    • 34447554847 scopus 로고    scopus 로고
    • Identification of mycobacterial genes that alter growth and pathology in macrophages and in mice
    • Chang, J. C., Harik, N. S., Liao, R. P., and Sherman, D. R. (2007) Identification of mycobacterial genes that alter growth and pathology in macrophages and in mice. J. Infect. Dis. 196, 788-795.
    • (2007) J. Infect. Dis , vol.196 , pp. 788-795
    • Chang, J.C.1    Harik, N.S.2    Liao, R.P.3    Sherman, D.R.4
  • 16
    • 20444419421 scopus 로고    scopus 로고
    • Genomewide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages
    • Rengarajan, J., Bloom, B. R., and Rubin, E. J. (2005) Genomewide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages. Proc. Natl. Acad. Sci. U.S.A. 102, 8327-8332.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 8327-8332
    • Rengarajan, J.1    Bloom, B.R.2    Rubin, E.J.3
  • 17
    • 0038136970 scopus 로고    scopus 로고
    • Atomic structure of Mycobacterium tuberculosis CYP121 to 1.06 A reveals novel features of cytochrome P450
    • Leys, D., Mowat, C. G., McLean, K. J., Richmond, A., Chapman, S. K., Walkinshaw, M. D., and Munro, A. W. (2003) Atomic structure of Mycobacterium tuberculosis CYP121 to 1.06 A reveals novel features of cytochrome P450. J. Biol. Chem. 278, 5141-5147.
    • (2003) J. Biol. Chem , vol.278 , pp. 5141-5147
    • Leys, D.1    Mowat, C.G.2    McLean, K.J.3    Richmond, A.4    Chapman, S.K.5    Walkinshaw, M.D.6    Munro, A.W.7
  • 18
    • 41949110521 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis CYP130: Crystal structure, biophysical characterization, and interactions with antifungal azole drugs
    • Ouellet, H., Podust, L. M., and de Montellano, P. R. (2008) Mycobacterium tuberculosis CYP130: crystal structure, biophysical characterization, and interactions with antifungal azole drugs. J. Biol. Chem. 283, 5069-5080.
    • (2008) J. Biol. Chem , vol.283 , pp. 5069-5080
    • Ouellet, H.1    Podust, L.M.2    de Montellano, P.R.3
  • 19
    • 33846015513 scopus 로고    scopus 로고
    • Crystal structure of the Mycobacterium tuberculosis P450 CYP121-fluconazole complex reveals new azole drug-P450 binding mode
    • Seward, H. E., Roujeinikova, A., McLean, K. J., Munro, A. W., and Leys, D. (2006) Crystal structure of the Mycobacterium tuberculosis P450 CYP121-fluconazole complex reveals new azole drug-P450 binding mode. J. Biol. Chem. 281, 39437-39443.
    • (2006) J. Biol. Chem , vol.281 , pp. 39437-39443
    • Seward, H.E.1    Roujeinikova, A.2    McLean, K.J.3    Munro, A.W.4    Leys, D.5
  • 20
    • 0035853108 scopus 로고    scopus 로고
    • Crystal structure of cytochrome P450 14alpha-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors
    • Podust, L. M., Poulos, T. L., and Waterman, M. R. (2001) Crystal structure of cytochrome P450 14alpha-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors. Proc. Natl. Acad. Sci. U.S.A. 98, 3068-3073.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 3068-3073
    • Podust, L.M.1    Poulos, T.L.2    Waterman, M.R.3
  • 21
    • 0026023551 scopus 로고
    • Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA
    • Gegner, J. A., and Dahlquist, F. W. (1991) Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA. Proc. Natl. Acad. Sci. U.S.A. 88, 750-754.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 750-754
    • Gegner, J.A.1    Dahlquist, F.W.2
  • 22
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura, T., and Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J. Biol. Chem. 239, 2370-2378.
    • (1964) J. Biol. Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 23
    • 4444342093 scopus 로고    scopus 로고
    • Stability of the heme environment of the nitric oxide synthase from Staphylococcus aureus in the absence of pterin cofactor
    • Chartier, F. J., and Couture, M. 2004) Stability of the heme environment of the nitric oxide synthase from Staphylococcus aureus in the absence of pterin cofactor. Biophys. J. 87, 1939-1950.
    • (2004) Biophys. J , vol.87 , pp. 1939-1950
    • Chartier, F.J.1    Couture, M.2
  • 24
  • 25
    • 0035851202 scopus 로고    scopus 로고
    • Regulation of the properties of the heme-NO complexes in nitric-oxide synthase by hydrogen bonding to the proximal cysteine
    • Couture, M., Adak, S., Stuehr, D. J., and Rousseau, D. L. (2001) Regulation of the properties of the heme-NO complexes in nitric-oxide synthase by hydrogen bonding to the proximal cysteine. J. Biol. Chem. 276, 38280-38288.
    • (2001) J. Biol. Chem , vol.276 , pp. 38280-38288
    • Couture, M.1    Adak, S.2    Stuehr, D.J.3    Rousseau, D.L.4
  • 26
    • 0021762910 scopus 로고
    • Electronic spectra for nitrosyl(protoporphyrin IX dimethyl ester)iron(II) and its complexes with nitrogenous bases as model systems for nitrosylhemoproteins
    • Yoshimura, T., and Ozaki, T. (1984) Electronic spectra for nitrosyl(protoporphyrin IX dimethyl ester)iron(II) and its complexes with nitrogenous bases as model systems for nitrosylhemoproteins. Arch. Biochem. Biophys. 229, 126-135.
    • (1984) Arch. Biochem. Biophys , vol.229 , pp. 126-135
    • Yoshimura, T.1    Ozaki, T.2
  • 27
    • 0029664621 scopus 로고    scopus 로고
    • Conserved Glu318 at the cytochrome P450 1A2 distal site is crucial in the nitric oxide complex stability
    • Nakano, R., Sato, H., Watanabe, A., Ito, O., and Shimizu, T. (1996) Conserved Glu318 at the cytochrome P450 1A2 distal site is crucial in the nitric oxide complex stability. J. Biol. Chem. 271, 8570-8574.
    • (1996) J. Biol. Chem , vol.271 , pp. 8570-8574
    • Nakano, R.1    Sato, H.2    Watanabe, A.3    Ito, O.4    Shimizu, T.5
  • 28
    • 0030942247 scopus 로고    scopus 로고
    • Characterization of ferrous FixL-nitric oxide adducts by resonance Raman spectroscopy
    • Lukat-Rodgers, G. S., and Rodgers, K. R. (1997) Characterization of ferrous FixL-nitric oxide adducts by resonance Raman spectroscopy. Biochemistry 36, 4178-4187.
    • (1997) Biochemistry , vol.36 , pp. 4178-4187
    • Lukat-Rodgers, G.S.1    Rodgers, K.R.2
  • 29
    • 0035965286 scopus 로고    scopus 로고
    • The heme environment of mouse neuroglobin. Evidence for the presence of two conformations of the heme pocket
    • Couture, M., Burmester, T., Hankeln, T., and Rousseau, D. L. (2001) The heme environment of mouse neuroglobin. Evidence for the presence of two conformations of the heme pocket. J. Biol. Chem. 276, 36377-36382.
    • (2001) J. Biol. Chem , vol.276 , pp. 36377-36382
    • Couture, M.1    Burmester, T.2    Hankeln, T.3    Rousseau, D.L.4
  • 30
    • 0033550059 scopus 로고    scopus 로고
    • Resonance Raman studies of cytochrome P450BM3 and its complexes with exogenous ligands
    • Deng, T. J., Proniewicz, L. M., Kincaid, J. R., Yeom, H., Macdonald, I. D., and Sligar, S. G. (1999) Resonance Raman studies of cytochrome P450BM3 and its complexes with exogenous ligands. Biochemistry 38, 13699-13706.
    • (1999) Biochemistry , vol.38 , pp. 13699-13706
    • Deng, T.J.1    Proniewicz, L.M.2    Kincaid, J.R.3    Yeom, H.4    Macdonald, I.D.5    Sligar, S.G.6
  • 31
    • 0000506287 scopus 로고
    • Resonance Raman spectra of the nitric oxide adducts of ferrous cytochrome P450cam in the presence of various substrates
    • Hu, S., and Kincaid, J. R. (1991) Resonance Raman spectra of the nitric oxide adducts of ferrous cytochrome P450cam in the presence of various substrates. J. Am. Chem. Soc. 113, 9760-9766.
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 9760-9766
    • Hu, S.1    Kincaid, J.R.2
  • 32
    • 0037418534 scopus 로고    scopus 로고
    • Spectroscopic characterization of five-and six-coordinate ferrous-NO heme complexes. Evidence for heme Fe-proximal cysteinate bond cleavage in the ferrous-NO adducts of the Trp-409Tyr/Phe proximal environment mutants of neuronal nitric oxide synthase
    • Voegtle, H. L., Sono, M., Adak, S., Pond, A. E., Tomita, T., Perera, R., Goodin, D. B., Ikeda-Saito, M., Stuehr, D. J., and Dawson, J. H. (2003) Spectroscopic characterization of five-and six-coordinate ferrous-NO heme complexes. Evidence for heme Fe-proximal cysteinate bond cleavage in the ferrous-NO adducts of the Trp-409Tyr/Phe proximal environment mutants of neuronal nitric oxide synthase. Biochemistry 42, 2475-2484.
    • (2003) Biochemistry , vol.42 , pp. 2475-2484
    • Voegtle, H.L.1    Sono, M.2    Adak, S.3    Pond, A.E.4    Tomita, T.5    Perera, R.6    Goodin, D.B.7    Ikeda-Saito, M.8    Stuehr, D.J.9    Dawson, J.H.10
  • 33
    • 41949097208 scopus 로고    scopus 로고
    • Nitrate enhances the survival of Mycobacterium tuberculosis during inhibition of respiration
    • Sohaskey, C. D. (2008) Nitrate enhances the survival of Mycobacterium tuberculosis during inhibition of respiration. J. Bacteriol. 190, 2981-2986.
    • (2008) J. Bacteriol , vol.190 , pp. 2981-2986
    • Sohaskey, C.D.1
  • 36
    • 0028807047 scopus 로고
    • Kinetic analysis of the fate of nitric oxide synthesized by macrophages in vitro
    • Lewis, R. S., Tamir, S., Tannenbaum, S. R., and Deen, W. M. (1995) Kinetic analysis of the fate of nitric oxide synthesized by macrophages in vitro. J. Biol. Chem. 270, 29350-29355.
    • (1995) J. Biol. Chem , vol.270 , pp. 29350-29355
    • Lewis, R.S.1    Tamir, S.2    Tannenbaum, S.R.3    Deen, W.M.4
  • 37
    • 1842450583 scopus 로고    scopus 로고
    • Substrate binding favors enhanced NO binding to P450cam
    • Franke, A., Stochel, G., Jung, C., and Van Eldik, R. (2004) Substrate binding favors enhanced NO binding to P450cam. J. Am. Chem. Soc. 126, 4181-4191.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 4181-4191
    • Franke, A.1    Stochel, G.2    Jung, C.3    Van Eldik, R.4
  • 38
    • 0036314910 scopus 로고    scopus 로고
    • Substrates modulate the rate-determining step for CO binding in cytochrome P450cam (CYP101). A high-pressure stopped-flow study
    • Jung, C., Bec, N., and Lange, R. (2002) Substrates modulate the rate-determining step for CO binding in cytochrome P450cam (CYP101). A high-pressure stopped-flow study. Eur. J. Biochem. 269, 2989-2996.
    • (2002) Eur. J. Biochem , vol.269 , pp. 2989-2996
    • Jung, C.1    Bec, N.2    Lange, R.3
  • 39
    • 34047158165 scopus 로고    scopus 로고
    • Visible spectra of type II cytochrome P450-drug complexes: Evidence that "incomplete" heme coordination is common
    • Locuson, C. W., Hutzler, J. M., and Tracy, T. S. (2007) Visible spectra of type II cytochrome P450-drug complexes: evidence that "incomplete" heme coordination is common. Drug Metab. Dispos. 35, 614-622.
    • (2007) Drug Metab. Dispos , vol.35 , pp. 614-622
    • Locuson, C.W.1    Hutzler, J.M.2    Tracy, T.S.3
  • 41
    • 1942469554 scopus 로고    scopus 로고
    • Activation of heme-regulated eukaryotic initiation factor 2alpha kinase by nitric oxide is induced by the formation of a five-coordinate NO-heme complex: Optical absorption, electron spin resonance, and resonance Raman spectral studies
    • Igarashi, J., Sato, A., Kitagawa, T., Yoshimura, T., Yamauchi, S., Sagami, I., and Shimizu, T. (2004) Activation of heme-regulated eukaryotic initiation factor 2alpha kinase by nitric oxide is induced by the formation of a five-coordinate NO-heme complex: optical absorption, electron spin resonance, and resonance Raman spectral studies. J. Biol. Chem. 279, 15752-15762.
    • (2004) J. Biol. Chem , vol.279 , pp. 15752-15762
    • Igarashi, J.1    Sato, A.2    Kitagawa, T.3    Yoshimura, T.4    Yamauchi, S.5    Sagami, I.6    Shimizu, T.7
  • 42
    • 0034681189 scopus 로고    scopus 로고
    • Electronic absorption, EPR, and resonance Raman spectroscopy of CooA, a CO-sensing transcription activator from R. rubrum, reveals a five-coordinate NO-heme
    • Reynolds, M. F., Parks, R. B., Burstyn, J. N., Shelver, D., Thorsteinsson, M. V., Kerby, R. L., Roberts, G P., Vogel, K M., and Spiro, T. G. (2000) Electronic absorption, EPR, and resonance Raman spectroscopy of CooA, a CO-sensing transcription activator from R. rubrum, reveals a five-coordinate NO-heme. Biochemistry 39, 388-396.
    • (2000) Biochemistry , vol.39 , pp. 388-396
    • Reynolds, M.F.1    Parks, R.B.2    Burstyn, J.N.3    Shelver, D.4    Thorsteinsson, M.V.5    Kerby, R.L.6    Roberts, G.P.7    Vogel, K.M.8    Spiro, T.G.9
  • 44
    • 0032571411 scopus 로고    scopus 로고
    • Structure of nitric oxide synthase oxygenase dimer with pterin and substrate
    • Crane, B. R., Arvai, A. S., Ghosh, D. K., Wu, C., Getzoff, E. D., Stuehr, D. J., and Tainer, J. A. (1998) Structure of nitric oxide synthase oxygenase dimer with pterin and substrate. Science 279, 2121-2126.
    • (1998) Science , vol.279 , pp. 2121-2126
    • Crane, B.R.1    Arvai, A.S.2    Ghosh, D.K.3    Wu, C.4    Getzoff, E.D.5    Stuehr, D.J.6    Tainer, J.A.7
  • 45
    • 0033578713 scopus 로고    scopus 로고
    • Tryptophan 409 controls the activity of neuronal nitric-oxide synthase by regulating nitric oxide feedback inhibition
    • Adak, S., Crooks, C., Wang, Q., Crane, B. R., Tainer, J. A., Getzoff, E. D., and Stuehr, D. J. (1999) Tryptophan 409 controls the activity of neuronal nitric-oxide synthase by regulating nitric oxide feedback inhibition. J. Biol. Chem. 274, 26907-26911.
    • (1999) J. Biol. Chem , vol.274 , pp. 26907-26911
    • Adak, S.1    Crooks, C.2    Wang, Q.3    Crane, B.R.4    Tainer, J.A.5    Getzoff, E.D.6    Stuehr, D.J.7
  • 46
    • 0034625417 scopus 로고    scopus 로고
    • Molecular basis for hyperactivity in tryptophan 409 mutants of neuronal NO synthase
    • Adak, S., Wang, Q., and Stuehr, D. J. (2000) Molecular basis for hyperactivity in tryptophan 409 mutants of neuronal NO synthase. J. Biol. Chem. 275, 17434-17439.
    • (2000) J. Biol. Chem , vol.275 , pp. 17434-17439
    • Adak, S.1    Wang, Q.2    Stuehr, D.J.3
  • 47
    • 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. (1997) Comparison of the roles of reactive oxygen and nitrogen intermediates in the host response to Mycobacterium tuberculosis using transgenic mice. Tuberc. Lung Dis. 78, 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
  • 49
    • 15844380037 scopus 로고    scopus 로고
    • Nicholson, S., Bonecini-Almeida Mda, G., Lapa e Silva, J. R., Nathan, C., Xie, Q. W., Mumford, R., Weidner, J. R., Calaycay, J., Geng, J., Boechat, N., Linhares, C., Rom, W., and Ho, J. L. (1996) Inducible nitric oxide synthase in pulmonary alveolar macrophages from patients with tuberculosis. J. Exp. Med. 183, 2293-2302.
    • Nicholson, S., Bonecini-Almeida Mda, G., Lapa e Silva, J. R., Nathan, C., Xie, Q. W., Mumford, R., Weidner, J. R., Calaycay, J., Geng, J., Boechat, N., Linhares, C., Rom, W., and Ho, J. L. (1996) Inducible nitric oxide synthase in pulmonary alveolar macrophages from patients with tuberculosis. J. Exp. Med. 183, 2293-2302.
  • 51
    • 0028963395 scopus 로고
    • Spectroscopic and kinetic studies on reaction of cytochrome P450nor with nitric oxide. Implication for its nitric oxide reduction mechanism
    • Shiro, Y., Fujii, M., Iizuka, T., Adachi, S., Tsukamoto, K., Nakahara, K., and Shoun, H. (1995) Spectroscopic and kinetic studies on reaction of cytochrome P450nor with nitric oxide. Implication for its nitric oxide reduction mechanism. J. Biol. Chem. 270, 1617-1623.
    • (1995) J. Biol. Chem , vol.270 , pp. 1617-1623
    • Shiro, Y.1    Fujii, M.2    Iizuka, T.3    Adachi, S.4    Tsukamoto, K.5    Nakahara, K.6    Shoun, H.7
  • 53
    • 0032539974 scopus 로고    scopus 로고
    • Stopped-flow analysis of CO and NO binding to inducible nitric oxide synthase
    • Abu-Soud, H. M., Wu, C., Ghosh, D. K., and Stuehr, D. J. (1998) Stopped-flow analysis of CO and NO binding to inducible nitric oxide synthase. Biochemistry 37, 3777-3786.
    • (1998) Biochemistry , vol.37 , pp. 3777-3786
    • Abu-Soud, H.M.1    Wu, C.2    Ghosh, D.K.3    Stuehr, D.J.4


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