메뉴 건너뛰기




Volumn 50, Issue 6, 2011, Pages 1023-1028

Nitric oxide dioxygenation reaction in devS and the initial response to nitric oxide in mycobacterium tuberculosis

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; NITRIC OXIDE; PLANTS (BOTANY); PORPHYRINS; ULTRAVIOLET VISIBLE SPECTROSCOPY;

EID: 79851486240     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1015315     Document Type: Article
Times cited : (21)

References (28)
  • 1
    • 0037099165 scopus 로고    scopus 로고
    • Analysis of nitric oxide synthase and nitrotyrosine expression in human pulmonary tuberculosis
    • Choi, H. S., Rai, P. R., Chu, H. W., Cool, C., and Chan, E. D. (2002) Analysis of nitric oxide synthase and nitrotyrosine expression in human pulmonary tuberculosis Am. J. Respir. Crit. Care Med. 166, 178-186
    • (2002) Am. J. Respir. Crit. Care Med. , vol.166 , pp. 178
    • Choi, H.S.1    Rai, P.R.2    Chu, H.W.3    Cool, C.4    Chan, E.D.5
  • 2
    • 0034780485 scopus 로고    scopus 로고
    • Nonreplicating persistence of Mycobacterium tuberculosis
    • Wayne, L. G. and Sohaskey, C. D. (2001) Nonreplicating persistence of Mycobacterium tuberculosis Annu. Rev. Microbiol. 55, 139-163
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 139
    • Wayne, L.G.1    Sohaskey, C.D.2
  • 3
    • 0031930142 scopus 로고    scopus 로고
    • Mycobacterial stationary phase induced by low oxygen tension: Cell wall thickening and localization of the 16-kilodalton α-crystallin homolog
    • Cunningham, A. F. and Spreadbury, C. L. (1998) Mycobacterial stationary phase induced by low oxygen tension: Cell wall thickening and localization of the 16-kilodalton α-crystallin homolog J. Bacteriol. 180, 801-808
    • (1998) J. Bacteriol. , vol.180 , pp. 801
    • Cunningham, A.F.1    Spreadbury, C.L.2
  • 7
    • 2542475060 scopus 로고    scopus 로고
    • Two sensor kinases contribute to the hypoxic response of Mycobacterium tuberculosis
    • Roberts, D. M., Liao, R. P., Wisedchaisri, G., Hol, W. G., and Sherman, D. R. (2004) Two sensor kinases contribute to the hypoxic response of Mycobacterium tuberculosis J. Biol. Chem. 279, 23082-23087
    • (2004) J. Biol. Chem. , vol.279 , pp. 23082
    • Roberts, D.M.1    Liao, R.P.2    Wisedchaisri, G.3    Hol, W.G.4    Sherman, D.R.5
  • 9
    • 34547568747 scopus 로고    scopus 로고
    • DosT and DevS are oxygen-switched kinases in Mycobacterium tuberculosis
    • Sousa, E. H., Tuckerman, J. R., Gonzalez, G., and Gilles-Gonzalez, M. A. (2007) DosT and DevS are oxygen-switched kinases in Mycobacterium tuberculosis Protein Sci. 16, 1708-1719
    • (2007) Protein Sci. , vol.16 , pp. 1708
    • Sousa, E.H.1    Tuckerman, J.R.2    Gonzalez, G.3    Gilles-Gonzalez, M.A.4
  • 10
    • 56749146042 scopus 로고    scopus 로고
    • A distal tyrosine residue is required for ligand discrimination in DevS from Mycobacterium tuberculosis
    • Yukl, E. T., Ioanoviciu, A., Nakano, M. M., de Montellano, P. R., and MoeÌ̂nne-Loccoz, P. (2008) A distal tyrosine residue is required for ligand discrimination in DevS from Mycobacterium tuberculosis Biochemistry 47, 12532-12539
    • (2008) Biochemistry , vol.47 , pp. 12532
    • Yukl, E.T.1    Ioanoviciu, A.2    Nakano, M.M.3    De Montellano, P.R.4    Moeì̂nne-Loccoz, P.5
  • 11
    • 67651202584 scopus 로고    scopus 로고
    • Unique roles of DosT and DosS in DosR regulon induction and Mycobacterium tuberculosis dormancy
    • Honaker, R. W., Leistikow, R. L., Bartek, I. L., and Voskuil, M. I. (2009) Unique roles of DosT and DosS in DosR regulon induction and Mycobacterium tuberculosis dormancy Infect. Immun. 77, 3258-3263
    • (2009) Infect. Immun. , vol.77 , pp. 3258
    • Honaker, R.W.1    Leistikow, R.L.2    Bartek, I.L.3    Voskuil, M.I.4
  • 12
    • 67649586805 scopus 로고    scopus 로고
    • Structural insight into the heme-based redox sensing by DosS from Mycobacterium tuberculosis
    • Cho, H. Y., Cho, H. J., Kim, Y. M., Oh, J. I., and Kang, B. S. (2009) Structural insight into the heme-based redox sensing by DosS from Mycobacterium tuberculosis J. Biol. Chem. 284, 13057-13067
    • (2009) J. Biol. Chem. , vol.284 , pp. 13057
    • Cho, H.Y.1    Cho, H.J.2    Kim, Y.M.3    Oh, J.I.4    Kang, B.S.5
  • 13
    • 67649631300 scopus 로고    scopus 로고
    • DevS oxy complex stability identifies this heme protein as a gas sensor in Mycobacterium tuberculosis dormancy
    • Ioanoviciu, A., Meharenna, Y. T., Poulos, T. L., and Ortiz de Montellano, P. R. (2009) DevS oxy complex stability identifies this heme protein as a gas sensor in Mycobacterium tuberculosis dormancy Biochemistry 48, 5839-5848
    • (2009) Biochemistry , vol.48 , pp. 5839
    • Ioanoviciu, A.1    Meharenna, Y.T.2    Poulos, T.L.3    Ortiz De Montellano, P.R.4
  • 14
    • 2342661639 scopus 로고    scopus 로고
    • Cross talk between DevS sensor kinase homologue, Rv2027c, and DevR response regulator of Mycobacterium tuberculosis
    • Saini, D. K., Malhotra, V., and Tyagi, J. S. (2004) Cross talk between DevS sensor kinase homologue, Rv2027c, and DevR response regulator of Mycobacterium tuberculosis FEBS Lett. 565, 75-80
    • (2004) FEBS Lett. , vol.565 , pp. 75
    • Saini, D.K.1    Malhotra, V.2    Tyagi, J.S.3
  • 16
    • 0034072208 scopus 로고    scopus 로고
    • New functions for the ancient globin family: Bacterial responses to nitric oxide and nitrosative stress
    • Poole, R. K. and Hughes, M. N. (2000) New functions for the ancient globin family: Bacterial responses to nitric oxide and nitrosative stress Mol. Microbiol. 36, 775-783
    • (2000) Mol. Microbiol. , vol.36 , pp. 775
    • Poole, R.K.1    Hughes, M.N.2
  • 17
    • 0035312317 scopus 로고    scopus 로고
    • Nitric oxide moves myoglobin centre stage
    • DOI 10.1016/S0968-0004(01)01824-2, PII S0968000401018242
    • Brunori, M. (2001) Nitric oxide moves myoglobin centre stage Trends Biochem. Sci. 26, 209-210 (Pubitemid 32289229)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.4 , pp. 209-210
    • Brunori, M.1
  • 18
    • 10644291828 scopus 로고    scopus 로고
    • Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases
    • DOI 10.1016/j.jinorgbio.2004.10.003, PII S016201340400296X, Heme-Diatomic Interactions, Part 1
    • Gardner, P. R. (2005) Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases J. Inorg. Biochem. 99, 247-266 (Pubitemid 39646484)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 247-266
    • Gardner, P.R.1
  • 20
    • 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. (2002) Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli Mol. Microbiol. 45, 1303-1314
    • (2002) Mol. Microbiol. , vol.45 , pp. 1303
    • Pathania, R.1    Navani, N.K.2    Gardner, A.M.3    Gardner, P.R.4    Dikshit, K.L.5
  • 22
    • 0035879486 scopus 로고    scopus 로고
    • Quantitative measurement of radioactive phosphorylated proteins in wet polyacrylamide gels
    • Nakamura, H., Saito, K., and Shiro, Y. (2001) Quantitative measurement of radioactive phosphorylated proteins in wet polyacrylamide gels Anal. Biochem. 294, 187-188
    • (2001) Anal. Biochem. , vol.294 , pp. 187
    • Nakamura, H.1    Saito, K.2    Shiro, Y.3
  • 23
    • 67650561714 scopus 로고    scopus 로고
    • The millisecond intermediate in the reaction of nitric oxide with oxymyoglobin is an iron(III)-nitrato complex, not a peroxynitrite
    • Yukl, E. T., de Vries, S., and MoeÌ̂nne-Loccoz, P. (2009) The millisecond intermediate in the reaction of nitric oxide with oxymyoglobin is an iron(III)-nitrato complex, not a peroxynitrite J. Am. Chem. Soc. 131, 7234-7235
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7234
    • Yukl, E.T.1    De Vries, S.2    Moeì̂nne-Loccoz, P.3
  • 25
    • 34548228384 scopus 로고    scopus 로고
    • Interdomain interactions within the two-component heme-based sensor DevS from Mycobacterium tuberculosis
    • Yukl, E. T., Ioanoviciu, A., de Montellano, P. R., and MoeÌ̂nne-Loccoz, P. (2007) Interdomain interactions within the two-component heme-based sensor DevS from Mycobacterium tuberculosis Biochemistry 46, 9728-9736
    • (2007) Biochemistry , vol.46 , pp. 9728
    • Yukl, E.T.1    Ioanoviciu, A.2    De Montellano, P.R.3    Moeì̂nne-Loccoz, P.4
  • 26
    • 0000729344 scopus 로고
    • Resonance Raman studies of nitric oxide binding to ferric and ferrous hemoproteins: Detection of Fe(III)-NO stretching, Fe(III)-N-O bending, and Fe(II)-N-O bending vibrations
    • Benko, B. and Yu, N. T. (1983) Resonance Raman studies of nitric oxide binding to ferric and ferrous hemoproteins: Detection of Fe(III)-NO stretching, Fe(III)-N-O bending, and Fe(II)-N-O bending vibrations Proc. Natl. Acad. Sci. U.S.A. 80, 7042-7046
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 7042
    • Benko, B.1    Yu, N.T.2
  • 27
    • 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. (2004) NO binding induced conformational changes in a truncated hemoglobin from Mycobacterium tuberculosis Biochemistry 43, 2764-2770
    • (2004) Biochemistry , vol.43 , pp. 2764
    • Mukai, M.1    Ouellet, Y.2    Ouellet, H.3    Guertin, M.4    Yeh, S.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.