메뉴 건너뛰기




Volumn 149, Issue 4, 2003, Pages 843-853

Transmissible Burkholderia cepacia genomovar IIIa strains bind and convert monomeric iron(III) protoporphyrin IX into the μ-oxo oligomeric form

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CATALASE; FERRIC ION; HEME; HEME BINDING PROTEIN; HYDROGEN PEROXIDE; MONOMER; OLIGOMER; OUTER MEMBRANE PROTEIN; PROTOPORPHYRIN; TETRAMETHYLBENZIDINE; UNCLASSIFIED DRUG;

EID: 0037690754     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.26160-0     Document Type: Review
Times cited : (11)

References (27)
  • 2
    • 41049100518 scopus 로고
    • A spectrophotometric assay for measuring the breakdown of hydrogen peroxide by catalase
    • Beers, R. F. & Sizer, I. W. (1952). A spectrophotometric assay for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 196, 133-140.
    • (1952) J. Biol. Chem. , vol.196 , pp. 133-140
    • Beers, R.F.1    Sizer, I.W.2
  • 3
    • 0020677346 scopus 로고
    • Endobronchial pH relevance to aminoglycoside activity in gram-negative bacillary pneumonia
    • Bodem, C. R., Lampton, L. M., Miller, D. P., Tarka, E. F. & Everett, E. D. (1983). Endobronchial pH relevance to aminoglycoside activity in gram-negative bacillary pneumonia. Am Rev Respir Dis 127, 39-41.
    • (1983) Am. Rev. Respir. Dis. , vol.127 , pp. 39-41
    • Bodem, C.R.1    Lampton, L.M.2    Miller, D.P.3    Tarka, E.F.4    Everett, E.D.5
  • 4
    • 0014784328 scopus 로고
    • Catalytic activity of iron(III)-centred catalysts. Role of dimerization in the catalytic actions of ferrihaems
    • Brown, S. B., Dean, T. C. & Jones, P. (1970). Catalytic activity of iron(III)-centred catalysts. Role of dimerization in the catalytic actions of ferrihaems. Biochem J 117, 741-744.
    • (1970) Biochem. J. , vol.117 , pp. 741-744
    • Brown, S.B.1    Dean, T.C.2    Jones, P.3
  • 5
    • 0018665012 scopus 로고
    • Semiquantitative catalase test as an aid in identification of oxidative and nonsaccharolytic Gram-negative bacteria
    • Chester, B. (1979). Semiquantitative catalase test as an aid in identification of oxidative and nonsaccharolytic Gram-negative bacteria. J Clin Microbiol 10, 525-528.
    • (1979) J. Clin. Microbiol. , vol.10 , pp. 525-528
    • Chester, B.1
  • 6
    • 0025153096 scopus 로고
    • Pathogenic factors of Pseudomonas cepacia isolates from patients with cystic fibrosis
    • Gessner, A. R. & Mortensen, J. E. (1990). Pathogenic factors of Pseudomonas cepacia isolates from patients with cystic fibrosis. J Med Microbiol 33, 115-120.
    • (1990) J. Med. Microbiol. , vol.33 , pp. 115-120
    • Gessner, A.R.1    Mortensen, J.E.2
  • 7
    • 0032800507 scopus 로고    scopus 로고
    • The effects of heme-binding proteins on the peroxidative and catalytic activities of hemin
    • Grinberg, L. N., O'Brien, P. J. & Hrkal, Z. (1999). The effects of heme-binding proteins on the peroxidative and catalytic activities of hemin. Free Rad Biol Med 26, 214-219.
    • (1999) Free Rad. Biol. Med. , vol.26 , pp. 214-219
    • Grinberg, L.N.1    O'Brien, P.J.2    Hrkal, Z.3
  • 8
    • 0024241523 scopus 로고
    • Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation
    • Gutteridge, J. M. C. & Smith, A. (1988). Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation. Biochem J 256, 861-865.
    • (1988) Biochem. J. , vol.256 , pp. 861-865
    • Gutteridge, J.M.C.1    Smith, A.2
  • 9
    • 0036244378 scopus 로고    scopus 로고
    • Persistent and aggressive bacteria in the lungs of cystic fibrosis children
    • Hart, C. A. & Winstanley, C. (2002). Persistent and aggressive bacteria in the lungs of cystic fibrosis children. Br Med Bull 61, 81-96.
    • (2002) Br. Med. Bull. , vol.61 , pp. 81-96
    • Hart, C.A.1    Winstanley, C.2
  • 11
    • 0015892246 scopus 로고
    • The catalase activity of ferrihaems
    • Jones, P., Robson, T. &, Brown. S. B. (1973). The catalase activity of ferrihaems. Biochem J 135, 353-359.
    • (1973) Biochem. J. , vol.135 , pp. 353-359
    • Jones, P.1    Robson, T.2    Brown, S.B.3
  • 12
    • 0026558681 scopus 로고
    • Isolation of haemin-binding proteins of Neisseria gonorrhoeae
    • Lee, B. C. (1992). Isolation of haemin-binding proteins of Neisseria gonorrhoeae. J Med Microbiol 36, 121-127.
    • (1992) J. Med. Microbiol. , vol.36 , pp. 121-127
    • Lee, B.C.1
  • 13
    • 0035156332 scopus 로고    scopus 로고
    • In vitro resistance of Burkholderia cepacia complex isolates to reactive oxygen species in relation to catalase and superoxide dismutase production
    • Lefebre, M. D. & Valvano, M. A. (2001). In vitro resistance of Burkholderia cepacia complex isolates to reactive oxygen species in relation to catalase and superoxide dismutase production. Microbiology 147, 97-109.
    • (2001) Microbiology , vol.147 , pp. 97-109
    • Lefebre, M.D.1    Valvano, M.A.2
  • 14
    • 0016686915 scopus 로고
    • Cellular and subcellular localization of heme and hemopexin in the rabbit
    • Liem, H. H., Tavassoli, M. & Muller-Eberhard, U. (1975). Cellular and subcellular localization of heme and hemopexin in the rabbit. Acta Haematol 53, 219-225.
    • (1975) Acta Haematol. , vol.53 , pp. 219-225
    • Liem, H.H.1    Tavassoli, M.2    Muller-Eberhard, U.3
  • 16
    • 0035503325 scopus 로고    scopus 로고
    • Infection with Burkholderia cepacia complex genomovars in patients with cystic fibrosis: Virulent transmissible strains of genomovar III can replace Burkholderia multivorans
    • & 7 other authors
    • Mahenthiralingam, E., Vandamme, P., Campbell, M. E. & 7 other authors (2001). Infection with Burkholderia cepacia complex genomovars in patients with cystic fibrosis: virulent transmissible strains of genomovar III can replace Burkholderia multivorans. Clin Infect Dis 33, 1469-1475.
    • (2001) Clin. Infect. Dis. , vol.33 , pp. 1469-1475
    • Mahenthiralingam, E.1    Vandamme, P.2    Campbell, M.E.3
  • 17
    • 0030058367 scopus 로고    scopus 로고
    • Identification of heme-binding proteins in the cell membranes of Vibrio anguillarum
    • Mazoy, R. & Lemos, M. L. (1996). Identification of heme-binding proteins in the cell membranes of Vibrio anguillarum. FEMS Microbiol Lett 135, 265-270.
    • (1996) FEMS Microbiol. Lett. , vol.135 , pp. 265-270
    • Mazoy, R.1    Lemos, M.L.2
  • 18
    • 0002441137 scopus 로고
    • Mossbauer and spectroscopic studies on substituted tetraphenylporphyrinato iron (III) complexes in aqueous solutions and the formation of the μ-oxo-bridged species
    • Miller, J. R., Taies, J. A. & Silver, J. (1987). Mossbauer and spectroscopic studies on substituted tetraphenylporphyrinato iron (III) complexes in aqueous solutions and the formation of the μ-oxo-bridged species. Inorg Chim Acta 138, 205-214.
    • (1987) Inorg. Chim. Acta , vol.138 , pp. 205-214
    • Miller, J.R.1    Taies, J.A.2    Silver, J.3
  • 19
    • 0001210830 scopus 로고
    • Mössbauer studies on protoporphyrin IX iron(III) solutions
    • Silver, J. & Lukas, B. (1983). Mössbauer studies on protoporphyrin IX iron(III) solutions. Inory Chim Acta 78, 219-224.
    • (1983) Inory Chim. Acta , vol.78 , pp. 219-224
    • Silver, J.1    Lukas, B.2
  • 20
    • 0027358741 scopus 로고
    • Haemin-binding proteins in Porphyromonas gingivalis W50 grown in the chemostat under haemin-limitation
    • Smalley, J. W., Birss, A. J., McKee, A. S. & Marsh, P. D. (1993). Haemin-binding proteins in Porphyromonas gingivalis W50 grown in the chemostat under haemin-limitation. J Gen Microbiol 139, 2145-2150.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2145-2150
    • Smalley, J.W.1    Birss, A.J.2    McKee, A.S.3    Marsh, P.D.4
  • 21
    • 0032080290 scopus 로고    scopus 로고
    • The periodontopathogen Porphyromonas gingivalis binds iron protoporphyrin IX in the μ-oxo dimeric form: An oxidative buffer and possible pathogenic mechanism
    • Smalley, J. W., Silver, J., Marsh, P. J. & Birss, A. J. (1998). The periodontopathogen Porphyromonas gingivalis binds iron protoporphyrin IX in the μ-oxo dimeric form: an oxidative buffer and possible pathogenic mechanism. Biochem J 331, 681-677.
    • (1998) Biochem. J. , vol.331 , pp. 677-681
    • Smalley, J.W.1    Silver, J.2    Marsh, P.J.3    Birss, A.J.4
  • 22
    • 0033963571 scopus 로고    scopus 로고
    • The periodontal pathogen Porphyromonas gingivalis harnesses the chemistry of the μ-oxo bishaem of iron protoporphyrin IX to protect against hydrogen peroxide
    • Smalley, J. W., Birss, A. J. & Silver, J. (2000). The periodontal pathogen Porphyromonas gingivalis harnesses the chemistry of the μ-oxo bishaem of iron protoporphyrin IX to protect against hydrogen peroxide. FEMS Microbiol Lett 183, 159-164.
    • (2000) FEMS Microbiol. Lett. , vol.183 , pp. 159-164
    • Smalley, J.W.1    Birss, A.J.2    Silver, J.3
  • 23
    • 0035025515 scopus 로고    scopus 로고
    • Detection of heme-binding proteins in epidemic strains of Burkolderia cepacia
    • Smalley, J. W., Charalabous, P., Birss, A. J. & Hart, C. A. (2001). Detection of heme-binding proteins in epidemic strains of Burkolderia cepacia. Clin Diag Lab Immunol 8, 509-514.
    • (2001) Clin. Diag. Lab. Immunol. , vol.8 , pp. 509-514
    • Smalley, J.W.1    Charalabous, P.2    Birss, A.J.3    Hart, C.A.4
  • 24
    • 0037084219 scopus 로고    scopus 로고
    • Interactions of Porphyromonas gingivalis with oxyhaemoglobin and deoxyhaemoglobin
    • Smalley, J. W., Birss, A. J., Withnall, R. & Silver, J. (2002). Interactions of Porphyromonas gingivalis with oxyhaemoglobin and deoxyhaemoglobin. Biochem J 362, 239-245.
    • (2002) Biochem. J. , vol.362 , pp. 239-245
    • Smalley, J.W.1    Birss, A.J.2    Withnall, R.3    Silver, J.4
  • 25
    • 0024469837 scopus 로고
    • A 101-kilodalton heme-binding protein associated with congo red binding and virulence of Shigella flexneri and enteroinvasive Escherichia coli strains
    • Stugard, C. E., Daskaleros, P. A. & Pain, S. M. (1989). A 101-kilodalton heme-binding protein associated with congo red binding and virulence of Shigella flexneri and enteroinvasive Escherichia coli strains. Infect Immun 57, 3534-3539.
    • (1989) Infect. Immun. , vol.57 , pp. 3534-3539
    • Stugard, C.E.1    Daskaleros, P.A.2    Pain, S.M.3
  • 26
    • 0034112116 scopus 로고    scopus 로고
    • Bacterial heme sources: The role of heme, hemoprotein receptors and hemophores
    • Wandersman, C. & Stojiljkovic, I. (2000). Bacterial heme sources: the role of heme, hemoprotein receptors and hemophores. Curr Opin Microbiol 3, 215-220.
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 215-220
    • Wandersman, C.1    Stojiljkovic, I.2
  • 27
    • 0000668753 scopus 로고
    • Edited by D. Dolphin. London: Academic Press
    • White, W. I. (1978). In The Porphyrins, vol. 7, p. 303. Edited by D. Dolphin. London: Academic Press.
    • (1978) The Porphyrins , vol.7 , pp. 303
    • White, W.I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.