메뉴 건너뛰기




Volumn 415, Issue 1, 2011, Pages 82-87

Crystal structure of Campylobacter jejuni ChuZ: A split-barrel family heme oxygenase with a novel heme-binding mode

Author keywords

Bacterial iron acquisition; Campylobacter jejuni; ChuZ; Crystal structure; Heme oxygenase

Indexed keywords

BACTERIAL ENZYME; CHUZ ENZYME; HISTIDINE; UNCLASSIFIED DRUG;

EID: 80755188914     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.10.016     Document Type: Article
Times cited : (20)

References (21)
  • 1
    • 9244234392 scopus 로고    scopus 로고
    • Bacterial iron sources: from siderophores to hemophores
    • Wandersman C., Delepelaire P. Bacterial iron sources: from siderophores to hemophores. Ann. Rev. Microbiol. 2004, 58:611-647.
    • (2004) Ann. Rev. Microbiol. , vol.58 , pp. 611-647
    • Wandersman, C.1    Delepelaire, P.2
  • 2
    • 0034793688 scopus 로고    scopus 로고
    • The Haber-Weiss cycle - 70 years later
    • Koppenol W.H. The Haber-Weiss cycle - 70 years later. Redox Rep. 2001, 6:229-234.
    • (2001) Redox Rep. , vol.6 , pp. 229-234
    • Koppenol, W.H.1
  • 3
    • 64049100955 scopus 로고    scopus 로고
    • Iron in innate immunity: starve the invaders
    • Ganz T. Iron in innate immunity: starve the invaders. Curr. Opin. Immunol. 2009, 63-67.
    • (2009) Curr. Opin. Immunol. , pp. 63-67
    • Ganz, T.1
  • 4
    • 4644310922 scopus 로고    scopus 로고
    • Iron-source preference of Staphylococcus aureus infections
    • Skaar E.P., Humayun M., Bae T., DeBord K.L., Schneewind O. Iron-source preference of Staphylococcus aureus infections. Science 2004, 305:1626-1628.
    • (2004) Science , vol.305 , pp. 1626-1628
    • Skaar, E.P.1    Humayun, M.2    Bae, T.3    DeBord, K.L.4    Schneewind, O.5
  • 6
    • 31344432103 scopus 로고    scopus 로고
    • Bacillus anthracis IsdG, a heme-degrading monooxygenase
    • Skaar E.P., Gaspar A.H., Schneewind O. Bacillus anthracis IsdG, a heme-degrading monooxygenase. J. Bacteriol. 2006, 188:1071-1080.
    • (2006) J. Bacteriol. , vol.188 , pp. 1071-1080
    • Skaar, E.P.1    Gaspar, A.H.2    Schneewind, O.3
  • 7
    • 57649233088 scopus 로고    scopus 로고
    • Ruffling of metalloporphyrins bound to IsdG and IsdI, two heme-degrading enzymes in Staphylococcus aureus
    • Lee W.C., Reniere M.L., Skaar E.P., Murphy M.E.P. Ruffling of metalloporphyrins bound to IsdG and IsdI, two heme-degrading enzymes in Staphylococcus aureus. J. Biol. Chem. 2008, 283:30957-30963.
    • (2008) J. Biol. Chem. , vol.283 , pp. 30957-30963
    • Lee, W.C.1    Reniere, M.L.2    Skaar, E.P.3    Murphy, M.E.P.4
  • 9
    • 0036285109 scopus 로고    scopus 로고
    • The role of iron in Campylobacter gene regulation, metabolism and oxidative stress defense
    • van Vliet A.H., Ketley J.M., Park S.F., Penn C.W. The role of iron in Campylobacter gene regulation, metabolism and oxidative stress defense. FEMS Microbiol. Rev. 2002, 26:173-186.
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 173-186
    • van Vliet, A.H.1    Ketley, J.M.2    Park, S.F.3    Penn, C.W.4
  • 13
    • 0028103275 scopus 로고
    • Collaborative Computational Project Number 4, The CCP4 suite: programs for protein crystallography, Acta Crystallogr
    • Collaborative Computational Project Number 4, The CCP4 suite: programs for protein crystallography, Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763.
    • (1994) Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 17
    • 0000582319 scopus 로고
    • Oxygen-bound heme-heme oxygenase complex - evidence for a highly bent structure of the coordinated oxygen
    • Takahashi S., Ishikawa K., Takeuchi N., Ikedasaito M., Yoshida T., Rousseau D.L. Oxygen-bound heme-heme oxygenase complex - evidence for a highly bent structure of the coordinated oxygen. J. Am. Chem. Soc. 1995, 117:6002-6006.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6002-6006
    • Takahashi, S.1    Ishikawa, K.2    Takeuchi, N.3    Ikedasaito, M.4    Yoshida, T.5    Rousseau, D.L.6
  • 18
    • 0346003806 scopus 로고    scopus 로고
    • Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide - implication for regiospecific hydroxylation of heme at the α-meso carbon
    • Sugishima M., Sakamoto H., Higashimoto Y., Omata Y., Hayashi S., Noguchi M., Fukuyama K. Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide - implication for regiospecific hydroxylation of heme at the α-meso carbon. J. Biol. Chem. 2002, 277:45086-45090.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45086-45090
    • Sugishima, M.1    Sakamoto, H.2    Higashimoto, Y.3    Omata, Y.4    Hayashi, S.5    Noguchi, M.6    Fukuyama, K.7
  • 21
    • 78649921851 scopus 로고    scopus 로고
    • Overcoming the heme paradox: heme toxicity and tolerance in bacterial pathogens
    • Anzaldi L.L., Skaar E.P. Overcoming the heme paradox: heme toxicity and tolerance in bacterial pathogens. Infect. Immun. 2010, 78:4977-4989.
    • (2010) Infect. Immun. , vol.78 , pp. 4977-4989
    • Anzaldi, L.L.1    Skaar, E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.