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Volumn 188, Issue 18, 2006, Pages 6476-6482

The hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes

Author keywords

[No Author keywords available]

Indexed keywords

BILIVERDIN; HEME; HEME OXYGENASE; IRON; ISDG MONOOXYGENASE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

EID: 33748768453     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00737-06     Document Type: Article
Times cited : (45)

References (34)
  • 4
    • 0035856979 scopus 로고    scopus 로고
    • Bacteriophytochromes are photochiomic histidine kinases using a biliveidin chromophore
    • Bhoo, S. H., S. J. Davis, J. Walker, B. Karniol, and R. D. Vierstra. 2001. Bacteriophytochromes are photochiomic histidine kinases using a biliveidin chromophore. Nature 414:776-779.
    • (2001) Nature , vol.414 , pp. 776-779
    • Bhoo, S.H.1    Davis, S.J.2    Walker, J.3    Karniol, B.4    Vierstra, R.D.5
  • 5
    • 0032946645 scopus 로고    scopus 로고
    • Bacterial solutions to the iron-supply problem
    • Braun, V., and H. Killmann. 1999. Bacterial solutions to the iron-supply problem. Trends Biochem. Sci. 24:104-109.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 104-109
    • Braun, V.1    Killmann, H.2
  • 7
    • 0034128270 scopus 로고    scopus 로고
    • Corynebacterium diphtheriae genes required for acquisition of iron from haemin and haemoglobin are homologous to ABC haemin transporters
    • Drazek, E. S., C. A. Hammack, and M. P. Schmitt. 2000. Corynebacterium diphtheriae genes required for acquisition of iron from haemin and haemoglobin are homologous to ABC haemin transporters. Mol. Microbiol. 36:68-84.
    • (2000) Mol. Microbiol. , vol.36 , pp. 68-84
    • Drazek, E.S.1    Hammack, C.A.2    Schmitt, M.P.3
  • 8
    • 0026071003 scopus 로고
    • Aerobic growth and respiration of a δ-aminolevulinic acid synthase (hemA) mutant of Bradyrhizobium japonicum
    • Frustaci, J. M., I. Sangwan, and M. R. O'Brian. 1991. Aerobic growth and respiration of a δ-aminolevulinic acid synthase (hemA) mutant of Bradyrhizobium japonicum. J. Bacteriol. 173:1145-1150.
    • (1991) J. Bacteriol. , vol.173 , pp. 1145-1150
    • Frustaci, J.M.1    Sangwan, I.2    O'Brian, M.R.3
  • 9
    • 0035181250 scopus 로고    scopus 로고
    • Emerging strategies in miciobial haem capture
    • Genco, C. A., and D. W. Dixon. 2001. Emerging strategies in miciobial haem capture. Mol. Microbiol. 39:1-11.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1-11
    • Genco, C.A.1    Dixon, D.W.2
  • 10
    • 0037674829 scopus 로고    scopus 로고
    • Is the bacterial ferrous iron transporter FeoB a living fossil?
    • Hantke, K. 2003. Is the bacterial ferrous iron transporter FeoB a living fossil? Trends Microbiol. 11:192-195.
    • (2003) Trends Microbiol. , vol.11 , pp. 192-195
    • Hantke, K.1
  • 11
    • 1642441846 scopus 로고    scopus 로고
    • The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae
    • Hirotsu, S., G. C. Chu, M. Unno, D. S. Lee, T. Yoshida, S. Y. Park, Y. Shiro, and M. Ikeda-Saito. 2004. The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae. J. Biol. Chem. 279:11937-11947.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11937-11947
    • Hirotsu, S.1    Chu, G.C.2    Unno, M.3    Lee, D.S.4    Yoshida, T.5    Park, S.Y.6    Shiro, Y.7    Ikeda-Saito, M.8
  • 13
    • 0035724183 scopus 로고    scopus 로고
    • Discovery of a haem uptake system in the soil bacterium Bradyrhizobium japonicum
    • Nienaber, A., H. Hennecke, and H. M. Fischer. 2001. Discovery of a haem uptake system in the soil bacterium Bradyrhizobium japonicum. Mol. Microbiol. 41:787-800.
    • (2001) Mol. Microbiol. , vol.41 , pp. 787-800
    • Nienaber, A.1    Hennecke, H.2    Fischer, H.M.3
  • 14
    • 0030895301 scopus 로고    scopus 로고
    • Heme compounds as iron sources for nonpathogenic Rhizobium bacteria
    • Noya, F., A. Arias, and E. Fabiano. 1997. Heme compounds as iron sources for nonpathogenic Rhizobium bacteria. J. Bacteriol. 179:3076-3078.
    • (1997) J. Bacteriol. , vol.179 , pp. 3076-3078
    • Noya, F.1    Arias, A.2    Fabiano, E.3
  • 15
    • 0042065285 scopus 로고    scopus 로고
    • Touch and go: Tying TonB to transport
    • Postle, K., and R. J. Kadner. 2003. Touch and go: tying TonB to transport. Mol. Microbiol. 49:869-882.
    • (2003) Mol. Microbiol. , vol.49 , pp. 869-882
    • Postle, K.1    Kadner, R.J.2
  • 16
    • 0035688874 scopus 로고    scopus 로고
    • Homologues of neisserial heme oxygenase in gram-negative bacteria: Degradation of heme by the product of the pigA gene of Pseudomonas aeruginosa
    • Ratliff, M., W. Zhu, R. Deshmukh, A. Wilks, and I. Stojiljkovic. 2001. Homologues of neisserial heme oxygenase in gram-negative bacteria: degradation of heme by the product of the pigA gene of Pseudomonas aeruginosa. J. Bacteriol. 183:6394-6403.
    • (2001) J. Bacteriol. , vol.183 , pp. 6394-6403
    • Ratliff, M.1    Zhu, W.2    Deshmukh, R.3    Wilks, A.4    Stojiljkovic, I.5
  • 18
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • Richardson, D. R., and P. Ponka. 1997. The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells. Biochim. Biophys. Acta 1331:1-40.
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 19
    • 30844432187 scopus 로고    scopus 로고
    • The iron control element, acting in positive and negative control of iron-regulated Bradyrhizobium japonicum genes, is a target for the Irr protein
    • Rudolph, G., G. Semini, F. Hauser, A. Lindemann, M. Friberg, H. Hennecke, and H. M. Fischer. 2006. The iron control element, acting in positive and negative control of iron-regulated Bradyrhizobium japonicum genes, is a target for the Irr protein. J. Bacteriol. 188:733-744.
    • (2006) J. Bacteriol. , vol.188 , pp. 733-744
    • Rudolph, G.1    Semini, G.2    Hauser, F.3    Lindemann, A.4    Friberg, M.5    Hennecke, H.6    Fischer, H.M.7
  • 20
    • 0031034090 scopus 로고    scopus 로고
    • Utilization of host iron sources by Corynebacterium diphtheriae: Identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin
    • Schmitt, M. P. 1997. Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin. J. Bacteriol. 179:838-845.
    • (1997) J. Bacteriol. , vol.179 , pp. 838-845
    • Schmitt, M.P.1
  • 22
    • 0035949642 scopus 로고    scopus 로고
    • Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1
    • Schuller, D. J., W. Zhu, I. Stojiljkovic, A. Wilks, and T. L. Poulos. 2001. Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1. Biochemistry 40:11552-11558.
    • (2001) Biochemistry , vol.40 , pp. 11552-11558
    • Schuller, D.J.1    Zhu, W.2    Stojiljkovic, I.3    Wilks, A.4    Poulos, T.L.5
  • 23
    • 0034838114 scopus 로고    scopus 로고
    • Coupled oxidation of heme by myoglobin is mediated by exogenous peroxide
    • Sigman, J. A., X. Wang, and Y. Lu. 2001. Coupled oxidation of heme by myoglobin is mediated by exogenous peroxide. J. Am. Chem. Soc. 123:6945-6946.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6945-6946
    • Sigman, J.A.1    Wang, X.2    Lu, Y.3
  • 24
    • 31344432103 scopus 로고    scopus 로고
    • Bacillus anthracis IsdG, a heme-degrading monooxygenase
    • Skaar, E. P., A. H. Gaspar, and O. Schneewind. 2006. Bacillus anthracis IsdG, a heme-degrading monooxygenase. J. Bacteriol. 188:1071-1080.
    • (2006) J. Bacteriol. , vol.188 , pp. 1071-1080
    • Skaar, E.P.1    Gaspar, A.H.2    Schneewind, O.3
  • 25
    • 0345791519 scopus 로고    scopus 로고
    • IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus
    • Skaar, E. P., A. H. Gaspar, and O. Schneewind. 2004. IsdG and IsdI, heme-degrading enzymes in the cytoplasm of Staphylococcus aureus. J. Biol. Chem. 279:436-443.
    • (2004) J. Biol. Chem. , vol.279 , pp. 436-443
    • Skaar, E.P.1    Gaspar, A.H.2    Schneewind, O.3
  • 26
    • 0034112116 scopus 로고    scopus 로고
    • Bacterial heme sources: The role of heme, hemoprotein receptors and hemophores
    • Wandersman, C., and I. Stojiljkovic. 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
  • 28
    • 0035725442 scopus 로고    scopus 로고
    • The Rhizobium leguminosarum tonB gene is required for the uptake of siderophore and haem as sources of iron
    • Wexler, M., K. H. Yeoman, J. B. Stevens, N. G. de Luca, G. Sawers, and A. W. B. Johnston. 2001. The Rhizobium leguminosarum tonB gene is required for the uptake of siderophore and haem as sources of iron. Mol. Microbiol. 41:801-816.
    • (2001) Mol. Microbiol. , vol.41 , pp. 801-816
    • Wexler, M.1    Yeoman, K.H.2    Stevens, J.B.3    De Luca, N.G.4    Sawers, G.5    Johnston, A.W.B.6
  • 29
    • 0030046411 scopus 로고    scopus 로고
    • Heme oxygenase (HO-1): His-132 stabilizes a distal water ligand and assists catalysis
    • Wilks, A., P. R. Ortiz de Montellano, J. Sun, and T. M. Loehr. 1996. Heme oxygenase (HO-1): His-132 stabilizes a distal water ligand and assists catalysis. Biochemistry 35:930-936.
    • (1996) Biochemistry , vol.35 , pp. 930-936
    • Wilks, A.1    De Ortiz Montellano, P.R.2    Sun, J.3    Loehr, T.M.4
  • 30
    • 0031984521 scopus 로고    scopus 로고
    • Expression and characterization of a heme oxygenase (HmuO) from Corynebacterium diphtheriae. Iron acquisition requires oxidative cleavage of the heme macrocycle
    • Wilks, A., and M. P. Schmitt. 1998. Expression and characterization of a heme oxygenase (HmuO) from Corynebacterium diphtheriae. Iron acquisition requires oxidative cleavage of the heme macrocycle. J. Biol. Chem. 273:837-841.
    • (1998) J. Biol. Chem. , vol.273 , pp. 837-841
    • Wilks, A.1    Schmitt, M.P.2
  • 31
    • 13244296905 scopus 로고    scopus 로고
    • Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases
    • Wu, R., E. P. Skaar, R. Zhang, G. Joachimiak, P. Gornicki, O. Schneewind, and A. Joachimiak. 2005. Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases. J. Biol. Chem. 280:2840-2846.
    • (2005) J. Biol. Chem. , vol.280 , pp. 2840-2846
    • Wu, R.1    Skaar, E.P.2    Zhang, R.3    Joachimiak, G.4    Gornicki, P.5    Schneewind, O.6    Joachimiak, A.7
  • 32
    • 33645322140 scopus 로고    scopus 로고
    • Bradyrhizobium japonicum senses iron through the status of haem to regulate iron homeostasis and metabolism
    • Yang, J., I. Sangwan, A. Lindemann, F. Hauser, H. Hennecke, H. M. Fischer, and M. R. O'Brian. 2006. Bradyrhizobium japonicum senses iron through the status of haem to regulate iron homeostasis and metabolism. Mol. Microbiol. 60:427-437.
    • (2006) Mol. Microbiol. , vol.60 , pp. 427-437
    • Yang, J.1    Sangwan, I.2    Lindemann, A.3    Hauser, F.4    Hennecke, H.5    Fischer, H.M.6    O'Brian, M.R.7
  • 33
    • 0033988059 scopus 로고    scopus 로고
    • Use of heme compounds as iron sources by pathogenic neisseriae requires the product of the hemO gene
    • Zhu, W., D. J. Hunt, A. R. Richardson, and I. Stojiljkovic. 2000. Use of heme compounds as iron sources by pathogenic neisseriae requires the product of the hemO gene. J. Bacteriol. 182:439-447.
    • (2000) J. Bacteriol. , vol.182 , pp. 439-447
    • Zhu, W.1    Hunt, D.J.2    Richardson, A.R.3    Stojiljkovic, I.4
  • 34
    • 0034461244 scopus 로고    scopus 로고
    • Degradation of heme in gram-negative bacteria: The product of the hemO gene of Neisseriae is a heme oxygenase
    • Zhu, W., A. Wilks, and I. Stojiljkovic. 2000. Degradation of heme in gram-negative bacteria: the product of the hemO gene of Neisseriae is a heme oxygenase. J. Bacteriol. 182:6783-6790.
    • (2000) J. Bacteriol. , vol.182 , pp. 6783-6790
    • Zhu, W.1    Wilks, A.2    Stojiljkovic, I.3


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