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Volumn 52, Issue , 2006, Pages 73-106

Structure, Mechanism and Physiological Roles of Bacterial Cytochrome c Peroxidases

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; CYTOCHROME C PEROXIDASE; GLUTATHIONE; HYDROGEN PEROXIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; THIOREDOXIN;

EID: 33749247782     PISSN: 00652911     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-2911(06)52002-8     Document Type: Review
Times cited : (67)

References (109)
  • 1
    • 14644391544 scopus 로고    scopus 로고
    • Complexity and diversity in c-type cytochrome biogenesis systems
    • Allen J.W.A., Ginger M.L., and Ferguson S.J. Complexity and diversity in c-type cytochrome biogenesis systems. Biochem. Soc. Trans. 33 (2005) 145-146
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 145-146
    • Allen, J.W.A.1    Ginger, M.L.2    Ferguson, S.J.3
  • 3
    • 0028235802 scopus 로고
    • A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states
    • Arciero D., and Hooper A. A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states. J. Biol. Chem. 269 (1994) 11878-11886
    • (1994) J. Biol. Chem. , vol.269 , pp. 11878-11886
    • Arciero, D.1    Hooper, A.2
  • 4
    • 0032837846 scopus 로고    scopus 로고
    • An iron-regulated alkyl hydroperoxide reductase (AhpC) confers aerotolerance and oxidative stress resistance to the microaerophilic pathogen Campylobacter jejuni
    • Baillon M.-L.A., van Vliet A.H.M., Ketley J.M., Constantinidou C., and Penn C.W. An iron-regulated alkyl hydroperoxide reductase (AhpC) confers aerotolerance and oxidative stress resistance to the microaerophilic pathogen Campylobacter jejuni. J. Bacteriol. 181 (1999) 4798-4804
    • (1999) J. Bacteriol. , vol.181 , pp. 4798-4804
    • Baillon, M.-L.A.1    van Vliet, A.H.M.2    Ketley, J.M.3    Constantinidou, C.4    Penn, C.W.5
  • 5
    • 0035108401 scopus 로고    scopus 로고
    • Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization
    • Baker L.M.S., Raudonikiene A., Hoffman P.S., and Poole L.B. Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization. J. Bacteriol. 183 (2001) 1961-1973
    • (2001) J. Bacteriol. , vol.183 , pp. 1961-1973
    • Baker, L.M.S.1    Raudonikiene, A.2    Hoffman, P.S.3    Poole, L.B.4
  • 6
    • 0342939339 scopus 로고
    • Peroxide metabolism in the liver fluke, Fasciola hepatica
    • Barrett J. Peroxide metabolism in the liver fluke, Fasciola hepatica. J. Parasitol. 66 (1980) 697
    • (1980) J. Parasitol. , vol.66 , pp. 697
    • Barrett, J.1
  • 7
    • 1842778899 scopus 로고    scopus 로고
    • A distinctive electrocatalytic response from the cytochrome c peroxidase of Nitrosomonas europaea
    • Bradley A.L., Chobot S.E., Arciero D.M., Hooper A.B., and Elliott S.J. A distinctive electrocatalytic response from the cytochrome c peroxidase of Nitrosomonas europaea. J. Biol. Chem. 279 (2004) 13297-13300
    • (2004) J. Biol. Chem. , vol.279 , pp. 13297-13300
    • Bradley, A.L.1    Chobot, S.E.2    Arciero, D.M.3    Hooper, A.B.4    Elliott, S.J.5
  • 8
    • 0344171894 scopus 로고    scopus 로고
    • A novel Campylobacter jejuni two-component regulatory system important for temperature-dependent growth and colonization
    • Bras A.M., Chatterjee S., Wren B.W., Newell D.G., and Ketley J.M. A novel Campylobacter jejuni two-component regulatory system important for temperature-dependent growth and colonization. J. Bacteriol. 181 (1999) 3298-3302
    • (1999) J. Bacteriol. , vol.181 , pp. 3298-3302
    • Bras, A.M.1    Chatterjee, S.2    Wren, B.W.3    Newell, D.G.4    Ketley, J.M.5
  • 9
    • 0346251029 scopus 로고    scopus 로고
    • Contribution of glutathione peroxidase to the virulence of Streptococcus pyogenes
    • Brenot A., King K.Y., Janowiak B., Griffith O., and Caparon M.G. Contribution of glutathione peroxidase to the virulence of Streptococcus pyogenes. Infect. Immun. 72 (2004) 408-413
    • (2004) Infect. Immun. , vol.72 , pp. 408-413
    • Brenot, A.1    King, K.Y.2    Janowiak, B.3    Griffith, O.4    Caparon, M.G.5
  • 10
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • Bryk R., Griffin P., and Nathan C. Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 407 (2000) 211-215
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 11
    • 0018701850 scopus 로고    scopus 로고
    • Butzler, J.P., Skirrow, M.B. (1979). Campylobacter enteritis. Clin. Gastroenterol. 8, 737-765.
  • 12
    • 0032987544 scopus 로고    scopus 로고
    • Characterisation of Fasciola hepatica cytochrome c peroxidase as an enzyme with potential antioxidant activity in vitro
    • Campos E.G., Hermes-Lima M., Smith J.M., and Prichard R.K. Characterisation of Fasciola hepatica cytochrome c peroxidase as an enzyme with potential antioxidant activity in vitro. Int. J. Parasitol. 29 (1999) 655-662
    • (1999) Int. J. Parasitol. , vol.29 , pp. 655-662
    • Campos, E.G.1    Hermes-Lima, M.2    Smith, J.M.3    Prichard, R.K.4
  • 13
    • 0028845858 scopus 로고
    • Thioredoxin-linked "thiol peroxidase" from the periplasmic space of Escherichia coli
    • Cha M.-K., Kim H.-K., and Kim I.-H. Thioredoxin-linked "thiol peroxidase" from the periplasmic space of Escherichia coli. J. Biol. Chem. 270 (1995) 28635-28641
    • (1995) J. Biol. Chem. , vol.270 , pp. 28635-28641
    • Cha, M.-K.1    Kim, H.-K.2    Kim, I.-H.3
  • 14
    • 22144475073 scopus 로고    scopus 로고
    • OxyR mediated compensatory expression between ahpC and katA and the significance of AhpC in protection from hydrogen peroxide in Xanthomonas campestris
    • Charoenlap N., Eiamphungporn W., Chauvatcharin N., Utamapongchai S., Vattanaviboon P., and Mongkolsuk S. OxyR mediated compensatory expression between ahpC and katA and the significance of AhpC in protection from hydrogen peroxide in Xanthomonas campestris. FEMS Microbiol. Lett. 249 (2005) 73-78
    • (2005) FEMS Microbiol. Lett. , vol.249 , pp. 73-78
    • Charoenlap, N.1    Eiamphungporn, W.2    Chauvatcharin, N.3    Utamapongchai, S.4    Vattanaviboon, P.5    Mongkolsuk, S.6
  • 15
    • 0842309140 scopus 로고    scopus 로고
    • Diversity of structures and properties among catalases
    • Chelikani P., Fita I., and Loewen P.C. Diversity of structures and properties among catalases. Cell Mol. Life Sci. 61 (2004) 192-208
    • (2004) Cell Mol. Life Sci. , vol.61 , pp. 192-208
    • Chelikani, P.1    Fita, I.2    Loewen, P.C.3
  • 16
    • 0028216615 scopus 로고
    • Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: complete nucleotide sequence and generation and characteristics of mau mutants
    • Chistoserdov A.Y., Chistoserdova L.V., McIntire W.S., and Lidstrom M.E. Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: complete nucleotide sequence and generation and characteristics of mau mutants. J. Bacteriol. 176 (1994) 4052-4065
    • (1994) J. Bacteriol. , vol.176 , pp. 4052-4065
    • Chistoserdov, A.Y.1    Chistoserdova, L.V.2    McIntire, W.S.3    Lidstrom, M.E.4
  • 17
    • 0028222405 scopus 로고
    • Organization of the methylamine utilization (mau) genes in Methylophilus methylotrophus W3A1-NS
    • Chistoserdov A.Y., McIntire W.S., Mathews F.S., and Lidstrom M.E. Organization of the methylamine utilization (mau) genes in Methylophilus methylotrophus W3A1-NS. J. Bacteriol. 176 (1994) 4073-4080
    • (1994) J. Bacteriol. , vol.176 , pp. 4073-4080
    • Chistoserdov, A.Y.1    McIntire, W.S.2    Mathews, F.S.3    Lidstrom, M.E.4
  • 18
    • 1542272169 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli thiol peroxidase in the oxidized state: insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys peroxiredoxins
    • Choi J., Choi S., Choi J., Cha M.-K., Kim I.-H., and Shin W. Crystal structure of Escherichia coli thiol peroxidase in the oxidized state: insights into intramolecular disulfide formation and substrate binding in atypical 2-Cys peroxiredoxins. J. Biol. Chem. 278 (2003) 49478-49486
    • (2003) J. Biol. Chem. , vol.278 , pp. 49478-49486
    • Choi, J.1    Choi, S.2    Choi, J.3    Cha, M.-K.4    Kim, I.-H.5    Shin, W.6
  • 19
    • 0037258943 scopus 로고    scopus 로고
    • Role of the thioredoxin system and the thiol-peroxidases Tpx and Bcp in mediating resistance to oxidative and nitrosative stress in Helicobacter pylori
    • Comtois S.L., Gidley M.D., and Kelly D.J. Role of the thioredoxin system and the thiol-peroxidases Tpx and Bcp in mediating resistance to oxidative and nitrosative stress in Helicobacter pylori. Microbiology 149 (2003) 121-129
    • (2003) Microbiology , vol.149 , pp. 121-129
    • Comtois, S.L.1    Gidley, M.D.2    Kelly, D.J.3
  • 20
    • 0142213304 scopus 로고    scopus 로고
    • Close encounters of the transient kind: protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy
    • Crowley P.B., and Ubbink M. Close encounters of the transient kind: protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy. Acc. Chem. Res. 36 (2003) 723-730
    • (2003) Acc. Chem. Res. , vol.36 , pp. 723-730
    • Crowley, P.B.1    Ubbink, M.2
  • 21
    • 0035663745 scopus 로고    scopus 로고
    • Cloning, overproduction and characterization of cytochrome c peroxidase from the purple phototrophic bacterium Rhodobacter capsulatus
    • De Smet L., Pettigrew G.W., and Van Beeumen J.J. Cloning, overproduction and characterization of cytochrome c peroxidase from the purple phototrophic bacterium Rhodobacter capsulatus. Eur. J. Biochem. 268 (2001) 6559-6568
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6559-6568
    • De Smet, L.1    Pettigrew, G.W.2    Van Beeumen, J.J.3
  • 22
    • 33645238281 scopus 로고    scopus 로고
    • Structural and mutagenesis studies on the cytochrome c peroxidase from Rhodobacter capsulatus provide new insights into structure-function relationships of bacterial di-heme peroxidases
    • De Smet L., Savvides S.N., Van Horen E., Pettigrew G.W., and Van Beeumen J.J. Structural and mutagenesis studies on the cytochrome c peroxidase from Rhodobacter capsulatus provide new insights into structure-function relationships of bacterial di-heme peroxidases. J. Biol. Chem. 281 (2006) 4371-4379
    • (2006) J. Biol. Chem. , vol.281 , pp. 4371-4379
    • De Smet, L.1    Savvides, S.N.2    Van Horen, E.3    Pettigrew, G.W.4    Van Beeumen, J.J.5
  • 24
    • 4644302117 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of a di-haem cytochrome c peroxidase from Paracoccus denitrificans
    • Echalier A., Goodhew C.F., Pettigrew G.W., and Fulop V. Crystallization and preliminary X-ray diffraction analysis of a di-haem cytochrome c peroxidase from Paracoccus denitrificans. Acta Crystallogr. 60 (2004) 331-333
    • (2004) Acta Crystallogr. , vol.60 , pp. 331-333
    • Echalier, A.1    Goodhew, C.F.2    Pettigrew, G.W.3    Fulop, V.4
  • 25
    • 33644795665 scopus 로고    scopus 로고
    • Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus
    • Echalier A., Goodhew C.F., Pettigrew G.W., and Fulop V. Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus. Structure 14 (2006) 107-117
    • (2006) Structure , vol.14 , pp. 107-117
    • Echalier, A.1    Goodhew, C.F.2    Pettigrew, G.W.3    Fulop, V.4
  • 27
    • 0014912795 scopus 로고
    • Pseudomonas cytochrome c peroxidase. I. Purification procedure
    • Ellfolk N., and Soininen R. Pseudomonas cytochrome c peroxidase. I. Purification procedure. Acta Chem. Scand. 24 (1970) 2126-2136
    • (1970) Acta Chem. Scand. , vol.24 , pp. 2126-2136
    • Ellfolk, N.1    Soininen, R.2
  • 28
    • 0030822346 scopus 로고    scopus 로고
    • Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium
    • Ellis H.R., and Poole L.B. Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium. Biochemistry 36 (1997) 13349-13356
    • (1997) Biochemistry , vol.36 , pp. 13349-13356
    • Ellis, H.R.1    Poole, L.B.2
  • 30
    • 0000122573 scopus 로고
    • PHYLIP, phylogeny inference package (Version 3.2)
    • Felsenstein J. PHYLIP, phylogeny inference package (Version 3.2). Cladistics 5 (1989) 164-166
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 31
    • 0029645915 scopus 로고
    • Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa
    • Fulop V., Ridout C.J., Greenwood C., and Hajdu J. Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa. Structure 3 (1995) 1225-1233
    • (1995) Structure , vol.3 , pp. 1225-1233
    • Fulop, V.1    Ridout, C.J.2    Greenwood, C.3    Hajdu, J.4
  • 33
    • 0029154216 scopus 로고
    • Cloning, sequencing, and mutation of a gene for azurin in Methylobacillus flagellatum KT
    • Gak E., Chistoserdov A., and Lidstrom M. Cloning, sequencing, and mutation of a gene for azurin in Methylobacillus flagellatum KT. J. Bacteriol. 177 (1995) 4575-4578
    • (1995) J. Bacteriol. , vol.177 , pp. 4575-4578
    • Gak, E.1    Chistoserdov, A.2    Lidstrom, M.3
  • 34
    • 10444242473 scopus 로고    scopus 로고
    • Cytochrome c peroxidase contributes to the antioxidant defense of Cryptococcus neoformans
    • Giles S.S., Perfect J.R., and Cox G.M. Cytochrome c peroxidase contributes to the antioxidant defense of Cryptococcus neoformans. Fungal Genet. Biol. 42 (2005) 20-29
    • (2005) Fungal Genet. Biol. , vol.42 , pp. 20-29
    • Giles, S.S.1    Perfect, J.R.2    Cox, G.M.3
  • 35
    • 0027489230 scopus 로고
    • Spectroscopic characterization of cytochrome c peroxidase from Paracoccus denitrificans
    • Gilmour R., Goodhew C.F., Pettigrew G.W., Prazeres S., Moura I., and Moura J.J. Spectroscopic characterization of cytochrome c peroxidase from Paracoccus denitrificans. Biochem. J. 294 (1993) 745-752
    • (1993) Biochem. J. , vol.294 , pp. 745-752
    • Gilmour, R.1    Goodhew, C.F.2    Pettigrew, G.W.3    Prazeres, S.4    Moura, I.5    Moura, J.J.6
  • 36
  • 38
  • 39
    • 0025045910 scopus 로고
    • The cellular location and specificity of bacterial cytochrome c peroxidases
    • Goodhew C.F., Wilson I.B., Hunter D.J., and Pettigrew G.W. The cellular location and specificity of bacterial cytochrome c peroxidases. Biochem. J. 271 (1990) 707-712
    • (1990) Biochem. J. , vol.271 , pp. 707-712
    • Goodhew, C.F.1    Wilson, I.B.2    Hunter, D.J.3    Pettigrew, G.W.4
  • 40
    • 0006778586 scopus 로고
    • A di-haem cytochrome c peroxidase (Pseudomonas aeruginosa): its activation and catalytic cycle
    • Greenwood C., Foote N., Gadsby P.M., and Thomson A.J. A di-haem cytochrome c peroxidase (Pseudomonas aeruginosa): its activation and catalytic cycle. Chem. Scripta 28A (1988) 79-84
    • (1988) Chem. Scripta , vol.28 A , pp. 79-84
    • Greenwood, C.1    Foote, N.2    Gadsby, P.M.3    Thomson, A.J.4
  • 41
    • 21844442599 scopus 로고    scopus 로고
    • Structure and mechanism of the alkyl hydroperoxidase AhpC, a key element of the Mycobacterium tuberculosis defense system against oxidative stress
    • Guimaraes B.G., Souchon H., Honore N., Saint-Joanis B., Brosch R., Shepard W., Cole S.T., and Alzari P.M. Structure and mechanism of the alkyl hydroperoxidase AhpC, a key element of the Mycobacterium tuberculosis defense system against oxidative stress. J. Biol. Chem. 280 (2005) 25735-25742
    • (2005) J. Biol. Chem. , vol.280 , pp. 25735-25742
    • Guimaraes, B.G.1    Souchon, H.2    Honore, N.3    Saint-Joanis, B.4    Brosch, R.5    Shepard, W.6    Cole, S.T.7    Alzari, P.M.8
  • 42
    • 0026781687 scopus 로고
    • The 44 kDa c-type cytochrome induced in Rhodobacter capsulatus during growth with dimethylsulphoxide as an electron acceptor is cytochrome c peroxidase
    • Hanlon S.P., Holt R.A., and McEwan A.G. The 44 kDa c-type cytochrome induced in Rhodobacter capsulatus during growth with dimethylsulphoxide as an electron acceptor is cytochrome c peroxidase. FEMS Microbiol. Lett. 97 (1992) 283-288
    • (1992) FEMS Microbiol. Lett. , vol.97 , pp. 283-288
    • Hanlon, S.P.1    Holt, R.A.2    McEwan, A.G.3
  • 43
    • 0037657832 scopus 로고    scopus 로고
    • Role of charges on cytochrome f from the cyanobacterium Phormidium laminosum in its interaction with plastocyanin
    • Hart S.E., Schlarb-Ridley B.G., Delon C., Bendall D.S., and Howe C.J. Role of charges on cytochrome f from the cyanobacterium Phormidium laminosum in its interaction with plastocyanin. Biochemistry 42 (2003) 4829-4836
    • (2003) Biochemistry , vol.42 , pp. 4829-4836
    • Hart, S.E.1    Schlarb-Ridley, B.G.2    Delon, C.3    Bendall, D.S.4    Howe, C.J.5
  • 44
    • 32544437414 scopus 로고    scopus 로고
    • Multiple haem lyase genes indicate substrate specificity in cytochrome c biogenesis
    • Hartshorne S., Richardson D.J., and Simon J. Multiple haem lyase genes indicate substrate specificity in cytochrome c biogenesis. Biochem. Soc. Trans. 34 (2006) 146-149
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 146-149
    • Hartshorne, S.1    Richardson, D.J.2    Simon, J.3
  • 45
    • 1942532926 scopus 로고    scopus 로고
    • Identification of Campylobacter jejuni genes involved in commensal colonization of the chick gastrointestinal tract
    • Hendrixson D.R., and DiRita V.J. Identification of Campylobacter jejuni genes involved in commensal colonization of the chick gastrointestinal tract. Mol. Microbiol. 52 (2004) 471-484
    • (2004) Mol. Microbiol. , vol.52 , pp. 471-484
    • Hendrixson, D.R.1    DiRita, V.J.2
  • 46
    • 0035723780 scopus 로고    scopus 로고
    • Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA
    • Herbig A.F., and Helmann J.D. Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA. Mol. Microbiol. 41 (2001) 849-859
    • (2001) Mol. Microbiol. , vol.41 , pp. 849-859
    • Herbig, A.F.1    Helmann, J.D.2
  • 47
    • 0141887670 scopus 로고    scopus 로고
    • Genetic analysis of an important oxidative stress locus in the anaerobe Bacteroides fragilis
    • Herren C.D., Rocha E.R., and Smith C.J. Genetic analysis of an important oxidative stress locus in the anaerobe Bacteroides fragilis. Gene 316 (2003) 167-175
    • (2003) Gene , vol.316 , pp. 167-175
    • Herren, C.D.1    Rocha, E.R.2    Smith, C.J.3
  • 49
    • 0035013928 scopus 로고    scopus 로고
    • PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus
    • Horsburgh M.J., Clements M.O., Crossley H., Ingham E., and Foster S.J. PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus. Infect. Immun. 69 (2001) 3744-3754
    • (2001) Infect. Immun. , vol.69 , pp. 3744-3754
    • Horsburgh, M.J.1    Clements, M.O.2    Crossley, H.3    Ingham, E.4    Foster, S.J.5
  • 51
    • 0035985581 scopus 로고    scopus 로고
    • How oxygen damages microbes: oxygen tolerance and obligate anaerobiosis
    • Imlay J.A. How oxygen damages microbes: oxygen tolerance and obligate anaerobiosis. Adv. Microb. Physiol. 46 (2002) 111-153
    • (2002) Adv. Microb. Physiol. , vol.46 , pp. 111-153
    • Imlay, J.A.1
  • 52
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay J.A. Pathways of oxidative damage. Annu. Rev. Microbiol. 57 (2003) 395-418
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 53
    • 0023905646 scopus 로고
    • Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
    • Imlay J.A., Chin S.M., and Linn S. Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 240 (1988) 640-642
    • (1988) Science , vol.240 , pp. 640-642
    • Imlay, J.A.1    Chin, S.M.2    Linn, S.3
  • 54
    • 0025832166 scopus 로고
    • Adaptation of Escherichia coli to respiratory conditions: regulation of gene expression
    • Iuchi S., and Lin E.C.C. Adaptation of Escherichia coli to respiratory conditions: regulation of gene expression. Cell 66 (1991) 5-7
    • (1991) Cell , vol.66 , pp. 5-7
    • Iuchi, S.1    Lin, E.C.C.2
  • 55
    • 0034916351 scopus 로고    scopus 로고
    • Out of the iron age: new insights into the critical role of manganese homeostasis in bacteria
    • Jakubovics N.S., and Jenkinson H.F. Out of the iron age: new insights into the critical role of manganese homeostasis in bacteria. Microbiology 147 (2001) 1709-1718
    • (2001) Microbiology , vol.147 , pp. 1709-1718
    • Jakubovics, N.S.1    Jenkinson, H.F.2
  • 56
    • 0034723165 scopus 로고    scopus 로고
    • Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin co-migratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/alkyl hydroperoxide peroxidase C (AhpC) family
    • Jeong W., Cha M.-K., and Kim I.-H. Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin co-migratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/alkyl hydroperoxide peroxidase C (AhpC) family. J. Biol. Chem. 275 (2000) 2924-2930
    • (2000) J. Biol. Chem. , vol.275 , pp. 2924-2930
    • Jeong, W.1    Cha, M.-K.2    Kim, I.-H.3
  • 57
    • 0027535314 scopus 로고
    • Characterization of a catalase-deficient strain of Neisseria gonorrhoeae: evidence for the significance of catalase in the biology of N. gonorrhoeae.
    • Johnson S.R., Steiner B.M., Cruce D.D., Perkins G.H., and Arko R.J. Characterization of a catalase-deficient strain of Neisseria gonorrhoeae: evidence for the significance of catalase in the biology of N. gonorrhoeae. Infect. Immun. 61 (1993) 1232-1238
    • (1993) Infect. Immun. , vol.61 , pp. 1232-1238
    • Johnson, S.R.1    Steiner, B.M.2    Cruce, D.D.3    Perkins, G.H.4    Arko, R.J.5
  • 58
    • 3142663916 scopus 로고    scopus 로고
    • Alkyl hydroperoxide peroxidase subunit C (ahpC) protects against organic peroxides but does not affect the virulence of Porphyromonas gingivalis W83
    • Johnson N.A., Liu Y., and Fletcher H.M. Alkyl hydroperoxide peroxidase subunit C (ahpC) protects against organic peroxides but does not affect the virulence of Porphyromonas gingivalis W83. Oral Microbiol. Immunol. 19 (2004) 233-239
    • (2004) Oral Microbiol. Immunol. , vol.19 , pp. 233-239
    • Johnson, N.A.1    Liu, Y.2    Fletcher, H.M.3
  • 59
    • 29144486999 scopus 로고    scopus 로고
    • Identification of a copper-repressible c-type heme protein of Methylococcus capsulatus (Bath). A member of a novel group of the bacterial di-heme cytochrome c peroxidase family of proteins
    • Karlsen O.A., Kindingstad L., Angelskar S.M., Bruseth L.J., Straume D., Puntervoll P., Fjellbirkeland A., Lillehaug J.R., and Jensen H.B. Identification of a copper-repressible c-type heme protein of Methylococcus capsulatus (Bath). A member of a novel group of the bacterial di-heme cytochrome c peroxidase family of proteins. FEBS J. 272 (2005) 6324-6335
    • (2005) FEBS J. , vol.272 , pp. 6324-6335
    • Karlsen, O.A.1    Kindingstad, L.2    Angelskar, S.M.3    Bruseth, L.J.4    Straume, D.5    Puntervoll, P.6    Fjellbirkeland, A.7    Lillehaug, J.R.8    Jensen, H.B.9
  • 60
    • 0034970220 scopus 로고    scopus 로고
    • The physiology and metabolism of Campylobacter jejuni and Helicobacter pylori
    • Kelly D.J. The physiology and metabolism of Campylobacter jejuni and Helicobacter pylori. J. Appl. Microbiol. 90 (2001) 16S-24S
    • (2001) J. Appl. Microbiol. , vol.90
    • Kelly, D.J.1
  • 62
    • 0025350809 scopus 로고
    • Isolation and characterisation of hydrogen peroxide producing Aerococcus sp. from soil samples
    • Kontchou C.Y., and Blondeau R. Isolation and characterisation of hydrogen peroxide producing Aerococcus sp. from soil samples. FEMS Microbiol. Lett. 68 (1990) 323-328
    • (1990) FEMS Microbiol. Lett. , vol.68 , pp. 323-328
    • Kontchou, C.Y.1    Blondeau, R.2
  • 63
    • 0042882611 scopus 로고    scopus 로고
    • Oxidative stresses elevate the expression of cytochrome c peroxidase in Saccharomyces cerevisiae
    • Kwon M., Chong S., Han S., and Kim K. Oxidative stresses elevate the expression of cytochrome c peroxidase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1623 (2003) 1-5
    • (2003) Biochim. Biophys. Acta , vol.1623 , pp. 1-5
    • Kwon, M.1    Chong, S.2    Han, S.3    Kim, K.4
  • 65
    • 0037177224 scopus 로고    scopus 로고
    • Role of the low-affinity binding site in electron transfer from cytochrome c to cytochrome c peroxidase
    • Mei H., Geren L., Miller M.A., Durham B., and Millett F. Role of the low-affinity binding site in electron transfer from cytochrome c to cytochrome c peroxidase. Biochemistry 41 (2002) 3968-3976
    • (2002) Biochemistry , vol.41 , pp. 3968-3976
    • Mei, H.1    Geren, L.2    Miller, M.A.3    Durham, B.4    Millett, F.5
  • 66
    • 0035884739 scopus 로고    scopus 로고
    • Antioxidant function of cytosolic sources of NADPH in yeast
    • Minard K.I., and McAlister-Henn L. Antioxidant function of cytosolic sources of NADPH in yeast. Free Radic. Biol. Med. 31 (2001) 832-843
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 832-843
    • Minard, K.I.1    McAlister-Henn, L.2
  • 68
    • 8944258926 scopus 로고    scopus 로고
    • Interruption of the gpxA gene increases the sensitivity of Neisseria meningitidis to paraquat
    • Moore T., and Sparling P. Interruption of the gpxA gene increases the sensitivity of Neisseria meningitidis to paraquat. J. Bacteriol. 178 (1996) 4301-4305
    • (1996) J. Bacteriol. , vol.178 , pp. 4301-4305
    • Moore, T.1    Sparling, P.2
  • 69
    • 13444259982 scopus 로고    scopus 로고
    • A sulphite respiration system in the chemoheterotrophic human pathogen Campylobacter jejuni
    • Myers J.D., and Kelly D.J. A sulphite respiration system in the chemoheterotrophic human pathogen Campylobacter jejuni. Microbiology 151 (2005) 233-242
    • (2005) Microbiology , vol.151 , pp. 233-242
    • Myers, J.D.1    Kelly, D.J.2
  • 70
    • 0037220694 scopus 로고    scopus 로고
    • Association of Helicobacter pylori antioxidant activities with host colonization proficiency
    • Olczak A.A., Seyler Jr. R.W., Olson J.W., and Maier R.J. Association of Helicobacter pylori antioxidant activities with host colonization proficiency. Infect. Immun. 71 (2003) 580-583
    • (2003) Infect. Immun. , vol.71 , pp. 580-583
    • Olczak, A.A.1    Seyler Jr., R.W.2    Olson, J.W.3    Maier, R.J.4
  • 71
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: an application to display phylogenetic trees on personal computers
    • Page R.D.M. TreeView: an application to display phylogenetic trees on personal computers. Comput. Appl. Biosci. 12 (1996) 357-358
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.M.1
  • 73
    • 23244466487 scopus 로고    scopus 로고
    • Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin
    • Parsonage D., Youngblood D.S., Sarma G.N., Wood Z.A., Karplus P.A., and Poole L.B. Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. Biochemistry 44 (2005) 10583-10592
    • (2005) Biochemistry , vol.44 , pp. 10583-10592
    • Parsonage, D.1    Youngblood, D.S.2    Sarma, G.N.3    Wood, Z.A.4    Karplus, P.A.5    Poole, L.B.6
  • 77
    • 0037465427 scopus 로고    scopus 로고
    • The electron transfer complexes of cytochrome c peroxidase from Paracoccus denitrificans
    • Pettigrew G.W., Goodhew C.F., Cooper A., Nutley M., Jumel K., and Harding S.E. The electron transfer complexes of cytochrome c peroxidase from Paracoccus denitrificans. Biochemistry 42 (2003) 2046-2055
    • (2003) Biochemistry , vol.42 , pp. 2046-2055
    • Pettigrew, G.W.1    Goodhew, C.F.2    Cooper, A.3    Nutley, M.4    Jumel, K.5    Harding, S.E.6
  • 80
    • 9744232974 scopus 로고    scopus 로고
    • Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases
    • Poole L.B. Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases. Arch. Biochem. Biophys. 433 (2005) 240-254
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 240-254
    • Poole, L.B.1
  • 81
    • 0033771859 scopus 로고    scopus 로고
    • AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase
    • Poole L.B., Reynolds C.M., Wood Z.A., Karplus P.A., Ellis H.R., and Li Calzi M. AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase. Eur. J. Biochem. 267 (2000) 6126-6133
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6126-6133
    • Poole, L.B.1    Reynolds, C.M.2    Wood, Z.A.3    Karplus, P.A.4    Ellis, H.R.5    Li Calzi, M.6
  • 82
    • 84989070986 scopus 로고
    • Control of the spin state of the peroxidatic heme by calcium ions in cytochrome c peroxidase: a 1 H NMR study
    • Prazeres S., Moura I., Moura J.J.G., Gilmour R., Goodhew C.F., and Pettigrew G.W. Control of the spin state of the peroxidatic heme by calcium ions in cytochrome c peroxidase: a 1 H NMR study. Magn. Reson. Chem. 31 (1993) 68-72
    • (1993) Magn. Reson. Chem. , vol.31 , pp. 68-72
    • Prazeres, S.1    Moura, I.2    Moura, J.J.G.3    Gilmour, R.4    Goodhew, C.F.5    Pettigrew, G.W.6
  • 83
    • 0028882301 scopus 로고
    • Competition between hydrogen peroxide and nitrate for electrons from the respiratory chains of Thiosphaera pantotropha and Rhodobacter capsulatus
    • Richardson D., and Ferguson S.J. Competition between hydrogen peroxide and nitrate for electrons from the respiratory chains of Thiosphaera pantotropha and Rhodobacter capsulatus. FEMS Microbiol. Lett. 132 (1995) 125-129
    • (1995) FEMS Microbiol. Lett. , vol.132 , pp. 125-129
    • Richardson, D.1    Ferguson, S.J.2
  • 84
    • 0019465006 scopus 로고
    • The reaction between reduced azurin and oxidized cytochrome c peroxidase from Pseudomonas aeruginosa
    • Ronnberg M., Araiso T., Ellfolk N., and Dunford H. The reaction between reduced azurin and oxidized cytochrome c peroxidase from Pseudomonas aeruginosa. J. Biol. Chem. 256 (1981) 2471-2474
    • (1981) J. Biol. Chem. , vol.256 , pp. 2471-2474
    • Ronnberg, M.1    Araiso, T.2    Ellfolk, N.3    Dunford, H.4
  • 85
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli
    • Seaver L.C., and Imlay J.A. Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J. Bacteriol. 183 (2001) 7173-7181
    • (2001) J. Bacteriol. , vol.183 , pp. 7173-7181
    • Seaver, L.C.1    Imlay, J.A.2
  • 86
    • 10344238617 scopus 로고    scopus 로고
    • Are respiratory enzymes the primary sources of intracellular hydrogen peroxide?
    • Seaver L.C., and Imlay J.A. Are respiratory enzymes the primary sources of intracellular hydrogen peroxide?. J. Biol. Chem. 279 (2004) 48742-48750
    • (2004) J. Biol. Chem. , vol.279 , pp. 48742-48750
    • Seaver, L.C.1    Imlay, J.A.2
  • 87
    • 3042842612 scopus 로고    scopus 로고
    • Defenses against oxidative stress in Neisseria gonorrhoeae and Neisseria meningitidis: distinctive systems for different lifestyles
    • Seib K.L., Tseng H.J., McEwan A.G., Apicella M.A., and Jennings M.P. Defenses against oxidative stress in Neisseria gonorrhoeae and Neisseria meningitidis: distinctive systems for different lifestyles. J. Infect. Dis. 190 (2004) 136-147
    • (2004) J. Infect. Dis. , vol.190 , pp. 136-147
    • Seib, K.L.1    Tseng, H.J.2    McEwan, A.G.3    Apicella, M.A.4    Jennings, M.P.5
  • 88
    • 0035856525 scopus 로고    scopus 로고
    • Crystal structure of Nitrosomonas europaea cytochrome c peroxidase and the structural basis for ligand switching in bacterial di-heme peroxidases
    • Shimizu H., Schuller D.J., Lanzilotta W.N., Sundaramoorthy M., Arciero D.M., Hooper A.B., and Poulos T.L. Crystal structure of Nitrosomonas europaea cytochrome c peroxidase and the structural basis for ligand switching in bacterial di-heme peroxidases. Biochemistry 40 (2001) 13483-13490
    • (2001) Biochemistry , vol.40 , pp. 13483-13490
    • Shimizu, H.1    Schuller, D.J.2    Lanzilotta, W.N.3    Sundaramoorthy, M.4    Arciero, D.M.5    Hooper, A.B.6    Poulos, T.L.7
  • 89
    • 0024473758 scopus 로고
    • Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES
    • Sivaraja M., Goodin D.B., Smith M., and Hoffman B.M. Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES. Science 245 (1989) 738-740
    • (1989) Science , vol.245 , pp. 738-740
    • Sivaraja, M.1    Goodin, D.B.2    Smith, M.3    Hoffman, B.M.4
  • 90
    • 0025820091 scopus 로고
    • Adaptive responses to oxygen limitation in Escherichia coli
    • Spiro S., and Guest J.R. Adaptive responses to oxygen limitation in Escherichia coli. Trends Biochem. Sci. 16 (1991) 310-314
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 310-314
    • Spiro, S.1    Guest, J.R.2
  • 92
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J., Gibson T., Plewniak F., Jeanmougin F., and Higgins D. The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucl. Acids Res. 25 (1997) 4876-4882
    • (1997) Nucl. Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.1    Gibson, T.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.5
  • 94
    • 0042569023 scopus 로고    scopus 로고
    • A novel cytochrome c peroxidase from Neisseria gonorrhoeae: a lipoprotein from a Gram-negative bacterium
    • Turner S., Reid E., Smith H., and Cole J. A novel cytochrome c peroxidase from Neisseria gonorrhoeae: a lipoprotein from a Gram-negative bacterium. Biochem. J. 373 (2003) 865-873
    • (2003) Biochem. J. , vol.373 , pp. 865-873
    • Turner, S.1    Reid, E.2    Smith, H.3    Cole, J.4
  • 96
    • 0031037665 scopus 로고    scopus 로고
    • FnrP and NNR of Paracoccus denitrificans are both members of the FNR family of transcriptional activators but have distinct roles in respiratory adaptation in response to oxygen limitation
    • van Spanning R.J., De Boer A.P., Reijnders W.N., Westerhoff H.V., Stouthamer A.H., and Van Der Oost J. FnrP and NNR of Paracoccus denitrificans are both members of the FNR family of transcriptional activators but have distinct roles in respiratory adaptation in response to oxygen limitation. Mol. Microbiol. 23 (1997) 893-907
    • (1997) Mol. Microbiol. , vol.23 , pp. 893-907
    • van Spanning, R.J.1    De Boer, A.P.2    Reijnders, W.N.3    Westerhoff, H.V.4    Stouthamer, A.H.5    Van Der Oost, J.6
  • 97
    • 0032716842 scopus 로고    scopus 로고
    • Campylobacter jejuni contains two Fur homologs: characterization of iron-responsive regulation of peroxide stress defense genes by the PerR repressor
    • van Vliet A.H.M., Baillon M.-L.A., Penn C.W., and Ketley J.M. Campylobacter jejuni contains two Fur homologs: characterization of iron-responsive regulation of peroxide stress defense genes by the PerR repressor. J. Bacteriol. 181 (1999) 6371-6376
    • (1999) J. Bacteriol. , vol.181 , pp. 6371-6376
    • van Vliet, A.H.M.1    Baillon, M.-L.A.2    Penn, C.W.3    Ketley, J.M.4
  • 98
    • 0036285109 scopus 로고    scopus 로고
    • The role of iron in Campylobacter gene regulation, metabolism and oxidative stress defense
    • van Vliet A.H.M., Ketley J.M., Park S.F., and Penn C.W. The role of iron in Campylobacter gene regulation, metabolism and oxidative stress defense. FEMS Microbiol. Rev. 26 (2002) 173-186
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 173-186
    • van Vliet, A.H.M.1    Ketley, J.M.2    Park, S.F.3    Penn, C.W.4
  • 99
    • 0021449775 scopus 로고
    • NMR and electron-paramagnetic-resonance studies of a di-haem cytochrome from Pseudomonas stutzeri (ATCC 11607) (cytochrome c peroxidase)
    • Villalain J., Moura I., Liu M.C., Payne W.J., LeGall J., Xavier A.V., and Moura J.J. NMR and electron-paramagnetic-resonance studies of a di-haem cytochrome from Pseudomonas stutzeri (ATCC 11607) (cytochrome c peroxidase). Eur. J. Biochem. 141 (1984) 305-312
    • (1984) Eur. J. Biochem. , vol.141 , pp. 305-312
    • Villalain, J.1    Moura, I.2    Liu, M.C.3    Payne, W.J.4    LeGall, J.5    Xavier, A.V.6    Moura, J.J.7
  • 100
    • 0033060309 scopus 로고    scopus 로고
    • Multiple transcription factors of the FNR family in denitrifying Pseudomonas stutzeri: characterization of four fnr-like genes, regulatory responses and cognate metabolic processes
    • Vollack K.-U., Hartig E., Korner H., and Zumft W.G. Multiple transcription factors of the FNR family in denitrifying Pseudomonas stutzeri: characterization of four fnr-like genes, regulatory responses and cognate metabolic processes. Mol. Microbiol. 31 (1999) 1681-1694
    • (1999) Mol. Microbiol. , vol.31 , pp. 1681-1694
    • Vollack, K.-U.1    Hartig, E.2    Korner, H.3    Zumft, W.G.4
  • 101
    • 10644290115 scopus 로고    scopus 로고
    • Role of a bacterial organic hydroperoxide detoxification system in preventing catalase inactivation
    • Wang G., Conover R.C., Benoit S., Olczak A.A., Olson J.W., Johnson MK., and Maier R.J. Role of a bacterial organic hydroperoxide detoxification system in preventing catalase inactivation. J. Biol. Chem. 279 (2004) 51908-51914
    • (2004) J. Biol. Chem. , vol.279 , pp. 51908-51914
    • Wang, G.1    Conover, R.C.2    Benoit, S.3    Olczak, A.A.4    Olson, J.W.5    Johnson, MK.6    Maier, R.J.7
  • 102
    • 11144328882 scopus 로고    scopus 로고
    • Contribution of the Helicobacter pylori thiol peroxidase bacterioferritin co-migratory protein to oxidative stress resistance and host colonization
    • Wang G., Olczak A.A., Walton J.P., and Maier R.J. Contribution of the Helicobacter pylori thiol peroxidase bacterioferritin co-migratory protein to oxidative stress resistance and host colonization. Infect. Immun. 73 (2005) 378-384
    • (2005) Infect. Immun. , vol.73 , pp. 378-384
    • Wang, G.1    Olczak, A.A.2    Walton, J.P.3    Maier, R.J.4
  • 103
    • 0038070331 scopus 로고    scopus 로고
    • MauG, a novel di-heme protein required for tryptophan tryptophylquinone biogenesis
    • Wang Y., Graichen M.E., Liu A., Pearson A.R., Wilmot C.M., and Davidson V.L. MauG, a novel di-heme protein required for tryptophan tryptophylquinone biogenesis. Biochemistry 42 (2003) 7318-7325
    • (2003) Biochemistry , vol.42 , pp. 7318-7325
    • Wang, Y.1    Graichen, M.E.2    Liu, A.3    Pearson, A.R.4    Wilmot, C.M.5    Davidson, V.L.6
  • 104
    • 20444493512 scopus 로고    scopus 로고
    • MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase
    • Wang Y., Li X., Jones L.H., Pearson A.R., Wilmot C.M., and Davidson V.L. MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase. J. Am. Chem. Soc. 127 (2005) 8258-8259
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8258-8259
    • Wang, Y.1    Li, X.2    Jones, L.H.3    Pearson, A.R.4    Wilmot, C.M.5    Davidson, V.L.6
  • 107
    • 0033991496 scopus 로고    scopus 로고
    • Redox sensing by prokaryotic transcription factors
    • Zheng M., and Storz G. Redox sensing by prokaryotic transcription factors. Biochem. Pharmacol. 59 (2000) 1-6
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 1-6
    • Zheng, M.1    Storz, G.2
  • 109
    • 0025873743 scopus 로고
    • Anaerobic growth and cyanide synthesis of Pseudomonas aeruginosa depend on anr, a regulatory gene homologous with FNR of Escherichia coli
    • Zimmermann A., Reimmann C., Galimand M., and Haas D. Anaerobic growth and cyanide synthesis of Pseudomonas aeruginosa depend on anr, a regulatory gene homologous with FNR of Escherichia coli. Mol. Microbiol. 5 (1991) 1483-1490
    • (1991) Mol. Microbiol. , vol.5 , pp. 1483-1490
    • Zimmermann, A.1    Reimmann, C.2    Galimand, M.3    Haas, D.4


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