메뉴 건너뛰기




Volumn 190, Issue 3, 2008, Pages 915-925

The Campylobacter jejuni NADH:Ubiquinone oxidoreductase (complex I) utilizes flavodoxin rather than NADH

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; FLAVODOXIN; GENOMIC DNA; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); RNA;

EID: 38649086396     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01647-07     Document Type: Article
Times cited : (60)

References (41)
  • 3
    • 0023697273 scopus 로고
    • Colonization of gastrointestinal tracts of chicks by Campylobacter jejuni
    • Beery, J. T., M. B. Hugdahl, and M. P. Doyle. 1988. Colonization of gastrointestinal tracts of chicks by Campylobacter jejuni. Appl. Environ. Microbiol. 54:2365-2370.
    • (1988) Appl. Environ. Microbiol , vol.54 , pp. 2365-2370
    • Beery, J.T.1    Hugdahl, M.B.2    Doyle, M.P.3
  • 4
    • 0032539640 scopus 로고    scopus 로고
    • Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    • Braun, M., S. Bungert, and T. Friedrich. 1998. Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochemistry 37:1861-1867.
    • (1998) Biochemistry , vol.37 , pp. 1861-1867
    • Braun, M.1    Bungert, S.2    Friedrich, T.3
  • 5
    • 0023985949 scopus 로고
    • Structure, function and evolution of bacterial ferredoxins
    • Bruschi, M., and F. Guerlesquin. 1988. Structure, function and evolution of bacterial ferredoxins. FEMS Microbiol. Rev. 4:155-175.
    • (1988) FEMS Microbiol. Rev , vol.4 , pp. 155-175
    • Bruschi, M.1    Guerlesquin, F.2
  • 6
    • 6444243531 scopus 로고    scopus 로고
    • Campylobacter, from obscurity to celebrity
    • Butzler, J. P. 2004. Campylobacter, from obscurity to celebrity. Clin. Microbiol. Infect. 10:868-876.
    • (2004) Clin. Microbiol. Infect , vol.10 , pp. 868-876
    • Butzler, J.P.1
  • 7
    • 33646827488 scopus 로고    scopus 로고
    • The versatile epsilon-proteobacteria: Key players in sulphidic habitats
    • Campbell, B. J., A. S. Engel, M. L. Porter, and K. Takai. 2006. The versatile epsilon-proteobacteria: key players in sulphidic habitats. Nat. Rev. Microbiol. 4:458-468.
    • (2006) Nat. Rev. Microbiol , vol.4 , pp. 458-468
    • Campbell, B.J.1    Engel, A.S.2    Porter, M.L.3    Takai, K.4
  • 8
    • 0020433098 scopus 로고
    • Aerobic and anaerobic respiratory systems in Campylobacter fetus subsp. jejuni grown in atmospheres containing hydrogen
    • Carlone, G. M., and J. Lascelles. 1982. Aerobic and anaerobic respiratory systems in Campylobacter fetus subsp. jejuni grown in atmospheres containing hydrogen. J. Bacteriol. 152:306-314.
    • (1982) J. Bacteriol , vol.152 , pp. 306-314
    • Carlone, G.M.1    Lascelles, J.2
  • 9
    • 0031771082 scopus 로고    scopus 로고
    • Does NADH play a central role in energy metabolism in Helicobacter pylori?
    • Finel, M. 1998. Does NADH play a central role in energy metabolism in Helicobacter pylori? Trends Biochem. Sci. 23:412-413.
    • (1998) Trends Biochem. Sci , vol.23 , pp. 412-413
    • Finel, M.1
  • 10
    • 0036145495 scopus 로고    scopus 로고
    • Crystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylori
    • Freigang, J., K. Diederichs, K. P. Schafer, W. Welte, and R. Paul. 2002. Crystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylori. Protein Sci. 11:253-261.
    • (2002) Protein Sci , vol.11 , pp. 253-261
    • Freigang, J.1    Diederichs, K.2    Schafer, K.P.3    Welte, W.4    Paul, R.5
  • 11
    • 0000742695 scopus 로고    scopus 로고
    • Epidemiology of Campylobacter jejuni in the United States and other industrialized nations
    • I. Nachamkin and M. J. Blaser ed, 2nd ed. ASM Press, Washington, DC
    • Friedman, C. R., J. Neiman, H. C. Wegener, and R. V. Tauxe. 2000. Epidemiology of Campylobacter jejuni in the United States and other industrialized nations, p. 121-138. In I. Nachamkin and M. J. Blaser (ed.), Campylobacter, 2nd ed. ASM Press, Washington, DC.
    • (2000) Campylobacter , pp. 121-138
    • Friedman, C.R.1    Neiman, J.2    Wegener, H.C.3    Tauxe, R.V.4
  • 12
    • 1642451816 scopus 로고    scopus 로고
    • The gross structure of the respiratory complex I: A Lego system
    • Friedrich, T., and B. Bottcher. 2004. The gross structure of the respiratory complex I: a Lego system. Biochim. Biophys. Acta 1608:1-9.
    • (2004) Biochim. Biophys. Acta , vol.1608 , pp. 1-9
    • Friedrich, T.1    Bottcher, B.2
  • 13
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    • Friedrich, T., and D. Scheide. 2000. The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases. FEBS Lett. 479:1-5.
    • (2000) FEBS Lett , vol.479 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 14
    • 0020029133 scopus 로고
    • Respiratory physiology and energy conservation efficiency of Campylobacter jejuni
    • Hoffman, P. S., and T. G. Goodman. 1982. Respiratory physiology and energy conservation efficiency of Campylobacter jejuni. J. Bacteriol. 150:319-326.
    • (1982) J. Bacteriol , vol.150 , pp. 319-326
    • Hoffman, P.S.1    Goodman, T.G.2
  • 15
    • 0029046363 scopus 로고
    • Identification of carboxylation enzymes and characterization of a novel four-subunit pyruvate:flavodoxin oxidoreductase from Helicobacter pylori
    • Hughes, N. J., P. A. Chalk, C. L. Clayton, and D. J. Kelly. 1995. Identification of carboxylation enzymes and characterization of a novel four-subunit pyruvate:flavodoxin oxidoreductase from Helicobacter pylori. J. Bacteriol. 177:3953-3959.
    • (1995) J. Bacteriol , vol.177 , pp. 3953-3959
    • Hughes, N.J.1    Chalk, P.A.2    Clayton, C.L.3    Kelly, D.J.4
  • 16
    • 0031885642 scopus 로고    scopus 로고
    • Helicobacter pylori porCDAB and oorDABC genes encode distinct pyruvate:flavodoxin and 2-oxoglutarate:acceptor oxidoreductases which mediate electron transport to NADP
    • Hughes, N. J., C. L. Clayton, P. A. Chalk, and D. J. Kelly. 1998. Helicobacter pylori porCDAB and oorDABC genes encode distinct pyruvate:flavodoxin and 2-oxoglutarate:acceptor oxidoreductases which mediate electron transport to NADP. J. Bacteriol. 180:1119-1128.
    • (1998) J. Bacteriol , vol.180 , pp. 1119-1128
    • Hughes, N.J.1    Clayton, C.L.2    Chalk, P.A.3    Kelly, D.J.4
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0030969593 scopus 로고    scopus 로고
    • Changes with growth rate in the membrane lipid composition of and amino acid utilization by continuous cultures of Campylobacter jejuni
    • Leach, S., P. Harvey, and R. Wali. 1997. Changes with growth rate in the membrane lipid composition of and amino acid utilization by continuous cultures of Campylobacter jejuni. J. Appl. Microbiol. 82:631-640.
    • (1997) J. Appl. Microbiol , vol.82 , pp. 631-640
    • Leach, S.1    Harvey, P.2    Wali, R.3
  • 19
    • 0029075136 scopus 로고
    • Isolation and characterization of the proton-translocating NADH: Ubiquinone oxidoreductase from Escherichia coli
    • Leif, H., V. D. Sled, T. Ohnishi, H. Weiss, and T. Friedrich. 1995. Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli. Eur. J. Biochem. 230:538-548.
    • (1995) Eur. J. Biochem , vol.230 , pp. 538-548
    • Leif, H.1    Sled, V.D.2    Ohnishi, T.3    Weiss, H.4    Friedrich, T.5
  • 20
    • 0242489005 scopus 로고    scopus 로고
    • Diversity and succession of the intestinal bacterial community of the maturing broiler chicken
    • Lu, J., U. Idris, B. Harmon, C. Hofacre, J. J. Maurer, and M. D. Lee. 2003. Diversity and succession of the intestinal bacterial community of the maturing broiler chicken. Appl. Environ. Microbiol. 69:6816-6824.
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 6816-6824
    • Lu, J.1    Idris, U.2    Harmon, B.3    Hofacre, C.4    Maurer, J.J.5    Lee, M.D.6
  • 22
  • 23
    • 4444376017 scopus 로고    scopus 로고
    • The pattern and kinetics of substrate metabolism of Campylobacter jejuni and Campylobacter coli
    • Mohammed, K. A., R. J. Miles, and M. A. Halablab. 2004. The pattern and kinetics of substrate metabolism of Campylobacter jejuni and Campylobacter coli. Lett. Appl. Microbiol. 39:261-266.
    • (2004) Lett. Appl. Microbiol , vol.39 , pp. 261-266
    • Mohammed, K.A.1    Miles, R.J.2    Halablab, M.A.3
  • 24
    • 38649090901 scopus 로고    scopus 로고
    • Myers, J. D., and D. J. Kelly. 2005. Respiratory electron transport in Helicobacter and Campylobacter, p. 63-80. In D. Zannoni (ed.), Respiration in archaea and bacteria, 2. Diversity of prokaryotic respiratory systems. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • Myers, J. D., and D. J. Kelly. 2005. Respiratory electron transport in Helicobacter and Campylobacter, p. 63-80. In D. Zannoni (ed.), Respiration in archaea and bacteria, vol. 2. Diversity of prokaryotic respiratory systems. Kluwer Academic Publishers, Dordrecht, The Netherlands.
  • 25
    • 13444259982 scopus 로고    scopus 로고
    • A sulphite respiration system in the chemoheterotrophic human pathogen Campylobacter jejuni
    • Myers, J. D., and D. J. Kelly. 2005. A sulphite respiration system in the chemoheterotrophic human pathogen Campylobacter jejuni. Microbiology 151:233-242.
    • (2005) Microbiology , vol.151 , pp. 233-242
    • Myers, J.D.1    Kelly, D.J.2
  • 28
    • 0033199239 scopus 로고    scopus 로고
    • Structural and kinetic studies of the pyruvate-ferredoxin oxidoreductase/ferredoxin complex from Desulfovibrio africanus
    • Pieulle, L., M. H. Charon, P. Bianco, J. Bonicel, Y. Petillot, and E. C. Hatchikian. 1999. Structural and kinetic studies of the pyruvate-ferredoxin oxidoreductase/ferredoxin complex from Desulfovibrio africanus. Eur. J. Biochem. 264:500-508.
    • (1999) Eur. J. Biochem , vol.264 , pp. 500-508
    • Pieulle, L.1    Charon, M.H.2    Bianco, P.3    Bonicel, J.4    Petillot, Y.5    Hatchikian, E.C.6
  • 29
    • 33646052947 scopus 로고    scopus 로고
    • Sancho, J. 2006. Flavodoxins: sequence, folding, binding, function and beyond. Cell. Mol. Life Sci. 63:855-864.
    • Sancho, J. 2006. Flavodoxins: sequence, folding, binding, function and beyond. Cell. Mol. Life Sci. 63:855-864.
  • 30
    • 0033872083 scopus 로고    scopus 로고
    • Characteristics of the aerobic respiratory chains of the microaerophiles Campylobacter jejuni and Helicobaaer pylori
    • Smith, M. A., M. Finel, V. Korolik, and G. L. Mendz. 2000. Characteristics of the aerobic respiratory chains of the microaerophiles Campylobacter jejuni and Helicobaaer pylori. Arch. Microbiol. 174:1-10.
    • (2000) Arch. Microbiol , vol.174 , pp. 1-10
    • Smith, M.A.1    Finel, M.2    Korolik, V.3    Mendz, G.L.4
  • 31
    • 34347386473 scopus 로고    scopus 로고
    • St. Maurice, M., N. Cremades, M. A. Croxen, G. Sisson, J. Sancho, and P. S. Hoffman. 2007. Flavodoxin:quinone reductase (FqrB): a redox partner of pyruvate:ferredoxin oxidoreductase that reversibly couples pyruvate oxidation to NADPH production in Helicobacter pylori and Campylobacter jejuni. J. Bacteriol. 189:4764-4773.
    • St. Maurice, M., N. Cremades, M. A. Croxen, G. Sisson, J. Sancho, and P. S. Hoffman. 2007. Flavodoxin:quinone reductase (FqrB): a redox partner of pyruvate:ferredoxin oxidoreductase that reversibly couples pyruvate oxidation to NADPH production in Helicobacter pylori and Campylobacter jejuni. J. Bacteriol. 189:4764-4773.
  • 34
    • 0030835739 scopus 로고    scopus 로고
    • Tomb, J. F., O. White, A. R. Kerlavage, R. A. Clayton, G. G. Sutton, R. D. Fleischmann, K. A. Ketchum, H. P. Klenk, S. Gill, B. A. Dougherty, K. Nelson, J. Quackenbush, L. Zhou, E. F. Kirkness, S. Peterson, B. Loftus, D. Richardson, R. Dodson, H. G. Khalak, A. Glodek, K. McKenney, L. M. Fitzegerald, N. Lee, M. D. Adams, E. K. Hickey, D. E. Berg, J. D. Gocayne, T. R. Utterback, J. D. Peterson, J. M. Kelley, M. D. Cotton, J. M. Weidman, C. Fujii, C. Bowman, L. Watthey, E. Wallin, W. S. Hayes, M. Borodovsky, P. D. Karp, H. O. Smith, C. M. Fraser, and J. C. Venter. 1997. The complete genome sequence of the gastric pathogen Helicobacter pylori. Nature 388:539-547.
    • Tomb, J. F., O. White, A. R. Kerlavage, R. A. Clayton, G. G. Sutton, R. D. Fleischmann, K. A. Ketchum, H. P. Klenk, S. Gill, B. A. Dougherty, K. Nelson, J. Quackenbush, L. Zhou, E. F. Kirkness, S. Peterson, B. Loftus, D. Richardson, R. Dodson, H. G. Khalak, A. Glodek, K. McKenney, L. M. Fitzegerald, N. Lee, M. D. Adams, E. K. Hickey, D. E. Berg, J. D. Gocayne, T. R. Utterback, J. D. Peterson, J. M. Kelley, M. D. Cotton, J. M. Weidman, C. Fujii, C. Bowman, L. Watthey, E. Wallin, W. S. Hayes, M. Borodovsky, P. D. Karp, H. O. Smith, C. M. Fraser, and J. C. Venter. 1997. The complete genome sequence of the gastric pathogen Helicobacter pylori. Nature 388:539-547.
  • 35
    • 0346881405 scopus 로고    scopus 로고
    • Velayudhan, J., M. A. Jones, P. A. Barrow, and D. J. Kelly. 2004. L-Serine catabolism via an oxygen-labile L-serine dehydratase is essential for colonization of the avian gut by Campylobacter jejuni. Infect. Immun. 72:260-268.
    • Velayudhan, J., M. A. Jones, P. A. Barrow, and D. J. Kelly. 2004. L-Serine catabolism via an oxygen-labile L-serine dehydratase is essential for colonization of the avian gut by Campylobacter jejuni. Infect. Immun. 72:260-268.
  • 36
    • 0025132642 scopus 로고
    • Chloramphenicol resistance in Campylobacter coli: Nucleotide sequence, expression, and cloning vector construction
    • Wang, Y., and D. E. Taylor. 1990. Chloramphenicol resistance in Campylobacter coli: nucleotide sequence, expression, and cloning vector construction. Gene 94:23-28.
    • (1990) Gene , vol.94 , pp. 23-28
    • Wang, Y.1    Taylor, D.E.2
  • 37
    • 0027519561 scopus 로고
    • The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I
    • Weidner, U., S. Geier, A. Ptock, T. Friedrich, H. Leif, and H. Weiss. 1993. The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I. J. Mol. Biol. 233:109-122.
    • (1993) J. Mol. Biol , vol.233 , pp. 109-122
    • Weidner, U.1    Geier, S.2    Ptock, A.3    Friedrich, T.4    Leif, H.5    Weiss, H.6
  • 38
    • 0022526617 scopus 로고
    • Substrate utilization by Campylobacter jejuni and Campylobacter coli
    • Westfall, H. N., D. M. Rollins, and E. Weiss. 1986. Substrate utilization by Campylobacter jejuni and Campylobacter coli. Appl. Environ. Microbiol. 52:700-705.
    • (1986) Appl. Environ. Microbiol , vol.52 , pp. 700-705
    • Westfall, H.N.1    Rollins, D.M.2    Weiss, E.3
  • 39
    • 0022974638 scopus 로고
    • Purification and characterization of NADH dehydrogenase complex from Paracoccus denitrificans
    • Yagi, T. 1986. Purification and characterization of NADH dehydrogenase complex from Paracoccus denitrificans. Arch. Biochem. Biophys. 250:302-311.
    • (1986) Arch. Biochem. Biophys , vol.250 , pp. 302-311
    • Yagi, T.1
  • 40
    • 0031041453 scopus 로고    scopus 로고
    • The proton-translocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8. Complete DNA sequence of the gene cluster and thermostable properties of the expressed NQO2 subunit
    • Yano, T., S. S. Chu, V. D. Sled, T. Ohnishi, and T. Yagi. 1997. The proton-translocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8. Complete DNA sequence of the gene cluster and thermostable properties of the expressed NQO2 subunit. J. Biol. Chem. 272:4201-4211.
    • (1997) J. Biol. Chem , vol.272 , pp. 4201-4211
    • Yano, T.1    Chu, S.S.2    Sled, V.D.3    Ohnishi, T.4    Yagi, T.5
  • 41
    • 0027327182 scopus 로고
    • Construction of new Campylobacter cloning vectors and a new mutational cat cassette
    • Yao, R., R. A. Alm, T. J. Trust, and P. Guerry. 1993. Construction of new Campylobacter cloning vectors and a new mutational cat cassette. Gene 130:127-130.
    • (1993) Gene , vol.130 , pp. 127-130
    • Yao, R.1    Alm, R.A.2    Trust, T.J.3    Guerry, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.