메뉴 건너뛰기




Volumn 62, Issue 4, 1998, Pages 1046-1078

Molecular genetics of the Genus paracoccus: Metabolically versatile bacteria with bioenergetic flexibility

Author keywords

[No Author keywords available]

Indexed keywords

AMINE DEHYDROGENASE; BACTERIAL DNA; CYTOCHROME C OXIDASE; FLAVOPROTEIN; FORMALDEHYDE DEHYDROGENASE; HYDROXYBUTYRIC ACID; METHANOL DEHYDROGENASE; NITRATE; NITRIC OXIDE; NITRITE; NITROUS OXIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); RNA POLYMERASE; SUCCINATE DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 0031793773     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/mmbr.62.4.1046-1078.1998     Document Type: Article
Times cited : (183)

References (354)
  • 1
    • 0000972384 scopus 로고
    • Structure and sequence of the photosynthetic gene cluster
    • R. E. Blakenship, M. T. Madigan, and C. E. Bauer (ed.) Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Alberti, M., D. H. Burke, and J. E. Hearst. 1995. Structure and sequence of the photosynthetic gene cluster, p. 1083-1106. In R. E. Blakenship, M. T. Madigan, and C. E. Bauer (ed.), Advances in photosynthesis, anoxygenic photosynthetic bacteria, vol. 2. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Advances in Photosynthesis, Anoxygenic Photosynthetic Bacteria , vol.2 , pp. 1083-1106
    • Alberti, M.1    Burke, D.H.2    Hearst, J.E.3
  • 2
    • 0027146592 scopus 로고
    • Presence of one linear and one circular chromosome in the Agrobacterium tumefaciens C58 genome
    • Allardet-Servent, A., S. Michaux-Charachon, E. Jumas-Bilak, L. Karayan, and M. Ramuz. 1993. Presence of one linear and one circular chromosome in the Agrobacterium tumefaciens C58 genome. J. Bacteriol. 175:7869-7874.
    • (1993) J. Bacteriol. , vol.175 , pp. 7869-7874
    • Allardet-Servent, A.1    Michaux-Charachon, S.2    Jumas-Bilak, E.3    Karayan, L.4    Ramuz, M.5
  • 3
    • 0022541528 scopus 로고
    • Bacterial oxidation of methane and methanol
    • Anthony, C. 1986. Bacterial oxidation of methane and methanol. Adv. Microb. Physiol. 37:113-210.
    • (1986) Adv. Microb. Physiol. , vol.37 , pp. 113-210
    • Anthony, C.1
  • 4
    • 0025963610 scopus 로고
    • Nucleotide sequence of the fixABC region of Azorhizobium caulinodans ORS571: Similarity of the fixB product with eukaryotic flavoproteins, characterization of fixX, and identification of nifW
    • Arigoni, F., P. A. Kaminski, H. Hennecke, and C. Elmerich. 1991. Nucleotide sequence of the fixABC region of Azorhizobium caulinodans ORS571: similarity of the fixB product with eukaryotic flavoproteins, characterization of fixX, and identification of nifW. Mol. Gen. Genet. 225:514-520.
    • (1991) Mol. Gen. Genet. , vol.225 , pp. 514-520
    • Arigoni, F.1    Kaminski, P.A.2    Hennecke, H.3    Elmerich, C.4
  • 7
    • 0030984912 scopus 로고    scopus 로고
    • Characterization of the nitric oxide reductase-encoding region in Rhodobacter sphaeroides 2.4.3
    • Bartnikas, T. B., I. E. Tosques, W. P. Laratta, J. Shi, and J. P. Shapleigh. 1997. Characterization of the nitric oxide reductase-encoding region in Rhodobacter sphaeroides 2.4.3. J. Bacteriol. 179:3534-3540.
    • (1997) J. Bacteriol. , vol.179 , pp. 3534-3540
    • Bartnikas, T.B.1    Tosques, I.E.2    Laratta, W.P.3    Shi, J.4    Shapleigh, J.P.5
  • 9
    • 0029001456 scopus 로고
    • Construction and preliminary characterisation of mini-derivatives of a large (107-kb) cryptic plasmid of the sulfur bacterium Thiobacillus versutus
    • Bartosik, D., J. Baj, and M. Wlodarczyk. 1995. Construction and preliminary characterisation of mini-derivatives of a large (107-kb) cryptic plasmid of the sulfur bacterium Thiobacillus versutus. FEMS Microbiol. Lett. 129: 169-174.
    • (1995) FEMS Microbiol. Lett. , vol.129 , pp. 169-174
    • Bartosik, D.1    Baj, J.2    Wlodarczyk, M.3
  • 10
    • 0028990246 scopus 로고
    • Characterization of FNR* mutant proteins indicates two distinct mechanisms for altering oxygen regulation of the Escherichia coli transcription factor FNR
    • Bates, D. M., B. A. Lazazzera, and P. J. Kiley. 1995. Characterization of FNR* mutant proteins indicates two distinct mechanisms for altering oxygen regulation of the Escherichia coli transcription factor FNR. J. Bacteriol. 177:3972-3978.
    • (1995) J. Bacteriol. , vol.177 , pp. 3972-3978
    • Bates, D.M.1    Lazazzera, B.A.2    Kiley, P.J.3
  • 11
    • 0023938869 scopus 로고
    • Analysis of the Rhodobacter capsulatus puf operon. Location of the oxygen-regulated promoter region and the identification of an additional puf-encoded gene
    • Bauer, C. E., D. A. Young, and B. L. Marrs. 1988. Analysis of the Rhodobacter capsulatus puf operon. Location of the oxygen-regulated promoter region and the identification of an additional puf-encoded gene. J. Biol. Chem. 263:4820-4827.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4820-4827
    • Bauer, C.E.1    Young, D.A.2    Marrs, B.L.3
  • 12
    • 0027218957 scopus 로고
    • Cloning, sequencing, and expression of the genes encoding subunits of Paracoccus denitrificans electron transfer flavoprotein
    • Bedzyk, L. A., K. W. Escudero, R. E. Gill, K. J. Griffin, and F. E. Frerman. 1993. Cloning, sequencing, and expression of the genes encoding subunits of Paracoccus denitrificans electron transfer flavoprotein. J. Biol. Chem. 268:20211-20217.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20211-20217
    • Bedzyk, L.A.1    Escudero, K.W.2    Gill, R.E.3    Griffin, K.J.4    Frerman, F.E.5
  • 14
    • 0026019614 scopus 로고
    • Nitric and nitrous oxide reductases are active under aerobic conditions in cells of Thiosphaera pantotropha
    • Bell, L. C., and S. J. Ferguson. 1991. Nitric and nitrous oxide reductases are active under aerobic conditions in cells of Thiosphaera pantotropha. Biochem. J. 273:423-427.
    • (1991) Biochem. J. , vol.273 , pp. 423-427
    • Bell, L.C.1    Ferguson, S.J.2
  • 15
    • 0027787624 scopus 로고
    • Insertion of transposon Tn5 into a structural gene of the membrane-bound nitrate reductase of Thiosphaera pantotropha results in anaerobic overexpression of periplasmic nitrate reductase activity
    • Bell, L. C., M. D. Page, B. C. Berks, D. J. Richardson, and S. J. Ferguson. 1993. Insertion of transposon Tn5 into a structural gene of the membrane-bound nitrate reductase of Thiosphaera pantotropha results in anaerobic overexpression of periplasmic nitrate reductase activity. J. Gen. Microbiol. 139:3205-3214.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 3205-3214
    • Bell, L.C.1    Page, M.D.2    Berks, B.C.3    Richardson, D.J.4    Ferguson, S.J.5
  • 16
    • 0025333241 scopus 로고
    • Periplasmic and membrane-bound respiratory nitrate reductases in Thiosphaera pantotropha. The periplasmic enzyme catalyzes the first step in aerobic denitrification
    • Bell, L. C., D. J. Richardson, and S. J. Ferguson. 1990. Periplasmic and membrane-bound respiratory nitrate reductases in Thiosphaera pantotropha. The periplasmic enzyme catalyzes the first step in aerobic denitrification. FEBS Lett. 265:85-87.
    • (1990) FEBS Lett. , vol.265 , pp. 85-87
    • Bell, L.C.1    Richardson, D.J.2    Ferguson, S.J.3
  • 18
    • 0030016330 scopus 로고    scopus 로고
    • Structural investigation of the molybdenum site of the periplasmic nitrate reductase from Thiosphaera pantotropha by X-ray absorption spectroscopy
    • Bennett, B., J. M. Charnock, H. J. Sears, B. C. Berks, A. J. Thomson, S. J. Ferguson, C. D. Garner, and D. J. Richardson. 1996. Structural investigation of the molybdenum site of the periplasmic nitrate reductase from Thiosphaera pantotropha by X-ray absorption spectroscopy. Biochem. J. 317:557-563.
    • (1996) Biochem. J. , vol.317 , pp. 557-563
    • Bennett, B.1    Charnock, J.M.2    Sears, H.J.3    Berks, B.C.4    Thomson, A.J.5    Ferguson, S.J.6    Garner, C.D.7    Richardson, D.J.8
  • 20
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks, B. C. 1996. A common export pathway for proteins binding complex redox cofactors? Mol. Microbiol. 22:393-404.
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 21
    • 0027476458 scopus 로고
    • Purification and characterization of a nitrous oxide reductase from Thiosphaera pantotropha. Implications for the mechanism of aerobic nitrous oxide reduction
    • Berks, B. C., D. Baratta, J. Richardson, and S. J. Ferguson. 1993. Purification and characterization of a nitrous oxide reductase from Thiosphaera pantotropha. Implications for the mechanism of aerobic nitrous oxide reduction. Eur. J. Biochem. 212:467-476.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 467-476
    • Berks, B.C.1    Baratta, D.2    Richardson, J.3    Ferguson, S.J.4
  • 22
    • 0028811652 scopus 로고
    • Enzymes and associated electron transport systems that catalyze the respiratory reduction of nitrogen oxides and oxyanions
    • Berks, B. C., S. J. Ferguson, J. W. B. Moir, and D. J. Richardson. 1995. Enzymes and associated electron transport systems that catalyze the respiratory reduction of nitrogen oxides and oxyanions. Biochim. Biophys. Acta 1232:97-173.
    • (1995) Biochim. Biophys. Acta , vol.1232 , pp. 97-173
    • Berks, B.C.1    Ferguson, S.J.2    Moir, J.W.B.3    Richardson, D.J.4
  • 23
    • 0028944291 scopus 로고
    • Sequence analysis of subunits of the membrane-bound nitrate reductase from a denitrifying bacterium: The integral membrane subunit provides a prototype for the dihaem electron-carrying arm of a redox loop
    • Berks, B. C., M. D. Page, D. J. Richardson, A. Reilly, A. Cavill, F. Outen, and S. J. Ferguson. 1995. Sequence analysis of subunits of the membrane-bound nitrate reductase from a denitrifying bacterium: the integral membrane subunit provides a prototype for the dihaem electron-carrying arm of a redox loop. Mol. Microbiol. 15:319-331.
    • (1995) Mol. Microbiol. , vol.15 , pp. 319-331
    • Berks, B.C.1    Page, M.D.2    Richardson, D.J.3    Reilly, A.4    Cavill, A.5    Outen, F.6    Ferguson, S.J.7
  • 24
    • 0029160337 scopus 로고
    • The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha
    • Berks, B. C., D. J. Richardson, A. Reilly, A. C. Willis, and S. J. Ferguson. 1995. The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha. Biochem. J. 309:983-992.
    • (1995) Biochem. J. , vol.309 , pp. 983-992
    • Berks, B.C.1    Richardson, D.J.2    Reilly, A.3    Willis, A.C.4    Ferguson, S.J.5
  • 25
    • 0028098074 scopus 로고
    • Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha
    • Berks, B. C., D. J. Richardson, C. Robinson, A. Reilly, R. T. Aplin, and S. J. Ferguson. 1994. Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha. Eur. J. Biochem. 220:117-124.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 117-124
    • Berks, B.C.1    Richardson, D.J.2    Robinson, C.3    Reilly, A.4    Aplin, R.T.5    Ferguson, S.J.6
  • 29
    • 0025765210 scopus 로고
    • A direct demonstration of "co-respiration" of oxygen and nitrogen oxides by Pseudomonas nautica: Some spectral and kinetic properties of the respiratory components
    • Bonin, P., and M. Gilewicz. 1991. A direct demonstration of "co-respiration" of oxygen and nitrogen oxides by Pseudomonas nautica: some spectral and kinetic properties of the respiratory components. FEMS Microbiol. Lett. 80:183-188.
    • (1991) FEMS Microbiol. Lett. , vol.80 , pp. 183-188
    • Bonin, P.1    Gilewicz, M.2
  • 30
    • 0018875128 scopus 로고
    • Electron transport to nitrous oxide in Paracoccus denitrificans
    • Boogerd, F. C., H. W. van Verseveld, and A. H. Stouthamer. 1980. Electron transport to nitrous oxide in Paracoccus denitrificans. FEBS Lett. 113:279-284
    • (1980) FEBS Lett. , vol.113 , pp. 279-284
    • Boogerd, F.C.1    Van Verseveld, H.W.2    Stouthamer, A.H.3
  • 31
    • 0031936259 scopus 로고    scopus 로고
    • The ATP synthase atpHAGDC (F-1) operon from Rhodobacter capsulatus
    • Borghese, R., M. Crimi, L. Fava, and B. A. Melandri. 1998. The ATP synthase atpHAGDC (F-1) operon from Rhodobacter capsulatus. J. Bacteriol. 180:416-421.
    • (1998) J. Bacteriol. , vol.180 , pp. 416-421
    • Borghese, R.1    Crimi, M.2    Fava, L.3    Melandri, B.A.4
  • 32
    • 3743116288 scopus 로고
    • Ph.D. thesis. Vrije Universiteit, Amsterdam, The Netherlands
    • Bosma, G. 1989. Ph.D. thesis. Vrije Universiteit, Amsterdam, The Netherlands.
    • (1989)
    • Bosma, G.1
  • 33
    • 0023265673 scopus 로고
    • Subfractionation and characterization of soluble c-type cytochromes from Paracoccus denitrificans cultured under various limiting conditions in the chemostat
    • Bosma, G., M. Braster, A. H. Stouthamer, and H. W. van Verseveld. 1987. Subfractionation and characterization of soluble c-type cytochromes from Paracoccus denitrificans cultured under various limiting conditions in the chemostat. Eur. J. Biochem. 165:665-670.
    • (1987) Eur. J. Biochem. , vol.165 , pp. 665-670
    • Bosma, G.1    Braster, M.2    Stouthamer, A.H.3    Van Verseveld, H.W.4
  • 34
    • 0026516423 scopus 로고
    • The structural genes of the nitric oxide reductase complex from Pseudomonas stutzeri are part of a 30-kilobase gene cluster for denitrification
    • Braun, C., and W. G. Zumft. 1992. The structural genes of the nitric oxide reductase complex from Pseudomonas stutzeri are part of a 30-kilobase gene cluster for denitrification. J. Bacteriol. 174:2394-2397.
    • (1992) J. Bacteriol. , vol.174 , pp. 2394-2397
    • Braun, C.1    Zumft, W.G.2
  • 35
    • 0028238591 scopus 로고
    • Characterization of the paramagnetic iron-containing redox centres of Thiosphaera pantotropha periplasmic nitrate reductase
    • Breton, J., B. C. Berks, A. Reilly, A. J. Thomson, S. J. Ferguson, and D. J. Richardson. 1994. Characterization of the paramagnetic iron-containing redox centres of Thiosphaera pantotropha periplasmic nitrate reductase. FEBS Lett. 345:76-80.
    • (1994) FEBS Lett. , vol.345 , pp. 76-80
    • Breton, J.1    Berks, B.C.2    Reilly, A.3    Thomson, A.J.4    Ferguson, S.J.5    Richardson, D.J.6
  • 36
    • 0029948486 scopus 로고    scopus 로고
    • Temperature-dependence of open-complex formation at two Escherichia coli promoters with extended - 10 sequences
    • Burns, H. D., T. A. Belyaeva, S. J. W. Busby, and S. D. Minchin. 1996. Temperature-dependence of open-complex formation at two Escherichia coli promoters with extended - 10 sequences. Biochem. J. 317:305-311.
    • (1996) Biochem. J. , vol.317 , pp. 305-311
    • Burns, H.D.1    Belyaeva, T.A.2    Busby, S.J.W.3    Minchin, S.D.4
  • 37
    • 0029773417 scopus 로고    scopus 로고
    • Purification and activities of the Rhodobacter capsulatus RpoN (sigma(N)) protein
    • Cannon, W., S. Missailidis, S. Austin, M. Moore, A. Drake, and M. Buck. 1996. Purification and activities of the Rhodobacter capsulatus RpoN (sigma(N)) protein. Mol. Microbiol. 21:233-245.
    • (1996) Mol. Microbiol. , vol.21 , pp. 233-245
    • Cannon, W.1    Missailidis, S.2    Austin, S.3    Moore, M.4    Drake, A.5    Buck, M.6
  • 38
    • 0025322981 scopus 로고
    • Structure and function of cytochrome c oxidase
    • Capaldi, R. A. 1990. Structure and function of cytochrome c oxidase. Annu. Rev. Biochem. 59:569-596.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 569-596
    • Capaldi, R.A.1
  • 39
    • 0025248146 scopus 로고
    • Nitric oxide formed by nitrite reductase of Paracoccus denitrificans is sufficiently stable to inhibit cytochrome oxidase activity and is reduced by its reductase under aerobic conditions
    • Carr, G. J., and S. J. Ferguson. 1990. Nitric oxide formed by nitrite reductase of Paracoccus denitrificans is sufficiently stable to inhibit cytochrome oxidase activity and is reduced by its reductase under aerobic conditions. Biochim. Biophys. Acta 1017:57-62.
    • (1990) Biochim. Biophys. Acta , vol.1017 , pp. 57-62
    • Carr, G.J.1    Ferguson, S.J.2
  • 40
    • 0024969601 scopus 로고
    • The energy conserving nitric oxide reductase system in Paracoccus denitrificans: Distinction from the nitrite reductase that catalyses synthesis of nitric oxide and evidence from trapping experiments for nitric oxide as a free intermediate during denitrification
    • Carr, G. J., M. D. Page, and S. J. Ferguson. 1989. The energy conserving nitric oxide reductase system in Paracoccus denitrificans: distinction from the nitrite reductase that catalyses synthesis of nitric oxide and evidence from trapping experiments for nitric oxide as a free intermediate during denitrification. Eur. J. Biochem. 179:683-692.
    • (1989) Eur. J. Biochem. , vol.179 , pp. 683-692
    • Carr, G.J.1    Page, M.D.2    Ferguson, S.J.3
  • 42
    • 0028239826 scopus 로고
    • Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen
    • Castresana, J., M. Lubben, M. Saraste, and D. G. Higgins. 1994. Evolution of cytochrome oxidase, an enzyme older than atmospheric oxygen. EMBO J. 13:2516-2525.
    • (1994) EMBO J. , vol.13 , pp. 2516-2525
    • Castresana, J.1    Lubben, M.2    Saraste, M.3    Higgins, D.G.4
  • 43
    • 0022596236 scopus 로고
    • Tn5-induced mutations affecting sulfur-oxidizing ability (Sox) of Thiosphaera pantotropha
    • Chandra, T. S., and C. G. Friedrich. 1986. Tn5-induced mutations affecting sulfur-oxidizing ability (Sox) of Thiosphaera pantotropha. J. Bacteriol. 166: 446-452.
    • (1986) J. Bacteriol. , vol.166 , pp. 446-452
    • Chandra, T.S.1    Friedrich, C.G.2
  • 44
    • 0026437717 scopus 로고
    • Discovery and characterization of a new transposable element, Tn4811, in Streptomyces lividans 66
    • Chen, C. W., T. W. Yu, H. M. Chung, and C. F. Chon. 1992. Discovery and characterization of a new transposable element, Tn4811, in Streptomyces lividans 66. J. Bacteriol. 174:7762-7769.
    • (1992) J. Bacteriol. , vol.174 , pp. 7762-7769
    • Chen, C.W.1    Yu, T.W.2    Chung, H.M.3    Chon, C.F.4
  • 46
    • 0026785015 scopus 로고
    • Three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans determined by molecular replacement at 2.8 A resolution
    • Chen, L., F. S. Mathews, V. L. Davidson, E. G. Huizinga, F. M. Vellieux, and W. G. Hol. 1992. Three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans determined by molecular replacement at 2.8 A resolution. Proteins 14:288-299.
    • (1992) Proteins , vol.14 , pp. 288-299
    • Chen, L.1    Mathews, F.S.2    Davidson, V.L.3    Huizinga, E.G.4    Vellieux, F.M.5    Hol, W.G.6
  • 48
    • 0026720414 scopus 로고
    • The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans
    • Chistoserdov, A. Y., J. Boyd, F. S. Mathews, and M. E. Lidstrom. 1992. The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans. Biochem. Biophys. Res. Commun. 184:1181-1189.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 1181-1189
    • Chistoserdov, A.Y.1    Boyd, J.2    Mathews, F.S.3    Lidstrom, M.E.4
  • 49
    • 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., L. V. Chistoserdova, W. S. McIntire, and M. E. Lidstrom. 1994. Genetic organization of the mau gene cluster in Methylobacterium extorquens AM1: complete nucleotide sequence and generation and characteristics of mau mutants. J. Bacteriol. 176:4052-4065.
    • (1994) J. Bacteriol. , vol.176 , pp. 4052-4065
    • Chistoserdov, A.Y.1    Chistoserdova, L.V.2    McIntire, W.S.3    Lidstrom, M.E.4
  • 50
    • 0027227558 scopus 로고
    • A family of IS1031 elements in the genome of Acetobacter xylinum: Nucleotide sequences and strain distribution
    • Coucheron, D. H. 1993. A family of IS1031 elements in the genome of Acetobacter xylinum: nucleotide sequences and strain distribution. Mol. Microbiol. 9:211-218.
    • (1993) Mol. Microbiol. , vol.9 , pp. 211-218
    • Coucheron, D.H.1
  • 51
    • 0018117629 scopus 로고
    • The variable cytochrome content of Paracoccus denitrificans grown aerobically under different conditions
    • Cox, J. C., W. J. Ingledew, B. A. Haddock, and H. G. Lawford. 1978. The variable cytochrome content of Paracoccus denitrificans grown aerobically under different conditions. FEBS Lett. 93:261-265.
    • (1978) FEBS Lett. , vol.93 , pp. 261-265
    • Cox, J.C.1    Ingledew, W.J.2    Haddock, B.A.3    Lawford, H.G.4
  • 52
    • 3743141905 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 53
    • 0025030202 scopus 로고
    • Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans fragment carrying eight genes involved in transformation of precorrin 2 to cobyrinic acid
    • Crouzet, J., B. Cameron, L. Cauchois, S. Rigault, M. C. Rouyez, F. Blanche, D. Thibaut, and L. Debussche. 1990. Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans fragment carrying eight genes involved in transformation of precorrin 2 to cobyrinic acid. J. Bacteriol. 172:5980-5990.
    • (1990) J. Bacteriol. , vol.172 , pp. 5980-5990
    • Crouzet, J.1    Cameron, B.2    Cauchois, L.3    Rigault, S.4    Rouyez, M.C.5    Blanche, F.6    Thibaut, D.7    Debussche, L.8
  • 54
    • 0030876450 scopus 로고    scopus 로고
    • Characterization of the Rhodobacter capsulatus housekeeping RNA polymerase
    • Cullen, P. J., K. J. Kaufman, W. C. Bowman, and R. G. Kranz. 1997. Characterization of the Rhodobacter capsulatus housekeeping RNA polymerase. J. Biol. Chem. 272:27266-27273.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27266-27273
    • Cullen, P.J.1    Kaufman, K.J.2    Bowman, W.C.3    Kranz, R.G.4
  • 55
    • 0026700226 scopus 로고
    • NosR, a membrane-bound regulatory component necessary for expression of nitrous oxide reductase in denitrifying Pseudomonas stutzeri
    • Cuypers, H., A. Viebrock-Sambale, and W. G. Zumft. 1992. NosR, a membrane-bound regulatory component necessary for expression of nitrous oxide reductase in denitrifying Pseudomonas stutzeri. J. Bacteriol. 174:5332-5339.
    • (1992) J. Bacteriol. , vol.174 , pp. 5332-5339
    • Cuypers, H.1    Viebrock-Sambale, A.2    Zumft, W.G.3
  • 56
    • 0022623068 scopus 로고
    • Electron transfer flavoprotein from Methylophilus methylotrophus: Properties, comparison with other electron transfer flavoproteins, and regulation of expression by carbon source
    • Davidson, V. L., M. Husain, and J. W. Neher. 1986. Electron transfer flavoprotein from Methylophilus methylotrophus: properties, comparison with other electron transfer flavoproteins, and regulation of expression by carbon source. J. Bacteriol. 166:812-817.
    • (1986) J. Bacteriol. , vol.166 , pp. 812-817
    • Davidson, V.L.1    Husain, M.2    Neher, J.W.3
  • 57
    • 0024968255 scopus 로고
    • 550 mediates electron transfer from inducible periplasmic c-type cytochromes to the cytoplasmic membrane of Paracoccus denitrificans
    • 550 mediates electron transfer from inducible periplasmic c-type cytochromes to the cytoplasmic membrane of Paracoccus denitrificans. FEBS Lett. 245:271-273.
    • (1989) FEBS Lett. , vol.245 , pp. 271-273
    • Davidson, V.L.1    Kumar, M.A.2
  • 58
    • 0024427349 scopus 로고
    • The effect of oxygen on denitrification in Paracoccus denitrificans and Pseudomonas aeruginosa
    • Davies, K. J., D. Lloyd, and L. Boddy. 1989. The effect of oxygen on denitrification in Paracoccus denitrificans and Pseudomonas aeruginosa. J. Gen. Microbiol. 135:2445-2451.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 2445-2451
    • Davies, K.J.1    Lloyd, D.2    Boddy, L.3
  • 59
    • 0028580539 scopus 로고
    • Isolation, sequencing and mutational analysis of a gene cluster involved in nitrite reduction in Paracoccus denitrificans
    • de Boer, A. P. N., W. N. M. Reijnders, J. G. Kuenen, A. H. Stouthamer, and R. J. M. van Spanning. 1994. Isolation, sequencing and mutational analysis of a gene cluster involved in nitrite reduction in Paracoccus denitrificans. Antonie Leeuwenhoek 66:111-127.
    • (1994) Antonie Leeuwenhoek , vol.66 , pp. 111-127
    • De Boer, A.P.N.1    Reijnders, W.N.M.2    Kuenen, J.G.3    Stouthamer, A.H.4    Van Spanning, R.J.M.5
  • 61
    • 3743086268 scopus 로고
    • Ph.D. thesis. Vrije Universiteit, Amsterdam, The Netherlands
    • de Gier, J. W. L. 1995. Ph.D. thesis. Vrije Universiteit, Amsterdam, The Netherlands.
    • (1995)
    • De Gier, J.W.L.1
  • 65
    • 0030999726 scopus 로고    scopus 로고
    • Expression of the mau gene cluster of Paracoccus denitrificans is controlled by MauR and a second transcription regulator
    • Delorme, C., T. T. Huisman, W. N. M. Reijnders, Y. L. Chan, N. Harms, A. H. Stouthamer, and R. J. M. van Spanning. 1997. Expression of the mau gene cluster of Paracoccus denitrificans is controlled by MauR and a second transcription regulator. Microbiology 143:793-801.
    • (1997) Microbiology , vol.143 , pp. 793-801
    • Delorme, C.1    Huisman, T.T.2    Reijnders, W.N.M.3    Chan, Y.L.4    Harms, N.5    Stouthamer, A.H.6    Van Spanning, R.J.M.7
  • 66
    • 0030847107 scopus 로고    scopus 로고
    • A new non-heme iron environment in Paracoccus denitrificans adenylate kinase studied by electron paramagnetic resonance and electron spin echo envelope modulation spectroscopy
    • Deligiannakis, Y., A. Boussac, H. Botin, V. Perrier, O. Barzu, and A. M. Giles. 1997. A new non-heme iron environment in Paracoccus denitrificans adenylate kinase studied by electron paramagnetic resonance and electron spin echo envelope modulation spectroscopy. Biochemistry 361:9446-9452.
    • (1997) Biochemistry , vol.361 , pp. 9446-9452
    • Deligiannakis, Y.1    Boussac, A.2    Botin, H.3    Perrier, V.4    Barzu, O.5    Giles, A.M.6
  • 67
    • 0025611032 scopus 로고
    • Nucleotide sequence of IS427 and its target sites in Agrobacterium tumefaciens T37
    • de Miersman, C., C. van Soom, C. Verreth, A. van Gool, and J. Vanderleyden. 1990. Nucleotide sequence of IS427 and its target sites in Agrobacterium tumefaciens T37. Plasmid 24:227-234.
    • (1990) Plasmid , vol.24 , pp. 227-234
    • De Miersman, C.1    Van Soom, C.2    Verreth, C.3    Van Gool, A.4    Vanderleyden, J.5
  • 68
    • 0001888973 scopus 로고
    • Isolation and characterization of Paracoccus denitrificans mutants with increased conjugation frequencies and pleiotropic loss of a (nGATCn)-DNA-modifying property
    • de Vries, G. E., N. Harms, J. Hoogendijk, and A. H. Stouthamer. 1989. Isolation and characterization of Paracoccus denitrificans mutants with increased conjugation frequencies and pleiotropic loss of a (nGATCn)-DNA-modifying property. Arch. Microbiol. 152:52-57.
    • (1989) Arch. Microbiol. , vol.152 , pp. 52-57
    • De Vries, G.E.1    Harms, N.2    Hoogendijk, J.3    Stouthamer, A.H.4
  • 71
    • 0027360463 scopus 로고
    • Identification of cis acting regulatory regions upstream of the rRNA operons of Rhodobacter sphaeroides
    • Dryden, S. C., and S. Kaplan. 1993. Identification of cis acting regulatory regions upstream of the rRNA operons of Rhodobacter sphaeroides. J. Bacteriol. 175:6392-6402.
    • (1993) J. Bacteriol. , vol.175 , pp. 6392-6402
    • Dryden, S.C.1    Kaplan, S.2
  • 72
    • 0026564513 scopus 로고
    • Transcriptional analysis and promoter mapping of the fdxA gene which encodes the 7Fe ferredoxin (FdII) of Rhodobacter capsulatus
    • Duport, C., Y. Jouanneau, and P. M. Vignais. 1992. Transcriptional analysis and promoter mapping of the fdxA gene which encodes the 7Fe ferredoxin (FdII) of Rhodobacter capsulatus. Mol. Gen. Genet. 231:323-328.
    • (1992) Mol. Gen. Genet. , vol.231 , pp. 323-328
    • Duport, C.1    Jouanneau, Y.2    Vignais, P.M.3
  • 73
    • 0027481125 scopus 로고
    • Crystal structure analysis of amicyanin and apoamicyanin from Paracoccus denitrificans at 2.0 A and 1.8 A resolution
    • Durley, R., L. Chen, L. W. Lim, F. S. Mathews, and V. L. Davidson. 1993. Crystal structure analysis of amicyanin and apoamicyanin from Paracoccus denitrificans at 2.0 A and 1.8 A resolution. Protein Sci. 2:739-752.
    • (1993) Protein Sci. , vol.2 , pp. 739-752
    • Durley, R.1    Chen, L.2    Lim, L.W.3    Mathews, F.S.4    Davidson, V.L.5
  • 74
    • 0344312436 scopus 로고    scopus 로고
    • The Paracoccus denitrificans electron transport system: Aspects of organization, structures and biogenesis
    • Ferguson, S. J. 1998. The Paracoccus denitrificans electron transport system: aspects of organization, structures and biogenesis. NATO ASI Ser. c512:77-88.
    • (1998) NATO ASI Ser. , vol.C512 , pp. 77-88
    • Ferguson, S.J.1
  • 75
    • 0000670332 scopus 로고
    • Anaerobic respiration in the Rhodospirillaceae: Characterisation of pathways and evaluation of roles in redox balancing during photosynthesis
    • Ferguson, S. J., J. B. Jackson, and A. G. McEwan. 1987. Anaerobic respiration in the Rhodospirillaceae: characterisation of pathways and evaluation of roles in redox balancing during photosynthesis. FEMS Microbiol. Rev. 46:117-143.
    • (1987) FEMS Microbiol. Rev. , vol.46 , pp. 117-143
    • Ferguson, S.J.1    Jackson, J.B.2    McEwan, A.G.3
  • 76
    • 0031043629 scopus 로고    scopus 로고
    • Cloning and characterization of the recA gene of Paracoccus denitrificans and construction of a rec4-deficient mutant
    • Fernandez de Henestrosa, A. R., A. del Rey, R. Tarraga, and J. Barbé. 1997. Cloning and characterization of the recA gene of Paracoccus denitrificans and construction of a rec4-deficient mutant. FEMS Microbiol. Lett. 147: 209-213.
    • (1997) FEMS Microbiol. Lett. , vol.147 , pp. 209-213
    • Fernandez De Henestrosa, A.R.1    Del Rey, A.2    Tarraga, R.3    Barbé, J.4
  • 78
    • 0025734539 scopus 로고
    • Nucleotide sequence of IS402 from Pseudomonas cepacia
    • Ferrante, A. A., and T. G. Lessie. 1991. Nucleotide sequence of IS402 from Pseudomonas cepacia. Gene 102:143-144.
    • (1991) Gene , vol.102 , pp. 143-144
    • Ferrante, A.A.1    Lessie, T.G.2
  • 79
    • 0027476313 scopus 로고
    • Porphyrobacter neustonensis gen. nov., sp. nov., an aerobic bacteriochlorophyll-synthesizing budding bacterium from freshwater
    • Feurst, J. A., J. A. Hawkins, A. Holmes, L. I. Sly, C. Moore, and E. Stackebrandt. 1993. Porphyrobacter neustonensis gen. nov., sp. nov., an aerobic bacteriochlorophyll-synthesizing budding bacterium from freshwater. Int. J. Syst. Bacteriol. 43:125-134.
    • (1993) Int. J. Syst. Bacteriol. , vol.43 , pp. 125-134
    • Feurst, J.A.1    Hawkins, J.A.2    Holmes, A.3    Sly, L.I.4    Moore, C.5    Stackebrandt, E.6
  • 80
    • 0030775370 scopus 로고    scopus 로고
    • Transcriptional control of several aerobically induced cytochrome structural genes in Rhodobacter sphaeroides
    • Flory, J. E., and T. J. Donohue. 1997. Transcriptional control of several aerobically induced cytochrome structural genes in Rhodobacter sphaeroides. Microbiology 143:3101-3110.
    • (1997) Microbiology , vol.143 , pp. 3101-3110
    • Flory, J.E.1    Donohue, T.J.2
  • 81
    • 0029149361 scopus 로고
    • Organization and expression of the Rhodobacter sphaeroides cycFG operon
    • Flory, J. E., and T. J. Donohue. 1995. Organization and expression of the Rhodobacter sphaeroides cycFG operon. J. Bacteriol. 177:4311-4320.
    • (1995) J. Bacteriol. , vol.177 , pp. 4311-4320
    • Flory, J.E.1    Donohue, T.J.2
  • 82
    • 0029895607 scopus 로고    scopus 로고
    • Promoter analysis of the catalase-peroxidase gene (cpeA) from Rhodobacter capsulatus
    • Forkl, H., G. Drews, and M. H. Tadros. 1996. Promoter analysis of the catalase-peroxidase gene (cpeA) from Rhodobacter capsulatus. FEMS Microbiol. Lett. 137:169-174.
    • (1996) FEMS Microbiol. Lett. , vol.137 , pp. 169-174
    • Forkl, H.1    Drews, G.2    Tadros, M.H.3
  • 83
    • 0028085897 scopus 로고
    • The Rhodobacter capsulatus glnB gene is regulated by NtrC at tandem rpoN-independent promoters
    • Foster-Hartnett, D., and R. G. Kranz. 1994. The Rhodobacter capsulatus glnB gene is regulated by NtrC at tandem rpoN-independent promoters. J. Bacteriol. 176:5171-5176.
    • (1994) J. Bacteriol. , vol.176 , pp. 5171-5176
    • Foster-Hartnett, D.1    Kranz, R.G.2
  • 84
    • 3743132045 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 86
    • 0023832706 scopus 로고
    • A bacteriophage T4 expression cassette that functions efficiently in a wide range of gram-negative bacteria
    • Frey, J., E. A. Mudd, and H. M. Krisch. 1988. A bacteriophage T4 expression cassette that functions efficiently in a wide range of gram-negative bacteria. Gene 62:237-247.
    • (1988) Gene , vol.62 , pp. 237-247
    • Frey, J.1    Mudd, E.A.2    Krisch, H.M.3
  • 87
    • 0000799836 scopus 로고
    • Oxidation of thiosulfate by Paracoccus denitrificans and other hydrogen bacteria
    • Friedrich, C. G., and G. Mitrenga. 1981. Oxidation of thiosulfate by Paracoccus denitrificans and other hydrogen bacteria. FEMS Microbiol. Lett. 10:209-212.
    • (1981) FEMS Microbiol. Lett. , vol.10 , pp. 209-212
    • Friedrich, C.G.1    Mitrenga, G.2
  • 89
    • 0028174805 scopus 로고
    • 3 gene regulation in members of the family Rhizobiaceae: Comparison of copper and oxygen effects in Bradyrhizobium japonicum and Rhizobium tropici
    • 3 gene regulation in members of the family Rhizobiaceae: comparison of copper and oxygen effects in Bradyrhizobium japonicum and Rhizobium tropici. Appl. Environ. Microbiol. 60:141-148.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 141-148
    • Gabel, C.1    Bittinger, M.A.2    Maier, R.J.3
  • 91
    • 0002734187 scopus 로고
    • Bacterial insertion sequences
    • D. E. Berg and M. M. Howe (ed.) American Society for Microbiology, Washington, D.C.
    • Galas, D. J., and M. Chandler. 1989. Bacterial insertion sequences, p. 109-162. In D. E. Berg and M. M. Howe (ed.), Mobile DNA. American Society for Microbiology, Washington, D.C.
    • (1989) Mobile DNA , pp. 109-162
    • Galas, D.J.1    Chandler, M.2
  • 94
    • 0024008339 scopus 로고
    • 2 fixation genes within two gene clusters in Rhodobacter sphaeroides
    • 2 fixation genes within two gene clusters in Rhodobacter sphaeroides. J. Bacteriol. 170:2153-2158.
    • (1988) J. Bacteriol. , vol.170 , pp. 2153-2158
    • Gibson, J.L.1    Tabita, F.R.2
  • 95
    • 0026564374 scopus 로고
    • A putative anaerobic coproporphyrinogen III oxidase in Rhodobacter sphaeroides. II. Analysis of a region of the genome encoding hemF and the puc operon
    • Gibson, L. C., P. McGlynn, M. Chaudhri, and C. N. Hunter. 1992. A putative anaerobic coproporphyrinogen III oxidase in Rhodobacter sphaeroides. II. Analysis of a region of the genome encoding hemF and the puc operon. Mol. Microbiol. 6:3171-3186.
    • (1992) Mol. Microbiol. , vol.6 , pp. 3171-3186
    • Gibson, L.C.1    McGlynn, P.2    Chaudhri, M.3    Hunter, C.N.4
  • 96
    • 0020339029 scopus 로고
    • Homologies between different prokaryotic DNA-binding regulatory proteins and between their sites of action
    • Gicquel-Sanzey, B., and P. Cossart. 1982. Homologies between different prokaryotic DNA-binding regulatory proteins and between their sites of action. EMBO J. 1:591-595.
    • (1982) EMBO J. , vol.1 , pp. 591-595
    • Gicquel-Sanzey, B.1    Cossart, P.2
  • 97
    • 0031028099 scopus 로고    scopus 로고
    • Purification and initial kinetic and spectroscopic characterization of NO reductase from Paracoccus denitrificans
    • Girsch, P., and S. de Vries. 1997. Purification and initial kinetic and spectroscopic characterization of NO reductase from Paracoccus denitrificans. Biochim. Biophys. Acta 1318:202-216.
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 202-216
    • Girsch, P.1    De Vries, S.2
  • 98
    • 0029970728 scopus 로고    scopus 로고
    • Sequence analysis of an internal 9.72 kb segment from the 30 kb denitrification gene cluster of Pseudomonas stutzeri
    • Glockner, A. B., and W. G. Zumft. 1996. Sequence analysis of an internal 9.72 kb segment from the 30 kb denitrification gene cluster of Pseudomonas stutzeri. Biochim. Biophys. Acta 1277:6-12.
    • (1996) Biochim. Biophys. Acta , vol.1277 , pp. 6-12
    • Glockner, A.B.1    Zumft, W.G.2
  • 99
    • 0030897302 scopus 로고    scopus 로고
    • Projection structure of the cytochrome bo ubiquinol oxidase from Escherichia colt at 6 Å resolution
    • Gohlke, U., A. Warne, and M. Saraste. 1997. Projection structure of the cytochrome bo ubiquinol oxidase from Escherichia colt at 6 Å resolution. EMBO J. 16:1181-1188.
    • (1997) EMBO J. , vol.16 , pp. 1181-1188
    • Gohlke, U.1    Warne, A.2    Saraste, M.3
  • 100
    • 0029927350 scopus 로고    scopus 로고
    • The Rhodobacter sphaeroides 2.4.1 rho gene: Expression and genetic analysis of structure and function
    • Gomelsky, M., and S. Kaplan. 1996. The Rhodobacter sphaeroides 2.4.1 rho gene: expression and genetic analysis of structure and function. J. Bacteriol. 178:1946-1954.
    • (1996) J. Bacteriol. , vol.178 , pp. 1946-1954
    • Gomelsky, M.1    Kaplan, S.2
  • 101
    • 0029659242 scopus 로고    scopus 로고
    • Identifying numerically abundant culturable bacteria from complex communities: An example from a lignin enrichment culture
    • Gonzalez, J. M., W. B. Whitman, R. E. Hodson, and M. A. Moran. 1996. Identifying numerically abundant culturable bacteria from complex communities: an example from a lignin enrichment culture. Appl. Environ. Microbiol. 62:4433-4440.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4433-4440
    • Gonzalez, J.M.1    Whitman, W.B.2    Hodson, R.E.3    Moran, M.A.4
  • 103
    • 0023849730 scopus 로고
    • Trapping of nitric oxide produced during denitrification by extracellular hemoglobin
    • Goretski, J., and T. C. Hollocher. 1988. Trapping of nitric oxide produced during denitrification by extracellular hemoglobin. J. Biol. Chem. 263:2316-2323.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2316-2323
    • Goretski, J.1    Hollocher, T.C.2
  • 105
    • 0029797082 scopus 로고    scopus 로고
    • Reconstitution of the [4Fe-4S] cluster in FNR and demonstration of the aerobic-anaerobic transcription switch in vitro
    • Green, J., B. Bennett, P. Jordan, E. T. Ralph, A. J. Thomson, and J. R. Guest. 1996. Reconstitution of the [4Fe-4S] cluster in FNR and demonstration of the aerobic-anaerobic transcription switch in vitro. Biochem. J. 316:887-892.
    • (1996) Biochem. J. , vol.316 , pp. 887-892
    • Green, J.1    Bennett, B.2    Jordan, P.3    Ralph, E.T.4    Thomson, A.J.5    Guest, J.R.6
  • 106
    • 0030458408 scopus 로고    scopus 로고
    • Functional Escherichia coli 23S rRNAs containing processed and unprocessed intervening sequences from Salmonella typhimurium
    • Gregory, S., M. O'Connor, and A. Dahlberg. 1996. Functional Escherichia coli 23S rRNAs containing processed and unprocessed intervening sequences from Salmonella typhimurium. Nucleic Acids Res. 24:4918-4923.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4918-4923
    • Gregory, S.1    O'Connor, M.2    Dahlberg, A.3
  • 107
    • 0031050795 scopus 로고    scopus 로고
    • 70-type sigma factors of group 1 and group 2
    • 70-type sigma factors of group 1 and group 2. J. Bacteriol. 179:1734-1747.
    • (1997) J. Bacteriol. , vol.179 , pp. 1734-1747
    • Gruber, T.M.1    Bryant, D.A.2
  • 108
    • 0027989421 scopus 로고
    • Aerobic-anaerobic gene regulation in Escherichia coli: Control by the ArcAB and Fnr regulons
    • Gunsalus, R. P., and S. J. Park. 1994. Aerobic-anaerobic gene regulation in Escherichia coli: control by the ArcAB and Fnr regulons. Res. Microbiol. 145:437-450.
    • (1994) Res. Microbiol. , vol.145 , pp. 437-450
    • Gunsalus, R.P.1    Park, S.J.2
  • 109
    • 0024845389 scopus 로고
    • Deletion of the gene for subumt III leads to defective assembly of bacterial cytochrome oxidase
    • Haltia, T., M. Finel, N. Harms, T. Nakari, M. Raitio, M. Wikstrom, and M. Saraste. 1989. Deletion of the gene for subumt III leads to defective assembly of bacterial cytochrome oxidase. EMBO J. 8:3571-3579.
    • (1989) EMBO J. , vol.8 , pp. 3571-3579
    • Haltia, T.1    Finel, M.2    Harms, N.3    Nakari, T.4    Raitio, M.5    Wikstrom, M.6    Saraste, M.7
  • 111
    • 0028038094 scopus 로고
    • Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans
    • Haltia, T., N. Semo, J. L. R. Arrondo, F. M. Goin, and E. Freire. 1994. Thermodynamic and structural stability of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 33:9731-9741.
    • (1994) Biochemistry , vol.33 , pp. 9731-9741
    • Haltia, T.1    Semo, N.2    Arrondo, J.L.R.3    Goin, F.M.4    Freire, E.5
  • 113
    • 0031776637 scopus 로고    scopus 로고
    • Paracoccus marcusii sp. nov., an orange gram-negative coccus
    • Harker, M., J. Hirschberg, and A. Oren.. 1998. Paracoccus marcusii sp. nov., an orange gram-negative coccus. Int. J. Syst. Bacteriol. 48:543-548.
    • (1998) Int. J. Syst. Bacteriol. , vol.48 , pp. 543-548
    • Harker, M.1    Hirschberg, J.2    Oren, A.3
  • 114
    • 3743077304 scopus 로고
    • Ph.D. thesis. Vrije Universiteit, Amsterdam, The Netherlands
    • Harms, N. 1988. Ph.D. thesis. Vrije Universiteit, Amsterdam, The Netherlands.
    • (1988)
    • Harms, N.1
  • 115
    • 0023407051 scopus 로고
    • Isolation and nucleotide sequence of the methanol dehydrogenase structural gene from Paracoccus denitrificans
    • Harms, N., G. E. de Vries, K. Maurer, J. Hoogendjjk, and A. H. Stouthamer. 1987. Isolation and nucleotide sequence of the methanol dehydrogenase structural gene from Paracoccus denitrificans. J. Bacteriol. 169:3969-3975.
    • (1987) J. Bacteriol. , vol.169 , pp. 3969-3975
    • Harms, N.1    De Vries, G.E.2    Maurer, K.3    Hoogendjjk, J.4    Stouthamer, A.H.5
  • 116
    • 0022356548 scopus 로고
    • Isolation and characterization of Paracoccus denitrificans mutants with defects in the metabolism of one-carbon compounds
    • Harms, N., G. E. de-Vries, K. Maurer, E. Veltkamp, and A. H. Stouthamer. 1985. Isolation and characterization of Paracoccus denitrificans mutants with defects in the metabolism of one-carbon compounds. J. Bacteriol. 164:1064-1070.
    • (1985) J. Bacteriol. , vol.164 , pp. 1064-1070
    • Harms, N.1    De-Vries, G.E.2    Maurer, K.3    Veltkamp, E.4    Stouthamer, A.H.5
  • 117
    • 0002294902 scopus 로고    scopus 로고
    • Genetics of C1 metabolism regulation in Paracoccus denitrificans
    • M. E. Lidstrom and F. R. Tabita (ed.) Kluwer Academic Publishers, Delft, The Netherlands
    • Harms, N., J. Ras, S. Koning, W. M. N. Reijnders, A. H. Stouthamer, and R. J. M. van Spanning. 1996. Genetics of C1 metabolism regulation in Paracoccus denitrificans, p. 126-132. In M. E. Lidstrom and F. R. Tabita (ed.), Microbial growth on C1 compounds. Kluwer Academic Publishers, Delft, The Netherlands.
    • (1996) Microbial Growth on C1 Compounds , pp. 126-132
    • Harms, N.1    Ras, J.2    Koning, S.3    Reijnders, W.M.N.4    Stouthamer, A.H.5    Van Spanning, R.J.M.6
  • 118
    • 0029967019 scopus 로고    scopus 로고
    • S-Formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: A universal pathway for formaldehyde detoxification
    • Harms, N., J. Ras, W. N. Reijnders, R. J. M. van Spanning, and A. H. Stouthamer. 1996. S-Formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification. J. Bacteriol. 178:6296-6299.
    • (1996) J. Bacteriol. , vol.178 , pp. 6296-6299
    • Harms, N.1    Ras, J.2    Reijnders, W.N.3    Van Spanning, R.J.M.4    Stouthamer, A.H.5
  • 120
    • 0025921657 scopus 로고
    • C1 metabolism in Paracoccus denitrificans: Genetics of Paracoccus denitrificans
    • Harms, N., and R. J. M. van Spanning. 1991. C1 metabolism in Paracoccus denitrificans: genetics of Paracoccus denitrificans. J. Bioenerg. Biomembr. 23:187-210.
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 187-210
    • Harms, N.1    Van Spanning, R.J.M.2
  • 121
    • 0021111879 scopus 로고
    • Compilation and analysis of Escherichia coli promoter DNA sequences
    • Hawley, D. K., and W. R. McClure. 1983. Compilation and analysis of Escherichia coli promoter DNA sequences. Nucleic Acids Res. 11:2237-2255.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 2237-2255
    • Hawley, D.K.1    McClure, W.R.2
  • 122
    • 0029946715 scopus 로고    scopus 로고
    • Effect of the pufQ-pufB intercistronic region on puf mRNA stability in Rhodobacter capsulants
    • Heck, C., R. Rothfuchs, A. Jǒger, R. Rauhut, and G. Klug. 1996. Effect of the pufQ-pufB intercistronic region on puf mRNA stability in Rhodobacter capsulants. Mol. Microbiol. 20:1165-1178.
    • (1996) Mol. Microbiol. , vol.20 , pp. 1165-1178
    • Heck, C.1    Rothfuchs, R.2    Jǒger, A.3    Rauhut, R.4    Klug, G.5
  • 123
    • 0024335650 scopus 로고
    • Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome be complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri
    • Heiss, B., K. Frunzke, and W. G. Zumft. 1989. Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome be complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri. J. Bacteriol. 171:3288-3297.
    • (1989) J. Bacteriol. , vol.171 , pp. 3288-3297
    • Heiss, B.1    Frunzke, K.2    Zumft, W.G.3
  • 124
    • 0027266813 scopus 로고
    • The sequence of electron carriers in the reaction of cytochrome c with oxygen
    • Hill, B. C. 1993. The sequence of electron carriers in the reaction of cytochrome c with oxygen. J. Bioenerg. Biomembr. 25:115-120.
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 115-120
    • Hill, B.C.1
  • 126
    • 0027440731 scopus 로고
    • Sequence and expression of the gene encoding the respiratory nitrous-oxide reductase from Paracoccus denitrificans: New and conserved structural and regulatory motifs
    • Hoeren, F. U., B. C. Berks, S. J. Ferguson, and J. E. G. McCarthy. 1993. Sequence and expression of the gene encoding the respiratory nitrous-oxide reductase from Paracoccus denitrificans: new and conserved structural and regulatory motifs. Eur. J. Biochem. 218:49-57.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 49-57
    • Hoeren, F.U.1    Berks, B.C.2    Ferguson, S.J.3    McCarthy, J.E.G.4
  • 127
    • 0026077298 scopus 로고
    • Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I)
    • Hofhaus, G., H. Weiss, and K. Leonard. 1991. Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I). J. Mol. Biol. 221:1027-1044.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1027-1044
    • Hofhaus, G.1    Weiss, H.2    Leonard, K.3
  • 128
    • 0025330293 scopus 로고
    • Cloning and sequencing of the hemA gene of Rhodobacter capsulatus and isolation of a 5-aminolevulinic acid-dependent mutant strain
    • Hornberger, U., R. Liebetanz, H.-V. Tichy, and G. Drews. 1990. Cloning and sequencing of the hemA gene of Rhodobacter capsulatus and isolation of a 5-aminolevulinic acid-dependent mutant strain. Mol. Gen. Genet. 221:371-378.
    • (1990) Mol. Gen. Genet. , vol.221 , pp. 371-378
    • Hornberger, U.1    Liebetanz, R.2    Tichy, H.-V.3    Drews, G.4
  • 131
    • 0027439274 scopus 로고
    • Cloning and sequencing of the gene coding for the large subunit of methylamine dehydrogenase from Thiobacillus versutus
    • Huitema, F., J. van Beeumen, G. van Driessche, J. A. Duine, and G. W. Canters. 1993. Cloning and sequencing of the gene coding for the large subunit of methylamine dehydrogenase from Thiobacillus versutus. J. Bacteriol. 175:6254-6259.
    • (1993) J. Bacteriol. , vol.175 , pp. 6254-6259
    • Huitema, F.1    Van Beeumen, J.2    Van Driessche, G.3    Duine, J.A.4    Canters, G.W.5
  • 132
    • 0023025816 scopus 로고
    • Sequences of Escherichia coli uvrA gene and protein reveal two potential ATP binding sites
    • Husain, I., B. van Houten, D. C. Thomas, and A. Sancar. 1986. Sequences of Escherichia coli uvrA gene and protein reveal two potential ATP binding sites. J. Biol. Chem. 261:4895-4901.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4895-4901
    • Husain, I.1    Van Houten, B.2    Thomas, D.C.3    Sancar, A.4
  • 133
    • 0022400803 scopus 로고
    • An inducible periplasmic blue copper protein from Paracoccus denitrificans: Purification, properties, and physiological role
    • Husain, M., and V. L. Davidson. 1985. An inducible periplasmic blue copper protein from Paracoccus denitrificans: purification, properties, and physiological role. J. Biol. Chem. 260:14626-14629.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14626-14629
    • Husain, M.1    Davidson, V.L.2
  • 134
    • 0022998580 scopus 로고
    • Characterization of two inducible periplasmic c-type cytochromes from Paracoccus denitrificans
    • Hosain, M., and V. L. Davidson. 1986. Characterization of two inducible periplasmic c-type cytochromes from Paracoccus denitrificans. J. Biol. Chem. 261:8577-8580.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8577-8580
    • Hosain, M.1    Davidson, V.L.2
  • 135
    • 0023217278 scopus 로고
    • Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans
    • Husain, M., and V. L. Davidson. 1987. Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans. J. Bacteriol. 169: 1712-1717.
    • (1987) J. Bacteriol. , vol.169 , pp. 1712-1717
    • Husain, M.1    Davidson, V.L.2
  • 136
    • 0021811007 scopus 로고
    • Partial purification and characterization of glutaryl-coenzyme A dehydrogenase, electron transfer flavoprotein, and electron transfer flavoprotein-Q oxidoreductase from Paracoccus denitrificans
    • Husain, M., and D. J. Steenkamp. 1985. Partial purification and characterization of glutaryl-coenzyme A dehydrogenase, electron transfer flavoprotein, and electron transfer flavoprotein-Q oxidoreductase from Paracoccus denitrificans. J. Bacteriol. 163:709-715.
    • (1985) J. Bacteriol. , vol.163 , pp. 709-715
    • Husain, M.1    Steenkamp, D.J.2
  • 137
    • 0028890031 scopus 로고
    • Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., C. Ostermeier, B. Ludwig, and H. Michel. 1995. Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376:660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 138
    • 0016837549 scopus 로고
    • Paracoccus denitrificans and the evolutionary origin of the mitochondrion
    • John, P., and F. R. Whatley. 1975. Paracoccus denitrificans and the evolutionary origin of the mitochondrion. Nature 254:495-498.
    • (1975) Nature , vol.254 , pp. 495-498
    • John, P.1    Whatley, F.R.2
  • 139
    • 0017741544 scopus 로고
    • The bioenergetics of Paracoccus denitrificans
    • John, P., and F. R. Whatley. 1977. The bioenergetics of Paracoccus denitrificans. Biochim. Biophys. Acta 463:129-153.
    • (1977) Biochim. Biophys. Acta , vol.463 , pp. 129-153
    • John, P.1    Whatley, F.R.2
  • 141
    • 0026064290 scopus 로고
    • Close linkage in Pseudomonas stutzeri of the structural genes for respiratory nitrite reductase and nitrous oxide reductase, and other essential genes for denitrification
    • Jungst, A., C. Braun, and W. G. Zumft. 1991. Close linkage in Pseudomonas stutzeri of the structural genes for respiratory nitrite reductase and nitrous oxide reductase, and other essential genes for denitrification. Mol. Gen. Genet. 225:241-248.
    • (1991) Mol. Gen. Genet. , vol.225 , pp. 241-248
    • Jungst, A.1    Braun, C.2    Zumft, W.G.3
  • 142
    • 0026620454 scopus 로고
    • Interdependence of respiratory NO reduction and nitrite reduction revealed by mutagenesis of nirQ, a novel gene in the denitrification gene cluster of Pseudomonas stutzeri
    • Jungst, A., and W. G. Zumft. 1992. Interdependence of respiratory NO reduction and nitrite reduction revealed by mutagenesis of nirQ, a novel gene in the denitrification gene cluster of Pseudomonas stutzeri. FEBS Lett. 314:308-314.
    • (1992) FEBS Lett. , vol.314 , pp. 308-314
    • Jungst, A.1    Zumft, W.G.2
  • 143
    • 0003142324 scopus 로고
    • Structure and regulation of the fixNOQP operon from Rhizobium meliloti
    • R. Palacios, J. Mora, and W. E. Newton (ed.) Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Kahn, D., J. Batut, M.-L. Daveran, and J. Fourment. 1993. Structure and regulation of the fixNOQP operon from Rhizobium meliloti, p. 474. In R. Palacios, J. Mora, and W. E. Newton (ed.), New horizons in nitrogen fixation. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1993) New Horizons in Nitrogen Fixation , pp. 474
    • Kahn, D.1    Batut, J.2    Daveran, M.-L.3    Fourment, J.4
  • 144
    • 3743062749 scopus 로고    scopus 로고
    • Personal communication
    • Kaplan, S. Personal communication.
    • Kaplan, S.1
  • 145
    • 0029935769 scopus 로고    scopus 로고
    • Evolutionary conservation of recA genes in relation to protein structure and function
    • Karlin, S., and L. Brocchieri. 1996. Evolutionary conservation of recA genes in relation to protein structure and function. J. Bacteriol. 178:1881-1894.
    • (1996) J. Bacteriol. , vol.178 , pp. 1881-1894
    • Karlin, S.1    Brocchieri, L.2
  • 146
    • 0029076627 scopus 로고
    • Paracoccus thiocyanatus sp. nov., a new species of thiocyanate-utilizing facultative chemolithotroph, and transfer of Thiobacillus versutus to the genus Paracoccus as Paracoccus versutus comb. nov. with emendation of the genus
    • Katayama, Y., A. Hiraishi, and H. Kuraishi. 1995. Paracoccus thiocyanatus sp. nov., a new species of thiocyanate-utilizing facultative chemolithotroph, and transfer of Thiobacillus versutus to the genus Paracoccus as Paracoccus versutus comb. nov. with emendation of the genus. Microbiology 141:1469-1477.
    • (1995) Microbiology , vol.141 , pp. 1469-1477
    • Katayama, Y.1    Hiraishi, A.2    Kuraishi, H.3
  • 147
    • 0027485443 scopus 로고
    • Is intracytoplasmic membrane structure a generic criterion? It does not coincide with phylogenetic interrelationships among phototrophic purple nonsulfur bacteria
    • Kawasaki, H., Y. Hoshino, A. Hirata, and K. Yamasato. 1993. Is intracytoplasmic membrane structure a generic criterion? It does not coincide with phylogenetic interrelationships among phototrophic purple nonsulfur bacteria. Arch. Microbiol. 160:358-362.
    • (1993) Arch. Microbiol. , vol.160 , pp. 358-362
    • Kawasaki, H.1    Hoshino, Y.2    Hirata, A.3    Yamasato, K.4
  • 148
    • 0027305184 scopus 로고
    • Phylogenetic diversity of phototrophic purple non-sulfur bacteria in the Proteobacteria alpha group
    • Kawasaki, H., Y. Hoshino, and K. Yamasato. 1993. Phylogenetic diversity of phototrophic purple non-sulfur bacteria in the Proteobacteria alpha group. FEMS Microbiol. Lett. 112:61-66.
    • (1993) FEMS Microbiol. Lett. , vol.112 , pp. 61-66
    • Kawasaki, H.1    Hoshino, Y.2    Yamasato, K.3
  • 149
    • 0002186890 scopus 로고
    • Oxidation of sulphur compounds
    • Kelly, D. P. 1988. Oxidation of sulphur compounds. Symp. Soc. Gen. Microbiol. 42:65-98.
    • (1988) Symp. Soc. Gen. Microbiol. , vol.42 , pp. 65-98
    • Kelly, D.P.1
  • 150
    • 0031032795 scopus 로고    scopus 로고
    • Oxidative metabolism of inorganic sulphur compounds by bacteria
    • Kelly, D. P., J. K. Shergill, W.-P. Lu, and A. P. Wood. 1997. Oxidative metabolism of inorganic sulphur compounds by bacteria. Antonie Leeuwenhoek 71:95-108.
    • (1997) Antonie Leeuwenhoek , vol.71 , pp. 95-108
    • Kelly, D.P.1    Shergill, J.K.2    Lu, W.-P.3    Wood, A.P.4
  • 151
    • 0028960504 scopus 로고
    • Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding
    • Khoroshilova, N., H. Beinert, and P. J. Kiley. 1995. Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding. Proc. Natl. Acad. Sci. USA 92:2499-2503.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2499-2503
    • Khoroshilova, N.1    Beinert, H.2    Kiley, P.J.3
  • 152
    • 0023122158 scopus 로고
    • DNA sequence and in vitro expression of the B875 light-harvesting polypeptides of Rhodobacter sphaeroides
    • Kiley, P. J., T. J. Donohue, W. A. Havelka, and S. Kaplan. 1987. DNA sequence and in vitro expression of the B875 light-harvesting polypeptides of Rhodobacter sphaeroides. J. Bacteriol. 169:742-750.
    • (1987) J. Bacteriol. , vol.169 , pp. 742-750
    • Kiley, P.J.1    Donohue, T.J.2    Havelka, W.A.3    Kaplan, S.4
  • 153
    • 0020699361 scopus 로고
    • Transposon-encoded site specific recombination: Nature of the Tn3 DNA sequences which constitute the recombination site res
    • Kitts, P. A., L. S. Symington, P. Dyson, and D. J. Sherratt. 1983. Transposon-encoded site specific recombination: nature of the Tn3 DNA sequences which constitute the recombination site res. EMBO J. 2:1055-1060.
    • (1983) EMBO J. , vol.2 , pp. 1055-1060
    • Kitts, P.A.1    Symington, L.S.2    Dyson, P.3    Sherratt, D.J.4
  • 154
    • 0029009981 scopus 로고
    • Immunoelectron microscopy and epitope mapping with monoclonal antibodies suggest the existence of an additional N-terminal transmembrane helix in the cytochrome b subunit of bacterial ubiquinol:cytochrome c oxidoreductases
    • Kleymann, G., S. Iwata, K. H. Weismuller, W. Haase, and H. Michel. 1995. Immunoelectron microscopy and epitope mapping with monoclonal antibodies suggest the existence of an additional N-terminal transmembrane helix in the cytochrome b subunit of bacterial ubiquinol:cytochrome c oxidoreductases. Eur. J. Biochem. 230:359-363.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 359-363
    • Kleymann, G.1    Iwata, S.2    Weismuller, K.H.3    Haase, W.4    Michel, H.5
  • 155
    • 0030988928 scopus 로고    scopus 로고
    • Identification, sequence analysis, and expression of the lepB gene for a leader peptidase in Rhodobacter capsulants
    • Klug, G., A. Jager, C. Heck, and R. Rauhut. 1997. Identification, sequence analysis, and expression of the lepB gene for a leader peptidase in Rhodobacter capsulants. Mol. Gen. Genet. 253:666-673.
    • (1997) Mol. Gen. Genet. , vol.253 , pp. 666-673
    • Klug, G.1    Jager, A.2    Heck, C.3    Rauhut, R.4
  • 156
    • 0001317396 scopus 로고
    • 1 complexes of photosynthetic purple bacteria
    • 1 complexes of photosynthetic purple bacteria. Photosynth. Res. 35:117-133.
    • (1993) Photosynth. Res. , vol.35 , pp. 117-133
    • Knaff, D.B.1
  • 157
    • 0026729297 scopus 로고
    • Identification and characterization of a novel insertion sequence, IS1106, downstream of the porA gene in B15 Neisseria meningitidis
    • Knight, A. I., H. Ni, K. A. V. Cartwright, and J. J. McFadden. 1992. Identification and characterization of a novel insertion sequence, IS1106, downstream of the porA gene in B15 Neisseria meningitidis. Mol. Microbiol. 6:1565-1573.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1565-1573
    • Knight, A.I.1    Ni, H.2    Cartwright, K.A.V.3    McFadden, J.J.4
  • 158
    • 0030055213 scopus 로고    scopus 로고
    • Denitrification, a novel type of respiratory metabolism in fungal mitochondrion
    • Kobayashi, M., Y. Matsuo, A. Takimoto, S. Suzuki, F. Maruo, and H. Shoun. 1996. Denitrification, a novel type of respiratory metabolism in fungal mitochondrion. J. Biol. Chem. 271:16263-16267.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16263-16267
    • Kobayashi, M.1    Matsuo, Y.2    Takimoto, A.3    Suzuki, S.4    Maruo, F.5    Shoun, H.6
  • 159
    • 3743148482 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 160
    • 0024759734 scopus 로고
    • Assimilation of methylamine by Paracoccus denitrificans involves formaldehyde transport by a specific carrier
    • Kostler, M., and D. Kleiner. 1989. Assimilation of methylamine by Paracoccus denitrificans involves formaldehyde transport by a specific carrier. FEMS Microbiol. Lett. 53:1-4.
    • (1989) FEMS Microbiol. Lett. , vol.53 , pp. 1-4
    • Kostler, M.1    Kleiner, D.2
  • 161
    • 0023109878 scopus 로고
    • Is the ubiquinone pool in the respiratory chain of the bacterium Paracoccus denitrificans really unhomogeneous?
    • Kucera, I., L. Kozak, and V. Dadak. 1987. Is the ubiquinone pool in the respiratory chain of the bacterium Paracoccus denitrificans really unhomogeneous? Arch. Biochem. Biophys. 253:199-204.
    • (1987) Arch. Biochem. Biophys. , vol.253 , pp. 199-204
    • Kucera, I.1    Kozak, L.2    Dadak, V.3
  • 162
    • 3743128617 scopus 로고
    • The release of nitric oxide from denitrifying cells of Paracoccus denitrificans by an uncoupler is the basis of a new oscillation
    • Kucera, I. 1989. The release of nitric oxide from denitrifying cells of
    • (1989) FEBS Lett. , vol.249 , pp. 56-58
    • Kucera, I.1
  • 163
    • 0023645713 scopus 로고
    • 1 complex. Nucleotide sequence and homologies between bacterial and mitochondrial subunits
    • 1 complex. Nucleotide sequence and homologies between bacterial and mitochondrial subunits. J. Biol. Chem. 262:13805-13811.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13805-13811
    • Kurowski, B.1    Ludwig, B.2
  • 164
    • 0029785470 scopus 로고    scopus 로고
    • Requirement of nitric oxide for induction of genes whose products are involved in nitric oxide metabolism in Rhodobacter sphaeroides 2.4.3
    • Kwiatkowski, A. V., and J. P. Shapleigh. 1996. Requirement of nitric oxide for induction of genes whose products are involved in nitric oxide metabolism in Rhodobacter sphaeroides 2.4.3. J. Biol. Chem. 271:24382-24388.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24382-24388
    • Kwiatkowski, A.V.1    Shapleigh, J.P.2
  • 165
    • 0028925550 scopus 로고
    • Complete DNA sequence, specific Tn5 insertion map, and gene assignment of the carotenoid biosynthesis pathway of Rhodobacter sphaeroides
    • Lang, H. P., R. J. Cogdell, S. Takaichi, and C. N. Hunter. 1995. Complete DNA sequence, specific Tn5 insertion map, and gene assignment of the carotenoid biosynthesis pathway of Rhodobacter sphaeroides. J. Bacteriol. 177:2064-2073.
    • (1995) J. Bacteriol. , vol.177 , pp. 2064-2073
    • Lang, H.P.1    Cogdell, R.J.2    Takaichi, S.3    Hunter, C.N.4
  • 166
    • 0030029817 scopus 로고    scopus 로고
    • DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen
    • Lazazzera, B. A., H. Beinert, N. Khoroshilova, M. C. Kennedy, and P. J. Kiley. 1996. DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen. J. Biol. Chem. 271: 2762-2768.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2762-2768
    • Lazazzera, B.A.1    Beinert, H.2    Khoroshilova, N.3    Kennedy, M.C.4    Kiley, P.J.5
  • 167
    • 0031014025 scopus 로고    scopus 로고
    • Cloning and characterization of two groESL operons of Rhodobacter sphaeroides: Transcriptional regulation of the heat-induced groESL operon
    • Lee, W. T., K. C. Terlesky, and F. R. Tabita. 1997. Cloning and characterization of two groESL operons of Rhodobacter sphaeroides: transcriptional regulation of the heat-induced groESL operon. J. Bacteriol. 179:487-495.
    • (1997) J. Bacteriol. , vol.179 , pp. 487-495
    • Lee, W.T.1    Terlesky, K.C.2    Tabita, F.R.3
  • 168
    • 0031940235 scopus 로고    scopus 로고
    • Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdenum enzymes
    • Leimkuhler, S., M. Kern, P. S. Solomon, A. G. McEwan, G. Schwarz, R. R. Mendel, and W. Klipp. 1998. Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdenum enzymes. Mol. Microbiol. 27:853-869.
    • (1998) Mol. Microbiol. , vol.27 , pp. 853-869
    • Leimkuhler, S.1    Kern, M.2    Solomon, P.S.3    McEwan, A.G.4    Schwarz, G.5    Mendel, R.R.6    Klipp, W.7
  • 169
    • 0031051445 scopus 로고    scopus 로고
    • The pseudoazurin gene from Thiosphaera pantotropha: Analysis of upstream putative regulatory sequences and overexpression in Escherichia coli
    • Leung, Y. C., C. Chan, J. S. Reader, A. C. Willis, R. J. M. van Spanning, S. J. Ferguson, and S. E. Radford. 1997. The pseudoazurin gene from Thiosphaera pantotropha: analysis of upstream putative regulatory sequences and overexpression in Escherichia coli. Biochem. J. 321:699-705.
    • (1997) Biochem. J. , vol.321 , pp. 699-705
    • Leung, Y.C.1    Chan, C.2    Reader, J.S.3    Willis, A.C.4    Van Spanning, R.J.M.5    Ferguson, S.J.6    Radford, S.E.7
  • 171
    • 0031798778 scopus 로고    scopus 로고
    • Identification of bacterial isolates from biofilters as Paracoccus alkenifer sp. nov. and Paracoccus solventivorans with emended description of Paracoccus solventivorans
    • Lipski, A., K. Reichert, B. Reuter, C. Sproer, and K. Altendorf. 1998. Identification of bacterial isolates from biofilters as Paracoccus alkenifer sp. nov. and Paracoccus solventivorans with emended description of Paracoccus solventivorans. Int. J. Syst. Bacteriol. 48:529-536.
    • (1998) Int. J. Syst. Bacteriol. , vol.48 , pp. 529-536
    • Lipski, A.1    Reichert, K.2    Reuter, B.3    Sproer, C.4    Altendorf, K.5
  • 172
    • 3743072781 scopus 로고
    • Persistence of bacterial denitrification capacity under aerobic conditions: The rule rather than the exception
    • Lloyd, D., L. Boddy, and K. J. P. Davies. 1987. Persistence of bacterial denitrification capacity under aerobic conditions: the rule rather than the exception. FEMS Microbiol. Ecol. 45:103-106.
    • (1987) FEMS Microbiol. Ecol. , vol.45 , pp. 103-106
    • Lloyd, D.1    Boddy, L.2    Davies, K.J.P.3
  • 173
    • 0026007207 scopus 로고
    • Assignment of the 600-MHz 1H-NMR spectrum of amicyanin from Thiobacillus versutus by two-dimensional NMR methods provides information on secondary structure
    • Lommen, A., S. Wijmenga, C. W. Hilbers, and G. W. Canters. 1991. Assignment of the 600-MHz 1H-NMR spectrum of amicyanin from Thiobacillus versutus by two-dimensional NMR methods provides information on secondary structure. Eur. J. Biochem. 201:695-702.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 695-702
    • Lommen, A.1    Wijmenga, S.2    Hilbers, C.W.3    Canters, G.W.4
  • 174
    • 0021017235 scopus 로고
    • Purification and some properties of two principle enzymes of the thiosulphate-oxidising multi-enzyme system from Thiobacillus A2
    • Lu, W. P., and D. P. Kelly. 1983. Purification and some properties of two principle enzymes of the thiosulphate-oxidising multi-enzyme system from Thiobacillus A2. J. Gen. Microbiol. 129:3549-3564.
    • (1983) J. Gen. Microbiol. , vol.129 , pp. 3549-3564
    • Lu, W.P.1    Kelly, D.P.2
  • 175
    • 0020563281 scopus 로고
    • Rhodanese: An enzyme not necessary for thiosulphate oxidation by Thiobacillus A2
    • Lu, W. P., and D. P. Kelly. 1983. Rhodanese: an enzyme not necessary for thiosulphate oxidation by Thiobacillus A2. FEMS Microbiol. Lett. 18:289-292.
    • (1983) FEMS Microbiol. Lett. , vol.18 , pp. 289-292
    • Lu, W.P.1    Kelly, D.P.2
  • 176
    • 0026651413 scopus 로고
    • Terminal oxidases in Paracoccus denitrificans
    • Ludwig, B. 1992. Terminal oxidases in Paracoccus denitrificans. Biochim. Biophys. Acta 1101:195-197.
    • (1992) Biochim. Biophys. Acta , vol.1101 , pp. 195-197
    • Ludwig, B.1
  • 178
    • 0021105542 scopus 로고
    • Cytochrome c, from Paracoccus denitrificans
    • Ludwig, B., K. Suda, and N. Cerletti. 1983. Cytochrome c, from Paracoccus denitrificans. Eur. J. Biochem. 137:597-602.
    • (1983) Eur. J. Biochem. , vol.137 , pp. 597-602
    • Ludwig, B.1    Suda, K.2    Cerletti, N.3
  • 179
    • 0027478696 scopus 로고
    • Transfer of Thiosphaera pantotropha to Paracoccus denitrificans
    • Ludwig, W., G. Mittenhuber, and C. G. Friedrich. 1993. Transfer of Thiosphaera pantotropha to Paracoccus denitrificans. Int. J. Syst. Bacteriol. 43: 363-367.
    • (1993) Int. J. Syst. Bacteriol. , vol.43 , pp. 363-367
    • Ludwig, W.1    Mittenhuber, G.2    Friedrich, C.G.3
  • 181
    • 0027399728 scopus 로고
    • Analysis of the promoter and regulatory sequences of an oxygen-regulated bch operon in Rhodobacter capsulatus by site-directed mutagenesis
    • Ma, D., D. N. Cook, D. A. O'Brien, and J. E. Hearst. 1993. Analysis of the promoter and regulatory sequences of an oxygen-regulated bch operon in Rhodobacter capsulatus by site-directed mutagenesis. J. Bacteriol. 175:2037-2045.
    • (1993) J. Bacteriol. , vol.175 , pp. 2037-2045
    • Ma, D.1    Cook, D.N.2    O'Brien, D.A.3    Hearst, J.E.4
  • 183
    • 0028297954 scopus 로고
    • Functional analysis of the fixNOQP region of Azorhizobium caulinodans
    • Mandon, K., P. A. Kaminski, and C. Elmerich. 1994. Functional analysis of the fixNOQP region of Azorhizobium caulinodans. J. Bacteriol. 176:2560-2568.
    • (1994) J. Bacteriol. , vol.176 , pp. 2560-2568
    • Mandon, K.1    Kaminski, P.A.2    Elmerich, C.3
  • 184
  • 185
    • 0030799991 scopus 로고    scopus 로고
    • Amaricoccus gen. nov., a gram-negative coccus occurring in regular packages or tertrads, isolated from activated sludges biomass, and descriptions of Amaricoccus veronensis sp. nov., Amaricoccus tamworthensis sp. nov., and Amaricoccus kaplicencis sp. nov
    • Maszenan, A. M., R. J. Seviour, B. K. Patel, G. N. Rees, and B. M. McDougall. 1997. Amaricoccus gen. nov., a gram-negative coccus occurring in regular packages or tertrads, isolated from activated sludges biomass, and descriptions of Amaricoccus veronensis sp. nov., Amaricoccus tamworthensis sp. nov., and Amaricoccus kaplicencis sp. nov. Int. J. Syst. Bacteriol. 47:727-734.
    • (1997) Int. J. Syst. Bacteriol. , vol.47 , pp. 727-734
    • Maszenan, A.M.1    Seviour, R.J.2    Patel, B.K.3    Rees, G.N.4    McDougall, B.M.5
  • 186
    • 0025859584 scopus 로고
    • Evidence for the role of soluble cytochrome c in the dissimilatory reduction of nitrite and nitrous oxide by cells of Paracoccus denitrificans
    • Mat'chova, I., and I. Kucera. 1991. Evidence for the role of soluble cytochrome c in the dissimilatory reduction of nitrite and nitrous oxide by cells of Paracoccus denitrificans. Biochim. Biophys. Acta 1058:256-260.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 256-260
    • Mat'chova, I.1    Kucera, I.2
  • 187
    • 0025812113 scopus 로고
    • Two new genes located between 2758 and 2761 kilobase pairs on the Escherichia coli genome
    • Miczak, A., A. K. Chauhan, and D. Apirion. 1991. Two new genes located between 2758 and 2761 kilobase pairs on the Escherichia coli genome. J. Bacteriol. 173:3271-3272.
    • (1991) J. Bacteriol. , vol.173 , pp. 3271-3272
    • Miczak, A.1    Chauhan, A.K.2    Apirion, D.3
  • 188
    • 0023667819 scopus 로고
    • Cholera toxin transcriptional activator ToxR is a transmembrane DNA binding protein
    • Miller, V. L., R. K. Taylor, and J. J. Mekalanos. 1987. Cholera toxin transcriptional activator ToxR is a transmembrane DNA binding protein. Cell 48:271-279.
    • (1987) Cell , vol.48 , pp. 271-279
    • Miller, V.L.1    Taylor, R.K.2    Mekalanos, J.J.3
  • 189
    • 0025790369 scopus 로고
    • Identification of the DNA region responsible for sulfur-oxidizing ability of Thiosphaera pantotropha
    • Mittenhuber, G., K. Sonomoto, M. Egert, and C. G. Friedrich. 1991. Identification of the DNA region responsible for sulfur-oxidizing ability of Thiosphaera pantotropha. J. Bacteriol. 173:7340-7344.
    • (1991) J. Bacteriol. , vol.173 , pp. 7340-7344
    • Mittenhuber, G.1    Sonomoto, K.2    Egert, M.3    Friedrich, C.G.4
  • 190
    • 0027340210 scopus 로고
    • 1-type nitrite reductase from, and the absence of a copper-type nitrite reductase from, the aerobic denitrifier Thiosphaera pantotropha: The role of pseudoazurin as an electron donor
    • 1-type nitrite reductase from, and the absence of a copper-type nitrite reductase from, the aerobic denitrifier Thiosphaera pantotropha: the role of pseudoazurin as an electron donor. Eur. J. Biochem. 212:377-385.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 377-385
    • Moir, J.W.B.1    Baratta, D.2    Richardson, D.J.3    Ferguson, S.J.4
  • 191
    • 3743054877 scopus 로고
    • D.Phil, thesis. University of Oxford, Oxford, United Kingdom
    • Moir, J. W. B. 1993. D.Phil, thesis. University of Oxford, Oxford, United Kingdom.
    • (1993)
    • Moir, J.W.B.1
  • 192
    • 0027382442 scopus 로고
    • Spontaneous mutation of Thiosphaera pantotripha enabling growth on methanol correlates with synthesis of a 26 kDa c-type cytochrome
    • Moir, J. W. B., and S. J. Ferguson. 1993. Spontaneous mutation of Thiosphaera pantotripha enabling growth on methanol correlates with synthesis of a 26 kDa c-type cytochrome. FEMS Microbiol. Lett. 113:321-326.
    • (1993) FEMS Microbiol. Lett. , vol.113 , pp. 321-326
    • Moir, J.W.B.1    Ferguson, S.J.2
  • 193
    • 0028345479 scopus 로고
    • 550 indicate that a copper protein can substitute for this cytochrome in electron transport to nitrite, nitric oxide and nitrous oxide
    • 550 indicate that a copper protein can substitute for this cytochrome in electron transport to nitrite, nitric oxide and nitrous oxide. Microbiology 140:389-397.
    • (1994) Microbiology , vol.140 , pp. 389-397
    • Moir, J.W.B.1    Ferguson, S.J.2
  • 194
    • 0029125387 scopus 로고
    • The expression of redox proteins of denitrification in Thiosphaera pantotropha grown with oxygen, nitrate, and nitrous oxide as electron acceptors
    • Moir, J. W. B., D. J. Richardson, and S. J. Ferguson. 1995. The expression of redox proteins of denitrification in Thiosphaera pantotropha grown with oxygen, nitrate, and nitrous oxide as electron acceptors. Arch. Microbiol. 164:43-49.
    • (1995) Arch. Microbiol. , vol.164 , pp. 43-49
    • Moir, J.W.B.1    Richardson, D.J.2    Ferguson, S.J.3
  • 195
    • 0030579935 scopus 로고    scopus 로고
    • Cloning and characterization of the tyrB gene from Salmonella typhimurium
    • Nakai, Y., H. Hayashi, and H. Kagamiyama. 1996. Cloning and characterization of the tyrB gene from Salmonella typhimurium. Biochim. Biophys. Acta 1308:189-192.
    • (1996) Biochim. Biophys. Acta , vol.1308 , pp. 189-192
    • Nakai, Y.1    Hayashi, H.2    Kagamiyama, H.3
  • 196
    • 0027252484 scopus 로고
    • 5-Aminolevulinic acid availability and control of spectral complex formation in hemA and hemT mutants of Rhodobacter sphaeroides
    • Neidle, E. L., and S. Kaplan. 1993. 5-Aminolevulinic acid availability and control of spectral complex formation in hemA and hemT mutants of Rhodobacter sphaeroides. J. Bacteriol. 175:2304-2313.
    • (1993) J. Bacteriol. , vol.175 , pp. 2304-2313
    • Neidle, E.L.1    Kaplan, S.2
  • 197
    • 0014462060 scopus 로고
    • The two-haem nitrite reductase of Micrococcus denitrificans
    • Newton, N. 1969. The two-haem nitrite reductase of Micrococcus denitrificans. Biochim. Biophys. Acta 185:316-331.
    • (1969) Biochim. Biophys. Acta , vol.185 , pp. 316-331
    • Newton, N.1
  • 199
    • 0030996091 scopus 로고    scopus 로고
    • Molecular analysis of the Rhodobacter capsulatus chaperone dnaKJ operon: Purification and characterization of DnaK
    • Nickel, C. M., J. Vandekerckhove, P. Beyer, and M. H. Tadros. 1997. Molecular analysis of the Rhodobacter capsulatus chaperone dnaKJ operon: purification and characterization of DnaK. Gene 192:251-259.
    • (1997) Gene , vol.192 , pp. 251-259
    • Nickel, C.M.1    Vandekerckhove, J.2    Beyer, P.3    Tadros, M.H.4
  • 200
    • 0020679869 scopus 로고
    • Taxonomic study of Paracoccus denitrificans
    • Nokhal, T. H., and H. G. Schlegel. 1983. Taxonomic study of Paracoccus denitrificans. Int. J. Syst. Bacteriol. 33:26-37.
    • (1983) Int. J. Syst. Bacteriol. , vol.33 , pp. 26-37
    • Nokhal, T.H.1    Schlegel, H.G.2
  • 202
    • 3743063844 scopus 로고
    • Several lines of evidence for the linearity of Thiobacillus versutus extrachromosomal pTAV2 DNA
    • Nowicka, B., A. Meler, M. Wlodarczyk, and K. I. Wolska. 1990. Several lines of evidence for the linearity of Thiobacillus versutus extrachromosomal pTAV2 DNA. Acta Microbiol. Pol. 39:205-210.
    • (1990) Acta Microbiol. Pol. , vol.39 , pp. 205-210
    • Nowicka, B.1    Meler, A.2    Wlodarczyk, M.3    Wolska, K.I.4
  • 203
    • 0026558482 scopus 로고
    • Gene organization deduced from the complete sequence of liverwort Marchantia polymorpha mitochondrial DNA. A primitive form of plant mitochondrial genome
    • Oda, K., K. Yamato, E. Ohta, Y. Nakamura, M. Takemura, N. Nozato, K. Akashi, T. Kanegae, Y. Ogura, and T. Kohchi. 1992. Gene organization deduced from the complete sequence of liverwort Marchantia polymorpha mitochondrial DNA. A primitive form of plant mitochondrial genome. J. Mol. Biol. 223:1-7.
    • (1992) J. Mol. Biol. , vol.223 , pp. 1-7
    • Oda, K.1    Yamato, K.2    Ohta, E.3    Nakamura, Y.4    Takemura, M.5    Nozato, N.6    Akashi, K.7    Kanegae, T.8    Ogura, Y.9    Kohchi, T.10
  • 205
    • 0028055018 scopus 로고
    • The winds of (evolutionary) change: Breathing new life into microbiology
    • Olsen, G. J., C. R. Woese, and R. Overbeek. 1994. The winds of (evolutionary) change: breathing new life into microbiology. J. Bacteriol. 176:1-6.
    • (1994) J. Bacteriol. , vol.176 , pp. 1-6
    • Olsen, G.J.1    Woese, C.R.2    Overbeek, R.3
  • 206
    • 0028991525 scopus 로고
    • Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase
    • Ostermeier, C., S. Iwata, B. Ludwig, and H. Michel. 1995. Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase. Nat. Struct. Biol. 10:842-846.
    • (1995) Nat. Struct. Biol. , vol.10 , pp. 842-846
    • Ostermeier, C.1    Iwata, S.2    Ludwig, B.3    Michel, H.4
  • 208
    • 0031014286 scopus 로고    scopus 로고
    • Paracoccus denitrificans aromatic amino acid aminotransferase: A model enzyme for the study of dual substrate recognition mechanism
    • Oue, S., A. Okamoto, Y. Nakai, M. Nakabira, T. Shibatani, H. Hayashi, and H. Kagamiyama. 1997. Paracoccus denitrificans aromatic amino acid aminotransferase: a model enzyme for the study of dual substrate recognition mechanism. J. Biochem. 121:161-171.
    • (1997) J. Biochem. , vol.121 , pp. 161-171
    • Oue, S.1    Okamoto, A.2    Nakai, Y.3    Nakabira, M.4    Shibatani, T.5    Hayashi, H.6    Kagamiyama, H.7
  • 209
    • 0022036205 scopus 로고
    • Cloning of Paracoccus cytochrome c oxidase subunit II
    • Paetow, B., G. Panskus, and B. Ludwig. 1985. Cloning of Paracoccus cytochrome c oxidase subunit II. J. Inorg. Biochem. 23:183-186.
    • (1985) J. Inorg. Biochem. , vol.23 , pp. 183-186
    • Paetow, B.1    Panskus, G.2    Ludwig, B.3
  • 210
    • 0024787970 scopus 로고
    • Structure, control and assembly of a bacterial electron transport system as exemplified by Paracoccus denitrificans
    • Page, M. D., G. Carr, L. C. Bell, and S. J. Ferguson. 1989. Structure, control and assembly of a bacterial electron transport system as exemplified by Paracoccus denitrificans. Biochem. Soc. Trans. 17:991-993.
    • (1989) Biochem. Soc. Trans. , vol.17 , pp. 991-993
    • Page, M.D.1    Carr, G.2    Bell, L.C.3    Ferguson, S.J.4
  • 212
    • 0025140710 scopus 로고
    • 1 are translocated to the periplasm of Paracoccus denitrificans in the absence of haem incorporation caused by either mutation or inhibition of haem synthesis
    • 1 are translocated to the periplasm of Paracoccus denitrificans in the absence of haem incorporation caused by either mutation or inhibition of haem synthesis. Mol. Microbiol. 4:1181-1182.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1181-1182
    • Page, M.D.1    Ferguson, S.J.2
  • 213
    • 0024372494 scopus 로고
    • 1 (nitrite reductase) from Paracoccus denitrificans
    • 1 (nitrite reductase) from Paracoccus denitrificans. Mol. Microbiol. 3:653-661.
    • (1990) Mol. Microbiol. , vol.3 , pp. 653-661
    • Page, M.D.1    Ferguson, S.J.2
  • 214
    • 0027133569 scopus 로고
    • Mutants of Methytobacterium extorquens and Paracoccus denitrificans deficient in c-type cytochrome biogenesis synthesise the methylamine-dehydrogenase polypeptides but cannot assemble the tryptophan-tryptophylquinone group
    • Page, M. D., and S. J. Ferguson. 1993. Mutants of Methytobacterium extorquens and Paracoccus denitrificans deficient in c-type cytochrome biogenesis synthesise the methylamine-dehydrogenase polypeptides but cannot assemble the tryptophan-tryptophylquinone group. Eur. J. Biochem. 218: 711-717.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 711-717
    • Page, M.D.1    Ferguson, S.J.2
  • 215
    • 0028111909 scopus 로고
    • Differential reduction in periplasmic and membrane-bound c-type cytochromes in a Paracoccus denitrificans mutant partially deficient in 5-aminolevulinate synthase
    • Page, M. D., and S. J. Ferguson. 1994. Differential reduction in periplasmic and membrane-bound c-type cytochromes in a Paracoccus denitrificans mutant partially deficient in 5-aminolevulinate synthase. J. Bacteriol. 176: 5919-5928.
    • (1994) J. Bacteriol. , vol.176 , pp. 5919-5928
    • Page, M.D.1    Ferguson, S.J.2
  • 217
    • 0030749493 scopus 로고    scopus 로고
    • 3-type cytochrome biogenesis: Evidence for a reductase role in vivo
    • 3-type cytochrome biogenesis: evidence for a reductase role in vivo. Mol. Microbiol. 24:977-990.
    • (1997) Mol. Microbiol. , vol.24 , pp. 977-990
    • Page, M.D.1    Ferguson, S.J.2
  • 218
    • 0031050448 scopus 로고    scopus 로고
    • The Paracoccus denitrificans ccmA, B and C genes: Cloning and sequencing, and analysis of the potential of their products to form a haem or apo-c-type cytochrome transporter
    • Page, M. D., D. A. Pearce, H. A. C. Norris, and S. J. Ferguson. 1997. The Paracoccus denitrificans ccmA, B and C genes: cloning and sequencing, and analysis of the potential of their products to form a haem or apo-c-type cytochrome transporter. Microbiology 143:563-576.
    • (1997) Microbiology , vol.143 , pp. 563-576
    • Page, M.D.1    Pearce, D.A.2    Norris, H.A.C.3    Ferguson, S.J.4
  • 219
    • 0032031987 scopus 로고    scopus 로고
    • Contrasting routes of c-type cytochrome assembly in mitochondria, chloroplasts and bacteria
    • Page, M. D., Y. Sambongi, and S. J. Ferguson. 1998. Contrasting routes of c-type cytochrome assembly in mitochondria, chloroplasts and bacteria. Trends Biochem. Sci. 23:103-108.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 103-108
    • Page, M.D.1    Sambongi, Y.2    Ferguson, S.J.3
  • 220
    • 0028589402 scopus 로고
    • Mechanistic and phenomenological features of proton pumps in the respiratory chain of mitochondria
    • Papa, S., M. Lorusson, and N. Capitanio. 1994. Mechanistic and phenomenological features of proton pumps in the respiratory chain of mitochondria. J. Bioenerg. Biomembr. 26:609-618.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 609-618
    • Papa, S.1    Lorusson, M.2    Capitanio, N.3
  • 221
    • 0027243652 scopus 로고
    • Signal transduction schemes of bacteria
    • Parkinson, J. S. 1993. Signal transduction schemes of bacteria. Cell 73:857-871.
    • (1993) Cell , vol.73 , pp. 857-871
    • Parkinson, J.S.1
  • 222
    • 0028286455 scopus 로고
    • Critical nucleotides in the interaction of a LysR-type regulator with its target promoter region: catBC promoter activation by CatR
    • Parsek, M. R., R. W. Ye, P. Pun, and A-M. Chakrabarty. 1994. Critical nucleotides in the interaction of a LysR-type regulator with its target promoter region: catBC promoter activation by CatR. J. Biol. Chem. 269: 11279-11284.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11279-11284
    • Parsek, M.R.1    Ye, R.W.2    Pun, P.3    Chakrabarty, A.M.4
  • 223
    • 0030020122 scopus 로고    scopus 로고
    • Expression of the thioredoxin gene (trxA) in Rhodobacter sphaeroides is regulated by oxygen
    • Pasternak, C., K. Assemat, A. M. Breton, J. D. Clement-Metral, and G. Klug. 1996. Expression of the thioredoxin gene (trxA) in Rhodobacter sphaeroides is regulated by oxygen. Mol. Gen. Genet. 250:189-196.
    • (1996) Mol. Gen. Genet. , vol.250 , pp. 189-196
    • Pasternak, C.1    Assemat, K.2    Breton, A.M.3    Clement-Metral, J.D.4    Klug, G.5
  • 224
    • 0030591768 scopus 로고    scopus 로고
    • Cloning, nucleotide sequence and characterization of the rpoD gene encoding the primary sigma factor of Rhodobacter capsulants
    • Pasternak, C., W. Chen, C. Heck, and G. Klug. 1996. Cloning, nucleotide sequence and characterization of the rpoD gene encoding the primary sigma factor of Rhodobacter capsulants. Gene 176:177-184.
    • (1996) Gene , vol.176 , pp. 177-184
    • Pasternak, C.1    Chen, W.2    Heck, C.3    Klug, G.4
  • 225
    • 0026148470 scopus 로고
    • Sequence of the iaa and ipt region of different Agrobacterium tumefaciens biotype III octopine strains: Reconstruction of octopine Ti plasmid evolution
    • Paulus, F., J. Canaday, F. Vincent, G. Bonnard, C. Kares, and L. Otten. 1991. Sequence of the iaa and ipt region of different Agrobacterium tumefaciens biotype III octopine strains: reconstruction of octopine Ti plasmid evolution. Plant Mol. Biol. 16:601-614.
    • (1991) Plant Mol. Biol. , vol.16 , pp. 601-614
    • Paulus, F.1    Canaday, J.2    Vincent, F.3    Bonnard, G.4    Kares, C.5    Otten, L.6
  • 226
    • 0031937605 scopus 로고    scopus 로고
    • Identification of the Paracoccus denitrificans ccmF and ccmH genes: Disruption of ccmF, coding for a putative transporter, results in formation of an unstable apo cytochrome c and deficiency in siderophore production
    • Pearce, D. A., M. D. Page, H. A. C. Norris, E. Tomlinson, and S. J. Ferguson. 1998. Identification of the Paracoccus denitrificans ccmF and ccmH genes: disruption of ccmF, coding for a putative transporter, results in formation of an unstable apo cytochrome c and deficiency in siderophore production. Microbiology 144:467-477.
    • (1998) Microbiology , vol.144 , pp. 467-477
    • Pearce, D.A.1    Page, M.D.2    Norris, H.A.C.3    Tomlinson, E.4    Ferguson, S.J.5
  • 227
    • 0024286155 scopus 로고
    • Purification and properties of succinate-ubiquinone oxidoreductase complex from Paracoccus denitrificans
    • Pennoyer, J. D., T. Ohnishi, and B. L. Trumpower. 1988. Purification and properties of succinate-ubiquinone oxidoreductase complex from Paracoccus denitrificans. Biochim. Biophys. Acta 935:195-207.
    • (1988) Biochim. Biophys. Acta , vol.935 , pp. 195-207
    • Pennoyer, J.D.1    Ohnishi, T.2    Trumpower, B.L.3
  • 230
    • 0030203778 scopus 로고    scopus 로고
    • The various strategies within the TyrR regulation of Escherichia coli to modulate gene expression
    • Pittard, J. 1996. The various strategies within the TyrR regulation of Escherichia coli to modulate gene expression. Genes Cells 1:717-725.
    • (1996) Genes Cells , vol.1 , pp. 717-725
    • Pittard, J.1
  • 231
    • 0027469984 scopus 로고
    • Genes for a microaerobically induced oxidase complex in Bradyrhizobium japonicum are essential for a nitrogen-fixing endosymbiosis
    • Preisig, O., D. Anthamattan, and H. Hennecke. 1993. Genes for a microaerobically induced oxidase complex in Bradyrhizobium japonicum are essential for a nitrogen-fixing endosymbiosis. Proc. Natl. Acad. Sci. USA 90:3309-3313.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3309-3313
    • Preisig, O.1    Anthamattan, D.2    Hennecke, H.3
  • 233
    • 0024962043 scopus 로고
    • Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli
    • Puustinen, A., M. Finel, M. Virkki, and M. Wikstrom. 1989. Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli. FEBS Lett. 249:163-167.
    • (1989) FEBS Lett. , vol.249 , pp. 163-167
    • Puustinen, A.1    Finel, M.2    Virkki, M.3    Wikstrom, M.4
  • 235
    • 0000673426 scopus 로고
    • Isolation and characterization of genes for cytochrome c oxidase in Paracoccus denitrificans
    • Raitio, M., T. Jalli, and M. Saraste. 1987. Isolation and characterization of genes for cytochrome c oxidase in Paracoccus denitrificans. EMBO J. 6:2825-2833.
    • (1987) EMBO J. , vol.6 , pp. 2825-2833
    • Raitio, M.1    Jalli, T.2    Saraste, M.3
  • 236
    • 0025135467 scopus 로고
    • Are there isoenzymes of cytochrome c oxidase in Paracoccus denitrificans?
    • Raitio, M., J. M. Pispa, T. Metso, and M. Saraste. 1990. Are there isoenzymes of cytochrome c oxidase in Paracoccus denitrificans? FEBS Lett. 261:431-435.
    • (1990) FEBS Lett. , vol.261 , pp. 431-435
    • Raitio, M.1    Pispa, J.M.2    Metso, T.3    Saraste, M.4
  • 237
    • 0028238264 scopus 로고
    • An alternative cytochrome oxidase of Paracoccus denitrificans functions as a proton pump
    • Raitio, M., and M. Wikstrom. 1994. An alternative cytochrome oxidase of Paracoccus denitrificans functions as a proton pump. Biochim. Biophys. Acta 1186:100-106.
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 100-106
    • Raitio, M.1    Wikstrom, M.2
  • 238
    • 3743091709 scopus 로고
    • Ph.D. thesis. Vrije Universiteit, Amsterdam, The Netherlands
    • Ras, J. 1995. Ph.D. thesis. Vrije Universiteit, Amsterdam, The Netherlands.
    • (1995)
    • Ras, J.1
  • 239
    • 0028917006 scopus 로고
    • Methanol oxidation in a spontaneous mutant of Thiosphaera pantotropha with a methanol positive phenotype is catalyzed by a dye-linked ethanol dehydrogenase
    • Ras, J., M. J. Hazelaar, L. A. Robertson, J. G. Kuenen, R. J. M. van Spanning, A. H. Stouthamer, and N. Harms. 1995. Methanol oxidation in a spontaneous mutant of Thiosphaera pantotropha with a methanol positive phenotype is catalyzed by a dye-linked ethanol dehydrogenase. FEMS Microbiol. Lett. 127:159-164.
    • (1995) FEMS Microbiol. Lett. , vol.127 , pp. 159-164
    • Ras, J.1    Hazelaar, M.J.2    Robertson, L.A.3    Kuenen, J.G.4    Van Spanning, R.J.M.5    Stouthamer, A.H.6    Harms, N.7
  • 241
    • 0028872476 scopus 로고
    • Isolation, sequencing, and mutagenesis of the gene encoding NAD- and glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth
    • Ras, J., P. W. van Ophem, W. N. M. Reijnders, R. J. M. van Spanning, J. A. Duine, A. H. Stouthamer, and N. Harms. 1995. Isolation, sequencing, and mutagenesis of the gene encoding NAD- and glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth. J. Bacteriol. 177:247-251.
    • (1995) J. Bacteriol. , vol.177 , pp. 247-251
    • Ras, J.1    Van Ophem, P.W.2    Reijnders, W.N.M.3    Van Spanning, R.J.M.4    Duine, J.A.5    Stouthamer, A.H.6    Harms, N.7
  • 244
    • 0029881191 scopus 로고    scopus 로고
    • Isolation of periplasmic nitrate reductase genes from Rhodobacter sphaeroides DSM 158: Structural and functional differences among prokaryotic nitrate reductases
    • Reyes, F., M. D. Roldan, W. Klipp, F. Castillo, and C. Moreno-Vivian. 1996. Isolation of periplasmic nitrate reductase genes from Rhodobacter sphaeroides DSM 158: structural and functional differences among prokaryotic nitrate reductases. Mol. Microbiol. 19:1307-1318.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1307-1318
    • Reyes, F.1    Roldan, M.D.2    Klipp, W.3    Castillo, F.4    Moreno-Vivian, C.5
  • 245
    • 0028168424 scopus 로고
    • 3 functions as a quinol oxidase in Paracoccus denitrificans. Purification, cloning and sequence comparison
    • 3 functions as a quinol oxidase in Paracoccus denitrificans. Purification, cloning and sequence comparison. J. Biol. Chem. 269:23079-23086.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23079-23086
    • Richter, O.-M.H.1    Tao, J.S.2    Turba, A.3    Ludwig, B.4
  • 246
    • 0029113246 scopus 로고
    • Crystallization and preliminary X-ray analysis of electron transfer flavoproteins from human and Paracoccus denitrificans
    • Roberts, D. L., K. R. Herrick, F. E. Frerman, and J. J. P. Kim. 1995. Crystallization and preliminary X-ray analysis of electron transfer flavoproteins from human and Paracoccus denitrificans. Protein Sci. 4:1654-1657.
    • (1995) Protein Sci. , vol.4 , pp. 1654-1657
    • Roberts, D.L.1    Herrick, K.R.2    Frerman, F.E.3    Kim, J.J.P.4
  • 248
    • 0001328962 scopus 로고
    • Thiosphaera pantotropha gen. nov. sp. nov., a facultatively anaerobic, facultatively autotrophic sulphur bacterium
    • Robertson, L. A., and J. G. Kuenen. 1983. Thiosphaera pantotropha gen. nov. sp. nov., a facultatively anaerobic, facultatively autotrophic sulphur bacterium. J. Gen. Microbiol. 129:2847-2855.
    • (1983) J. Gen. Microbiol. , vol.129 , pp. 2847-2855
    • Robertson, L.A.1    Kuenen, J.G.2
  • 249
    • 0032582701 scopus 로고    scopus 로고
    • Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial respiratory electron transport
    • in press
    • Roldán, M. D., H. J. Sears, M. R. Cheeseman, S. J. Ferguson, A. J. Thomson, B. C. Berks, and D. J. Richardson. Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial respiratory electron transport. J. Biol. Chem., in press.
    • J. Biol. Chem.
    • Roldán, M.D.1    Sears, H.J.2    Cheeseman, M.R.3    Ferguson, S.J.4    Thomson, A.J.5    Berks, B.C.6    Richardson, D.J.7
  • 250
    • 0025768497 scopus 로고
    • Genetic analysis of functional differences among distinct ferredoxins in Rhodobacter capsulatus
    • Saeki, K., Y. Suetsugi, K.-I. Tokuda, Y. Miyatake, D. A. Young, B. L. Mars, and H. Matsubara. 1991. Genetic analysis of functional differences among distinct ferredoxins in Rhodobacter capsulatus. J. Biol. Chem. 266:12889-12895.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12889-12895
    • Saeki, K.1    Suetsugi, Y.2    Tokuda, K.-I.3    Miyatake, Y.4    Young, D.A.5    Mars, B.L.6    Matsubara, H.7
  • 251
    • 0028226882 scopus 로고
    • Cytochrome oxidase evolved by tinkering with denitrification enzymes
    • Saraste, M., and J. Castresana. 1994. Cytochrome oxidase evolved by tinkering with denitrification enzymes. FEBS Lett. 341:1-4.
    • (1994) FEBS Lett. , vol.341 , pp. 1-4
    • Saraste, M.1    Castresana, J.2
  • 253
    • 0023059022 scopus 로고
    • A gene in Paracoccus for subunit III of cytochrome oxidase
    • Saraste, M., M. Raitio, T. Jalli, and A. Peramaa. 1986. A gene in Paracoccus for subunit III of cytochrome oxidase. FEBS Lett. 206:154-156.
    • (1986) FEBS Lett. , vol.206 , pp. 154-156
    • Saraste, M.1    Raitio, M.2    Jalli, T.3    Peramaa, A.4
  • 256
    • 0027253703 scopus 로고
    • Pseudomonas aeruginosa promoters which contain a conserved GG-N10-GC motif but appear to be RpoN-independent
    • Savioz, A., A. Zimmermann, and D. Haas. 1993. Pseudomonas aeruginosa promoters which contain a conserved GG-N10-GC motif but appear to be RpoN-independent. Mol. Gen. Genet. 238:74-80.
    • (1993) Mol. Gen. Genet. , vol.238 , pp. 74-80
    • Savioz, A.1    Zimmermann, A.2    Haas, D.3
  • 257
    • 0030980669 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of the Paracoccus denitrificans porin
    • Saxena, K., O.-M. H. Richter, B. Ludwig, and R. Benz. 1997. Molecular cloning and functional characterization of the Paracoccus denitrificans porin. Eur. J. Biochem. 245:300-306.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 300-306
    • Saxena, K.1    Richter, O.-M.H.2    Ludwig, B.3    Benz, R.4
  • 258
    • 0032080514 scopus 로고    scopus 로고
    • Nitrous oxide reductase (nosZ) gene-specific PCR primers for detection of denitrifiers and three nosZ genes from marine sediments
    • Scala, D. J., and L. J. Kerkhof. 1998. Nitrous oxide reductase (nosZ) gene-specific PCR primers for detection of denitrifiers and three nosZ genes from marine sediments. FEMS Microbiol. Lett. 162:61-68.
    • (1998) FEMS Microbiol. Lett. , vol.162 , pp. 61-68
    • Scala, D.J.1    Kerkhof, L.J.2
  • 259
    • 0027446708 scopus 로고
    • Molecular biology of the LysR family of transcriptional regulators
    • Schell, M. A. 1993. Molecular biology of the LysR family of transcriptional regulators. Annu. Rev. Microbiol. 47:597-626.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 597-626
    • Schell, M.A.1
  • 262
    • 0029155341 scopus 로고
    • Identification of periplasmic nitrate reductase Mo(V) EPR signals in intact cells of Paracoccus denitrificans
    • Sears, H. J., B. Bennett, S. Spiro, A. J. Thomson, and D. J. Richardson. 1995. Identification of periplasmic nitrate reductase Mo(V) EPR signals in intact cells of Paracoccus denitrificans. Biochem. J. 310:311-314.
    • (1995) Biochem. J. , vol.310 , pp. 311-314
    • Sears, H.J.1    Bennett, B.2    Spiro, S.3    Thomson, A.J.4    Richardson, D.J.5
  • 263
    • 0031464531 scopus 로고    scopus 로고
    • Effect of carbon substrate and aeration on nitrate reduction and expression of the periplasmic and membrane-bound nitrate reductases in carbon-limited continuous cultures of Paracoccus denitrificans Pd1222
    • Sears, H. J., S. Spiro, and D. J. Richardson. 1997. Effect of carbon substrate and aeration on nitrate reduction and expression of the periplasmic and membrane-bound nitrate reductases in carbon-limited continuous cultures of Paracoccus denitrificans Pd1222. Microbiology 143:3767-3774.
    • (1997) Microbiology , vol.143 , pp. 3767-3774
    • Sears, H.J.1    Spiro, S.2    Richardson, D.J.3
  • 264
    • 0021931295 scopus 로고
    • Nitric oxide-dependent proton translocation in various denitrifiers
    • Shapleigh, J. P., and W. J. Payne. 1985. Nitric oxide-dependent proton translocation in various denitrifiers. J. Bacteriol. 163:837-840.
    • (1985) J. Bacteriol. , vol.163 , pp. 837-840
    • Shapleigh, J.P.1    Payne, W.J.2
  • 265
    • 0021103983 scopus 로고
    • Homology between CAP and Fnr, a regulator of anaerobic respiration in Escherichia coli
    • Shaw, D. J., D. W. Rice, and J. R. Guest. 1983. Homology between CAP and Fnr, a regulator of anaerobic respiration in Escherichia coli. J. Mol. Biol. 1983:241-247.
    • (1983) J. Mol. Biol. , vol.1983 , pp. 241-247
    • Shaw, D.J.1    Rice, D.W.2    Guest, J.R.3
  • 266
    • 0024677088 scopus 로고
    • Micrococcus luteus homolog of the Escherichia coli uvrA gene: Identification of a mutation in the UV-sensitive mutant DB7
    • Shiota, S., and H. Nakayama. 1989. Micrococcus luteus homolog of the Escherichia coli uvrA gene: identification of a mutation in the UV-sensitive mutant DB7. Mol. Gen. Genet. 217:332-340.
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 332-340
    • Shiota, S.1    Nakayama, H.2
  • 267
    • 0029820169 scopus 로고    scopus 로고
    • Isolation and characterization of a new gram-negative, acetone-degrading, nitrate-reducing bacterium from soil, Paracoccus solventivorans sp. nov
    • Siller, H., F. A. Rainey, E. Stackebrandt, and J. Winter. 1996. Isolation and characterization of a new gram-negative, acetone-degrading, nitrate-reducing bacterium from soil, Paracoccus solventivorans sp. nov. Int. J. Syst. Bacteriol. 46:1125-1130.
    • (1996) Int. J. Syst. Bacteriol. , vol.46 , pp. 1125-1130
    • Siller, H.1    Rainey, F.A.2    Stackebrandt, E.3    Winter, J.4
  • 270
    • 0026326008 scopus 로고
    • Electrophoretic separation of the three Rhizobium meliloti replicons
    • Sobral, B. W. S., R. J. Honeycutt, A. G. Atherly, and M. Mcclelland. 1991. Electrophoretic separation of the three Rhizobium meliloti replicons. J. Bacteriol. 173:5173-5180.
    • (1991) J. Bacteriol. , vol.173 , pp. 5173-5180
    • Sobral, B.W.S.1    Honeycutt, R.J.2    Atherly, A.G.3    Mcclelland, M.4
  • 271
    • 0026660618 scopus 로고
    • Sequence of ISRm4 from Rhizobium meliloti strain GR4
    • Soto, M. J., A. Zorzano, J. Olivares, and N. Toro. 1992. Sequence of ISRm4 from Rhizobium meliloti strain GR4. Gene 120:125-126.
    • (1992) Gene , vol.120 , pp. 125-126
    • Soto, M.J.1    Zorzano, A.2    Olivares, J.3    Toro, N.4
  • 272
    • 0028556430 scopus 로고
    • The FNR family of transcriptional regulators
    • Spiro, S. 1994. The FNR family of transcriptional regulators. Antonie Leeuwenhoek 66:23-36.
    • (1994) Antonie Leeuwenhoek , vol.66 , pp. 23-36
    • Spiro, S.1
  • 273
    • 0025173637 scopus 로고
    • Interconversion of the DNA-binding specificities of two related transcription regulators, CRP and FNR
    • Spiro, S., K. L. Gaston, A. I. Bell, R. E. Roberts, S. J. W. Busby, and J. R. Guest. 1990. Interconversion of the DNA-binding specificities of two related transcription regulators, CRP and FNR. Mol. Microbiol. 4:1831-1838.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1831-1838
    • Spiro, S.1    Gaston, K.L.2    Bell, A.I.3    Roberts, R.E.4    Busby, S.J.W.5    Guest, J.R.6
  • 274
    • 0025820091 scopus 로고
    • Adaptive responses to oxygen limitation in Escherichia coli
    • Spiro, S., and J. R. Guest. 1991. Adaptive responses to oxygen limitation in Escherichia coli. Trends Biochem. Sci. 16:310-314.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 310-314
    • Spiro, S.1    Guest, J.R.2
  • 275
    • 0024969717 scopus 로고
    • The amino acid sequence of adenylate kinase from Paracoccus denitrificans and its relationship to mitochondrial and microbial adenylate kinases
    • Spurgin, P., A. G. Tomasselli, and E. Schiltz. 1989. The amino acid sequence of adenylate kinase from Paracoccus denitrificans and its relationship to mitochondrial and microbial adenylate kinases. Eur. J. Biochem. 179:621-628.
    • (1989) Eur. J. Biochem. , vol.179 , pp. 621-628
    • Spurgin, P.1    Tomasselli, A.G.2    Schiltz, E.3
  • 276
    • 0018276695 scopus 로고
    • The natural flavoprotein electron acceptor of trimethylamine dehydrogenase
    • Steenkamp, D. J., and M. Gallup. 1978. The natural flavoprotein electron acceptor of trimethylamine dehydrogenase. J. Biol. Chem. 253:4086-4089.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4086-4089
    • Steenkamp, D.J.1    Gallup, M.2
  • 278
    • 0025803811 scopus 로고
    • The cytochrome c reductase/oxidase respiratory pathway of Paracoccus denitrificans: Genetic and functional studies
    • Steinrücke, P., E. Gerhus, M. Jetzek, A. Turba, and B. Ludwig. 1991. The cytochrome c reductase/oxidase respiratory pathway of Paracoccus denitrificans: genetic and functional studies. J. Bioenerg. Biomembr. 23:227-239.
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 227-239
    • Steinrücke, P.1    Gerhus, E.2    Jetzek, M.3    Turba, A.4    Ludwig, B.5
  • 279
    • 0025830461 scopus 로고
    • Paracoccus denitrificans mutants deleted in the gene for subunit II of cytochrome c oxidase also lack subunit I
    • Steinrücke, P., E. Gerhus, and B. Ludwig. 1991. Paracoccus denitrificans mutants deleted in the gene for subunit II of cytochrome c oxidase also lack subunit I. J. Biol. Chem. 266:7676-7681.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7676-7681
    • Steinrücke, P.1    Gerhus, E.2    Ludwig, B.3
  • 280
    • 0027525884 scopus 로고
    • Genetics of Paracoccus denitrificans
    • Steinrücke, P., and B. Ludwig. 1993. Genetics of Paracoccus denitrificans. FEMS Microbiol. Rev. 104:83-118.
    • (1993) FEMS Microbiol. Rev. , vol.104 , pp. 83-118
    • Steinrücke, P.1    Ludwig, B.2
  • 281
    • 0023656242 scopus 로고
    • Subunit II of cytochrome c oxidase from Paracoccus denitrificans. DNA sequence, gene expression and the protein
    • Steinrücke, P., G. C. Steffens, G. Panskus, G. Buse, and B. Ludwig. 1987. Subunit II of cytochrome c oxidase from Paracoccus denitrificans. DNA sequence, gene expression and the protein. Eur. J. Biochem. 167:431-439.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 431-439
    • Steinrücke, P.1    Steffens, G.C.2    Panskus, G.3    Buse, G.4    Ludwig, B.5
  • 282
    • 0029785523 scopus 로고    scopus 로고
    • 550 expression in Paracoccus denitrificans strongly depends on growth condition: Identification of promoter region for cycA by transcription start analysis
    • 550 expression in Paracoccus denitrificans strongly depends on growth condition: identification of promoter region for cycA by transcription start analysis. Microbiology 142:2577-2585.
    • (1996) Microbiology , vol.142 , pp. 2577-2585
    • Stoll, R.1    Page, M.D.2    Sambongi, Y.3    Ferguson, S.J.4
  • 283
    • 0345536682 scopus 로고
    • Metabolic pathways in Paracoccus denitrificans and closely related bacteria in relation to the phylogeny of prokaryotes
    • Stouthamer, A. H. 1992. Metabolic pathways in Paracoccus denitrificans and closely related bacteria in relation to the phylogeny of prokaryotes. Antonie Leeuwenhoek 61:1-33.
    • (1992) Antonie Leeuwenhoek , vol.61 , pp. 1-33
    • Stouthamer, A.H.1
  • 284
    • 0031017493 scopus 로고    scopus 로고
    • Emerging principles of inorganic nitrogen metabolism in Paracoccus denitrificans and related bacteria
    • Stouthamer, A. H., A. P. N. de Boer, J. van der Oost, and R. J. M. van Spanning. 1997. Emerging principles of inorganic nitrogen metabolism in Paracoccus denitrificans and related bacteria. Antonie Leeuwenhoek 71:33-41.
    • (1997) Antonie Leeuwenhoek , vol.71 , pp. 33-41
    • Stouthamer, A.H.1    De Boer, A.P.N.2    Van Der Oost, J.3    Van Spanning, R.J.M.4
  • 285
    • 0024443488 scopus 로고
    • Physical and genetic mapping of the Rhodobacter sphaeroides 2.4.1 genome: Presence of two unique circular chromosomes
    • Suwanto, A., and S. Kaplan. 1989. Physical and genetic mapping of the Rhodobacter sphaeroides 2.4.1 genome: presence of two unique circular chromosomes. J. Bacteriol. 171:5850-5859.
    • (1989) J. Bacteriol. , vol.171 , pp. 5850-5859
    • Suwanto, A.1    Kaplan, S.2
  • 286
    • 0026013118 scopus 로고
    • Molecular cloning of the L-phenylalanine transaminase gene from Paracoccus denitrificans in Escherichia coli K12
    • Tagaki, T., T. Taniguchi, Y. Yamamoto, and T. Shibatani. 1991. Molecular cloning of the L-phenylalanine transaminase gene from Paracoccus denitrificans in Escherichia coli K12. Biotechnol. Appl. Biochem. 13:112-119.
    • (1991) Biotechnol. Appl. Biochem. , vol.13 , pp. 112-119
    • Tagaki, T.1    Taniguchi, T.2    Yamamoto, Y.3    Shibatani, T.4
  • 287
    • 0031054313 scopus 로고    scopus 로고
    • Characterization of the promoter of the Rhizobium etli recA gene
    • Tapias, A., A. R. Fernandez de Henestrosa, and J. Barbé. 1997. Characterization of the promoter of the Rhizobium etli recA gene. J. Bacteriol. 179: 1573-1579.
    • (1997) J. Bacteriol. , vol.179 , pp. 1573-1579
    • Tapias, A.1    Fernandez De Henestrosa, A.R.2    Barbé, J.3
  • 288
    • 0037990786 scopus 로고    scopus 로고
    • Biogenesis of respiratory cytochromes in bacteria
    • Thöny-Meyer, L. 1997. Biogenesis of respiratory cytochromes in bacteria. Microbiol. Mol. Biol. Rev. 61:337-376.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 337-376
    • Thöny-Meyer, L.1
  • 289
    • 0027969974 scopus 로고
    • The cco-NOQP gene cluster codes for a cb-type cytochrome oxidase that functions in aerobic respiration of Rhodobacter capsulatus
    • Thöny-Meyer, L., C. Beck, O. Preisig, and H. Hennecke. 1994. The cco-NOQP gene cluster codes for a cb-type cytochrome oxidase that functions in aerobic respiration of Rhodobacter capsulatus. Mol. Microbiol. 14:705-716.
    • (1994) Mol. Microbiol. , vol.14 , pp. 705-716
    • Thöny-Meyer, L.1    Beck, C.2    Preisig, O.3    Hennecke, H.4
  • 290
    • 0031047127 scopus 로고    scopus 로고
    • Characterization and regulation of the gene encoding nitrite reductase in Rhodobacter sphaeroides 2.4.3
    • Tosques, I. E., A. V. Kwiatkowski, J. Shi, and J. P. Shapleigh. 1997. Characterization and regulation of the gene encoding nitrite reductase in Rhodobacter sphaeroides 2.4.3. J. Bacteriol. 179:1090-1095.
    • (1997) J. Bacteriol. , vol.179 , pp. 1090-1095
    • Tosques, I.E.1    Kwiatkowski, A.V.2    Shi, J.3    Shapleigh, J.P.4
  • 292
    • 0029909888 scopus 로고    scopus 로고
    • Molecular analysis of the Rhodobacter capsulatus B10 porin (porCa) gene: Purification and biochemical characterization of the porin protein
    • Trieschmann, M. D. A., F. Pattus, and M. H. Tadros. 1996. Molecular analysis of the Rhodobacter capsulatus B10 porin (porCa) gene: purification and biochemical characterization of the porin protein. Mol. Gen. Genet. 253:253-258.
    • (1996) Mol. Gen. Genet. , vol.253 , pp. 253-258
    • Trieschmann, M.D.A.1    Pattus, F.2    Tadros, M.H.3
  • 293
    • 0025194064 scopus 로고
    • 1 complexes of microorganisms
    • 1 complexes of microorganisms. Microbiol. Rev. 54:101-129.
    • (1990) Microbiol. Rev. , vol.54 , pp. 101-129
    • Trumpower, B.L.1
  • 294
    • 0028290824 scopus 로고
    • Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: The enzymology of coupling electron transfer reactions to transmembrane proton translocation
    • Trumpower, B. L., and R. B. Gennis. 1994. Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: the enzymology of coupling electron transfer reactions to transmembrane proton translocation. Annu. Rev. Biochem. 63:675-716.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 675-716
    • Trumpower, B.L.1    Gennis, R.B.2
  • 295
    • 3743098397 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 296
    • 3743092743 scopus 로고
    • Ph.D. thesis. University of Frankfurt, Frankfurt, Germany
    • Turba, A. 1993. Ph.D. thesis. University of Frankfurt, Frankfurt, Germany.
    • (1993)
    • Turba, A.1
  • 299
    • 0026611786 scopus 로고
    • 550 from Thiobacillus versutus: Cloning, expression in Escherichia coli, and purification of the heterologous holoprotein
    • 550 from Thiobacillus versutus: cloning, expression in Escherichia coli, and purification of the heterologous holoprotein. J. Bacteriol. 174:3707-3714.
    • (1993) J. Bacteriol. , vol.174 , pp. 3707-3714
    • Ubbink, M.1    Van Beeumen, J.2    Canters, G.W.3
  • 300
    • 0026342987 scopus 로고
    • Cloning, sequencing and expression studies of the genes encoding amicyanin and the beta-subunit of methylamine dehydrogenase from Thiobacillus versutus
    • Ubbink, M., M. A. van Kleef, D. J. Kleinjan, C. W. Hoitink, F. Huitema, J. J. Beintema, J. A. Duine, and G. W. Canters. 1991. Cloning, sequencing and expression studies of the genes encoding amicyanin and the beta-subunit of methylamine dehydrogenase from Thiobacillus versutus. Eur. J. Biochem. 202:1003-1012.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1003-1012
    • Ubbink, M.1    Van Kleef, M.A.2    Kleinjan, D.J.3    Hoitink, C.W.4    Huitema, F.5    Beintema, J.J.6    Duine, J.A.7    Canters, G.W.8
  • 301
    • 0030024162 scopus 로고    scopus 로고
    • Molecular analysis of the poly(3-hydroxyalkanoate) synthase gene from a methylotrophic bacterium, Paracoccus denitrificans
    • Ueda, S., T. Yabutani, A. Maehara, and S. Yamane. 1996. Molecular analysis of the poly(3-hydroxyalkanoate) synthase gene from a methylotrophic bacterium, Paracoccus denitrificans. J. Bacteriol. 178:774-779.
    • (1996) J. Bacteriol. , vol.178 , pp. 774-779
    • Ueda, S.1    Yabutani, T.2    Maehara, A.3    Yamane, S.4
  • 302
    • 0030738589 scopus 로고    scopus 로고
    • The oxygen-responsive transcriptional regulator FNR of Escherichia coli: The search for signals and reactions
    • Unden, G., and J. Schirawski. 1997. The oxygen-responsive transcriptional regulator FNR of Escherichia coli: the search for signals and reactions. Biochim. Biophys. Acta 1320:217-234.
    • (1997) Biochim. Biophys. Acta , vol.1320 , pp. 217-234
    • Unden, G.1    Schirawski, J.2
  • 303
    • 0025358474 scopus 로고
    • Paracoccus aminophilus sp. nov. and Paracoccus aminovorans sp. nov., which utilize N,N-dimethylformamide
    • Urakami, T., H. Araki, H. Oyangi, K.-I. Suzuki, and K. Komagata. 1990. Paracoccus aminophilus sp. nov. and Paracoccus aminovorans sp. nov., which utilize N,N-dimethylformamide. Int. J. Syst. Bacteriol. 40:287-291.
    • (1990) Int. J. Syst. Bacteriol. , vol.40 , pp. 287-291
    • Urakami, T.1    Araki, H.2    Oyangi, H.3    Suzuki, K.-I.4    Komagata, K.5
  • 304
    • 0024503638 scopus 로고
    • Paracoccus alcaliphilus sp. nov., an alciphilic and facultatively methylotrophic bacterium
    • Urakami, T., J. Tamaoka, K.-I. Suzuki, and K. Komagata. 1989. Paracoccus alcaliphilus sp. nov., an alciphilic and facultatively methylotrophic bacterium. Int. J. Syst. Bacteriol. 39:116-121.
    • (1989) Int. J. Syst. Bacteriol. , vol.39 , pp. 116-121
    • Urakami, T.1    Tamaoka, J.2    Suzuki, K.-I.3    Komagata, K.4
  • 308
    • 0028153789 scopus 로고
    • NAD- and co-substrate (GSH or factor)-dependent formaldehyde dehydrogenases from methylotrophic microorganisms act as a class III alcohol dehydrogenase
    • van Ophem, P. W., and J. A. Duine. 1994. NAD- and co-substrate (GSH or factor)-dependent formaldehyde dehydrogenases from methylotrophic microorganisms act as a class III alcohol dehydrogenase. FEMS Microbiol. Lett. 116:87-93.
    • (1994) FEMS Microbiol. Lett. , vol.116 , pp. 87-93
    • Van Ophem, P.W.1    Duine, J.A.2
  • 312
    • 0028959433 scopus 로고
    • Nitrite and nitric oxide reduction in Paracoccus denitrificans is under the control of NNR, a regulatory protein that belongs to the FNR family of transcriptional activators
    • van Spanning, R. J. M., A. P. N. de Boer, W. N. M. Reijnders, S. Spiro, H. V. Westerhoff, A. H. Stouthamer, and J. van der Oost. 1995. Nitrite and nitric oxide reduction in Paracoccus denitrificans is under the control of NNR, a regulatory protein that belongs to the FNR family of transcriptional activators. FEBS Lett. 360:151-154.
    • (1995) FEBS Lett. , vol.360 , pp. 151-154
    • Van Spanning, R.J.M.1    De Boer, A.P.N.2    Reijnders, W.N.M.3    Spiro, S.4    Westerhoff, H.V.5    Stouthamer, A.H.6    Van Der Oost, J.7
  • 313
    • 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. M., A. P. N. de Boer, W. N. M. Reijnders, H. V. Westerhoff, A. H. Stouthamer, and J. van der Oost. 1997. 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. 23:893-907.
    • (1997) Mol. Microbiol. , vol.23 , pp. 893-907
    • Van Spanning, R.J.M.1    De Boer, A.P.N.2    Reijnders, W.N.M.3    Westerhoff, H.V.4    Stouthamer, A.H.5    Van Der Oost, J.6
  • 314
    • 0029147556 scopus 로고
    • Isolation and characterization of a novel insertion sequence element, IS1248, in Paracoccus denitrificans
    • van Spanning, R. J. M., A. P. N. de Boer, D. J. Slotboom, W. N. M. Reijnders, and A. H. Stouthamer. 1995. Isolation and characterization of a novel insertion sequence element, IS1248, in Paracoccus denitrificans. Plasmid 34:11-21.
    • (1995) Plasmid , vol.34 , pp. 11-21
    • Van Spanning, R.J.M.1    De Boer, A.P.N.2    Slotboom, D.J.3    Reijnders, W.N.M.4    Stouthamer, A.H.5
  • 315
    • 0029120102 scopus 로고
    • Integration of heterologous DNA into the genome of Paracoccus denitrificans is mediated by a family of 151248-related elements and a second type of integrative recombination event
    • van Spanning, R. J. M., W. N. M. Reijnders, and A. H. Stouthamer. 1995. Integration of heterologous DNA into the genome of Paracoccus denitrificans is mediated by a family of 151248-related elements and a second type of integrative recombination event. J. Bacteriol. 177:4772-4778.
    • (1995) J. Bacteriol. , vol.177 , pp. 4772-4778
    • Van Spanning, R.J.M.1    Reijnders, W.N.M.2    Stouthamer, A.H.3
  • 316
    • 0027996934 scopus 로고
    • Expression of the mau genes involved in methylamine metabolism in Paracoccus denitrificans is under control of a LysR-type transcriptional activator
    • van Spanning, R. J. M., C. J. N. M. van der Palen, D. J. Slotboom, W. N. M. Reijnders, A. H. Stouthamer, and J. A. Duine. 1994. Expression of the mau genes involved in methylamine metabolism in Paracoccus denitrificans is under control of a LysR-type transcriptional activator. Eur. J. Biochem. 226:201-210.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 201-210
    • Van Spanning, R.J.M.1    Van Der Palen, C.J.N.M.2    Slotboom, D.J.3    Reijnders, W.N.M.4    Stouthamer, A.H.5    Duine, J.A.6
  • 317
    • 0025885443 scopus 로고
    • Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of Paracoccus denitrificans: Inactivation of moxJ, moxG, and moxR and the resultant effect on methylotrophic growth
    • van Spanning, R. J. M., C. W. Wansell, A. P. N. de Boer, M. J. Hazelaar, H. Anazawa, N. Harms, L. F. Oltmann, and A. H. Stouthamer. 1991. Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of Paracoccus denitrificans: inactivation of moxJ, moxG, and moxR and the resultant effect on methylotrophic growth. J. Bacteriol. 173:6948-6961.
    • (1991) J. Bacteriol. , vol.173 , pp. 6948-6961
    • Van Spanning, R.J.M.1    Wansell, C.W.2    De Boer, A.P.N.3    Hazelaar, M.J.4    Anazawa, H.5    Harms, N.6    Oltmann, L.F.7    Stouthamer, A.H.8
  • 320
    • 0025149403 scopus 로고
    • Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation
    • van Spanning, R. J. M., C. W. Wansell, W. N. Reijnders, L. F. Oltmann, and A. H. Stouthamer. 1990. Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation. FEBS Lett. 275:217-220.
    • (1990) FEBS Lett. , vol.275 , pp. 217-220
    • Van Spanning, R.J.M.1    Wansell, C.W.2    Reijnders, W.N.3    Oltmann, L.F.4    Stouthamer, A.H.5
  • 321
    • 0017889486 scopus 로고
    • Growth yields and the efficiency of oxidative phosphorylation during autotrophic growth of Paracoccus denitrificans on methanol and formate
    • van Verseveld, H. W., and A. H. Stouthamer. 1978. Growth yields and the efficiency of oxidative phosphorylation during autotrophic growth of Paracoccus denitrificans on methanol and formate. Arch. Microbiol. 118:21-26.
    • (1978) Arch. Microbiol. , vol.118 , pp. 21-26
    • Van Verseveld, H.W.1    Stouthamer, A.H.2
  • 322
    • 51249194287 scopus 로고
    • Studies on true dissimilatory nitrate reduction. V. Nitric oxide production and consumption by microorganisms
    • Verhoeven, W. 1956. Studies on true dissimilatory nitrate reduction. V. Nitric oxide production and consumption by microorganisms. Antonie Leeuwenhoek 22:384-406.
    • (1956) Antonie Leeuwenhoek , vol.22 , pp. 384-406
    • Verhoeven, W.1
  • 323
    • 0028300062 scopus 로고
    • Influence of the lipid matrix on incorporation and function of LPS-free porin from Paracoccus denitrificans
    • Wiese, A., G. Schröder, K. Brandenberg, A. Hirsch, W. Welte, and V. Seydel. 1994. Influence of the lipid matrix on incorporation and function of LPS-free porin from Paracoccus denitrificans. Biochim. Biophys. Acta 1190: 231-242.
    • (1994) Biochim. Biophys. Acta , vol.1190 , pp. 231-242
    • Wiese, A.1    Schröder, G.2    Brandenberg, K.3    Hirsch, A.4    Welte, W.5    Seydel, V.6
  • 325
    • 0026317589 scopus 로고
    • The role of two surface exposed loops in transcription activation by the
    • Williams, R., A. Bell, G. Sims, and S. Busby. 1991. The role of two surface exposed loops in transcription activation by the Escherichia coli CRP and FNR proteins. Nucleic Acids Res. 19:6705-6712.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6705-6712
    • Williams, R.1    Bell, A.2    Sims, G.3    Busby, S.4
  • 326
    • 0031959474 scopus 로고    scopus 로고
    • Genes coding for respiratory complexes map on all three chromosomes of the Paracoccus denitrificans genome
    • Winterstein, C., and B. Ludwig. 1998. Genes coding for respiratory complexes map on all three chromosomes of the Paracoccus denitrificans genome. Arch. Microbiol. 169:275-281.
    • (1998) Arch. Microbiol. , vol.169 , pp. 275-281
    • Winterstein, C.1    Ludwig, B.2
  • 327
    • 3743119529 scopus 로고    scopus 로고
    • Chimeric quinol oxidases expressed in Paracoccus denitrificans
    • Winterstein, C., O.-M. Richter, and B. Ludwig. 1998. Chimeric quinol oxidases expressed in Paracoccus denitrificans. NATO ASI Ser. c512:259-269.
    • (1998) NATO ASI Ser. , vol.C512 , pp. 259-269
    • Winterstein, C.1    Richter, O.-M.2    Ludwig, B.3
  • 328
    • 0031054250 scopus 로고    scopus 로고
    • Isolation, analysis and deletion of the gene coding for subunit IV of cytochrome c oxidase in Paracoccus denitrificans
    • Witt, H., and B. Ludwig. 1997. Isolation, analysis and deletion of the gene coding for subunit IV of cytochrome c oxidase in Paracoccus denitrificans. J. Biol. Chem. 272:5514-5517.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5514-5517
    • Witt, H.1    Ludwig, B.2
  • 329
    • 0030843666 scopus 로고    scopus 로고
    • Cloning and characterization of sulfite dehydrogenase, two c-type cytochromes, and a flavoprotein of Paracoccus denitrificans GB-17: Essential role of sulfite dehydrogenase in lithotrophic sulfur oxidation
    • Wodara, C., F. Bardischewsky, and C. G. Friedrich. 1997. Cloning and characterization of sulfite dehydrogenase, two c-type cytochromes, and a flavoprotein of Paracoccus denitrificans GB-17: essential role of sulfite dehydrogenase in lithotrophic sulfur oxidation. J. Bacteriol. 179:5014-5023.
    • (1997) J. Bacteriol. , vol.179 , pp. 5014-5023
    • Wodara, C.1    Bardischewsky, F.2    Friedrich, C.G.3
  • 330
    • 0028149485 scopus 로고
    • Identification and sequence analysis of the soxB gene essential for sulfur oxidation of Paracoccus denitrificans GB-17
    • Wodara, C., S. Kostka, M. Egert, D. P. Kelly, and C. G. Friedrich. 1994. Identification and sequence analysis of the soxB gene essential for sulfur oxidation of Paracoccus denitrificans GB-17. J. Bacteriol. 176:6188-6191.
    • (1994) J. Bacteriol. , vol.176 , pp. 6188-6191
    • Wodara, C.1    Kostka, S.2    Egert, M.3    Kelly, D.P.4    Friedrich, C.G.5
  • 331
    • 3743129718 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 332
    • 0023184331 scopus 로고
    • Bacterial evolution
    • Woese, C. R. 1987. Bacterial evolution. Microbiol. Rev. 51:221-271.
    • (1987) Microbiol. Rev. , vol.51 , pp. 221-271
    • Woese, C.R.1
  • 333
    • 0028818304 scopus 로고
    • Nucleotide sequence of the mxcQ and mxcE genes, required for methanol dehydrogenase synthesis in Methylobacterium organophilum XX: A two-component regulatory system
    • Xu, H. H., J. J. Janka, M. Viebahn, and R S. Hanson. 1995. Nucleotide sequence of the mxcQ and mxcE genes, required for methanol dehydrogenase synthesis in Methylobacterium organophilum XX: a two-component regulatory system. Microbiology 141:2543-2551.
    • (1995) Microbiology , vol.141 , pp. 2543-2551
    • Xu, H.H.1    Janka, J.J.2    Viebahn, M.3    Hanson, R.S.4
  • 334
    • 0025952505 scopus 로고
    • Characterization of the 25-kilodalton subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: Sequence similarity to the 24-kilodalton subunit of the flavoprotein fraction of mammalian complex I
    • Xu, X. M., A. Matsuno-Yagi, and T. Yagi. 1991. Characterization of the 25-kilodalton subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: sequence similarity to the 24-kilodalton subunit of the flavoprotein fraction of mammalian complex I. Biochemistry 30:8678-8684.
    • (1991) Biochemistry , vol.30 , pp. 8678-8684
    • Xu, X.M.1    Matsuno-Yagi, A.2    Yagi, T.3
  • 335
    • 0025779257 scopus 로고
    • The NADH-binding subunit of the energy-transducing NADH-ubiquinone oridoreductase of Paracoccus denitrificans: Gene cloning and deduced primary structure
    • Xu, X. M., A. Matsuno-Yagi, and T. Yagi. 1991. The NADH-binding subunit of the energy-transducing NADH-ubiquinone oridoreductase of Paracoccus denitrificans: gene cloning and deduced primary structure. Biochemistry 30:6422-6428.
    • (1991) Biochemistry , vol.30 , pp. 6422-6428
    • Xu, X.M.1    Matsuno-Yagi, A.2    Yagi, T.3
  • 336
    • 0026686343 scopus 로고
    • Gene cluster of the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans: Characterization of four structural gene products
    • Xu, X. M., A. Matsnno-Yagi, and T. Yagi. 1992. Gene cluster of the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans: characterization of four structural gene products. Biochemistry 31:6925-6932.
    • (1992) Biochemistry , vol.31 , pp. 6925-6932
    • Xu, X.M.1    Matsnno-Yagi, A.2    Yagi, T.3
  • 337
    • 0026634739 scopus 로고
    • Structural features of the 66-kDa subunit of the energy-transducing NADH-ubiquinone oxidoreductase (NDH-1) at Paracoccus denitrificans
    • Xu, X. M., A. Matsuno-Yagi, and T. Yagi. 1992. Structural features of the 66-kDa subunit of the energy-transducing NADH-ubiquinone oxidoreductase (NDH-1) at Paracoccus denitrificans. Arch. Biochem. Biophys. 296:40-48.
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 40-48
    • Xu, X.M.1    Matsuno-Yagi, A.2    Yagi, T.3
  • 338
    • 0027477868 scopus 로고
    • DNA sequencing of the seven remaining structural genes of the gene cluster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Xu, X. M., A. Matsuno-Yagi, and T. Yagi. 1993. DNA sequencing of the seven remaining structural genes of the gene cluster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans. Biochemistry 32:968-981.
    • (1993) Biochemistry , vol.32 , pp. 968-981
    • Xu, X.M.1    Matsuno-Yagi, A.2    Yagi, T.3
  • 339
    • 0028972673 scopus 로고
    • Analysis of β-thioketolase and aceto-acetyl-coA reductase genes of a methylotrophic bacterium, Paracoccus denitrificans, and their expression in Escherichia coli
    • Yabutani, T., A. Maehara, S. Ueda, and T. Yamane. 1995. Analysis of β-thioketolase and aceto-acetyl-coA reductase genes of a methylotrophic bacterium, Paracoccus denitrificans, and their expression in Escherichia coli. FEMS Microbiol. Lett. 133:85-90.
    • (1995) FEMS Microbiol. Lett. , vol.133 , pp. 85-90
    • Yabutani, T.1    Maehara, A.2    Ueda, S.3    Yamane, T.4
  • 340
    • 0023512814 scopus 로고
    • The blue copper protein gene of Alcaligenes faecalis S-6 directs secretion of blue copper protein from Escherichia coli cells
    • Yamamoto, K., T. Uozumi, and T. Beppu. 1987. The blue copper protein gene of Alcaligenes faecalis S-6 directs secretion of blue copper protein from Escherichia coli cells. J. Bacteriol. 169:5648-5652.
    • (1987) J. Bacteriol. , vol.169 , pp. 5648-5652
    • Yamamoto, K.1    Uozumi, T.2    Beppu, T.3
  • 341
    • 0030031770 scopus 로고    scopus 로고
    • Polyhroxyalkanoate synthesis from alcohols during the growth of Paracoccus denitrificans
    • Yamane, T., X.-F. Chen, and S. Uda. 1996. Polyhroxyalkanoate synthesis from alcohols during the growth of Paracoccus denitrificans. FEMS Microbiol. Lett. 135:207-211.
    • (1996) FEMS Microbiol. Lett. , vol.135 , pp. 207-211
    • Yamane, T.1    Chen, X.-F.2    Uda, S.3
  • 342
    • 0029000413 scopus 로고
    • Expression of the structural max genes in Paracoccus denitrificans follows wild-type regulation in mutants with a deletion in mxaY, the gene encoding the signal sensor
    • Yang, H., W. N. M. Reijnders, R. J. M. van Spanning, A. H. Stouthamer, and N. Harms. 1995. Expression of the structural max genes in Paracoccus denitrificans follows wild-type regulation in mutants with a deletion in mxaY, the gene encoding the signal sensor. Microbiology 141:825-830.
    • (1995) Microbiology , vol.141 , pp. 825-830
    • Yang, H.1    Reijnders, W.N.M.2    Van Spanning, R.J.M.3    Stouthamer, A.H.4    Harms, N.5
  • 343
    • 0022972966 scopus 로고
    • Purification of a three-subunit ubiquinol-cytochrome c oxidoreductase complex from Paracoccus denitrificans
    • Yang, X., and B. L. Trumpower. 1986. Purification of a three-subunit ubiquinol-cytochrome c oxidoreductase complex from Paracoccus denitrificans. J. Biol. Chem. 261:12282-12289.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12282-12289
    • Yang, X.1    Trumpower, B.L.2
  • 344
    • 0023780753 scopus 로고
    • Protonmotive Q cycle pathway of electron transfer and energy transduction in the three-subunit ubiquinol-cytochrome c oxidoreductase complex of Paracoccus denitrificans
    • Yang, X., and B. L. Trumpower. 1988. Protonmotive Q cycle pathway of electron transfer and energy transduction in the three-subunit ubiquinol-cytochrome c oxidoreductase complex of Paracoccus denitrificans. J. Biol. Chem. 263:11962-11970.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11962-11970
    • Yang, X.1    Trumpower, B.L.2
  • 345
    • 0027531490 scopus 로고
    • Characterization of the structural gene encoding a copper-containing nitrite reductase and homology of this gene to DNA of other denitrifiers
    • Ye, R. W., M. R. Fries, S. G. Bezborodnikov, B. A. Averill, and J. M. Tiedje. 1993. Characterization of the structural gene encoding a copper-containing nitrite reductase and homology of this gene to DNA of other denitrifiers. Appl. Environ. Microbiol. 59:250-254.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 250-254
    • Ye, R.W.1    Fries, M.R.2    Bezborodnikov, S.G.3    Averill, B.A.4    Tiedje, J.M.5
  • 346
    • 0020404141 scopus 로고
    • Molecular cloning of the ribosomal RNA genes of the photosynthetic bacterium Rhodopseudomonas capsulata
    • Yu, P. L., B. Hohn, H. Falk, and G. Drews. 1982. Molecular cloning of the ribosomal RNA genes of the photosynthetic bacterium Rhodopseudomonas capsulata. Mol. Gen. Genet. 188:392-398.
    • (1982) Mol. Gen. Genet. , vol.188 , pp. 392-398
    • Yu, P.L.1    Hohn, B.2    Falk, H.3    Drews, G.4
  • 347
    • 0021919152 scopus 로고
    • Dimeric porin from Paracoccus denitrificans
    • Zalman, L. S., and H. Nikaido. 1984. Dimeric porin from Paracoccus denitrificans. J. Bacteriol. 162:430-433.
    • (1984) J. Bacteriol. , vol.162 , pp. 430-433
    • Zalman, L.S.1    Nikaido, H.2
  • 350
    • 0027326619 scopus 로고
    • The biological role of nitric oxide in bacteria
    • Zumft, W. G. 1993. The biological role of nitric oxide in bacteria. Arch. Microbiol. 160:253-264.
    • (1993) Arch. Microbiol. , vol.160 , pp. 253-264
    • Zumft, W.G.1
  • 351
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • Zumft, W. G. 1998. Cell biology and molecular basis of denitrification. Microbiol. Mol. Biol. Rev. 61:533-616.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 533-616
    • Zumft, W.G.1
  • 353
    • 0031018503 scopus 로고    scopus 로고
    • Enzyme diversity and mosaic gene organisation in denitrification
    • Zumft, W. G., and H. Korner. 1997. Enzyme diversity and mosaic gene organisation in denitrification. Antonie Leeuwenhoek 71:43-58.
    • (1997) Antonie Leeuwenhoek , vol.71 , pp. 43-58
    • Zumft, W.G.1    Korner, H.2
  • 354
    • 0028158048 scopus 로고
    • Nitric oxide reductase from Pseudomonas stutzeri. Primary structure and gene organisation of a novel bacterial cytochrome bc complex
    • Zumft, W. G., C. Braun, and H. Cuypers. 1994. Nitric oxide reductase from Pseudomonas stutzeri. Primary structure and gene organisation of a novel bacterial cytochrome bc complex. Eur. J. Biochem. 219:481-490.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 481-490
    • Zumft, W.G.1    Braun, C.2    Cuypers, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.