메뉴 건너뛰기




Volumn 180, Issue 8, 1998, Pages 2133-2136

Availability of O2 as a substrate in the cytoplasm of bacteria under aerobic and microaerobic conditions

Author keywords

[No Author keywords available]

Indexed keywords

4 HYDROXYBENZOIC ACID; BENZOIC ACID; BENZOIC ACID DERIVATIVE; GLUCOSE; OXYGEN; SUCCINIC ACID; 4 HYDROXYBENZOIC ACID ESTER; 4 METHYLBENZOIC ACID; 4-HYDROXYBENZOIC ACID; 4-TOLUIC ACID; CATECHOL 1,2 DIOXYGENASE; CATECHOL DERIVATIVE; DIOXYGENASE; OXYGENASE; SUCCINIC ACID DERIVATIVE;

EID: 0031596608     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.8.2133-2136.1998     Document Type: Article
Times cited : (36)

References (25)
  • 1
    • 14444287491 scopus 로고
    • Springer-Verlag KG, Berlin, Germany
    • Barman, T. E. 1969. Enzyme handbook, vol. 1, p. 237-238. Springer-Verlag KG, Berlin, Germany.
    • (1969) Enzyme Handbook , vol.1 , pp. 237-238
    • Barman, T.E.1
  • 3
    • 0030609907 scopus 로고    scopus 로고
    • 2 tensions for the synthesis of fermentation products in Escherichia coli and relation to aerobic respiration
    • 2 tensions for the synthesis of fermentation products in Escherichia coli and relation to aerobic respiration. Arch. Microbiol. 168:290-296.
    • (1997) Arch. Microbiol. , vol.168 , pp. 290-296
    • Becker, S.1    Vlad, D.2    Schuster, S.3    Pfeiffer, P.4    Unden, G.5
  • 4
    • 0029981912 scopus 로고    scopus 로고
    • The cytpochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: Implications for regulation of activity in vivo by oxygen inhibition
    • D'mello, R., S. Hill, and R. K. Poole. 1996. The cytpochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: implications for regulation of activity in vivo by oxygen inhibition. Microbiology 142:755-763.
    • (1996) Microbiology , vol.142 , pp. 755-763
    • D'mello, R.1    Hill, S.2    Poole, R.K.3
  • 5
    • 0005536404 scopus 로고
    • Molecular and functional analysis of the TOL plasmid pWWO from Pseudomonas putida and cloning of genes for the entire regulated aromatic ring meta cleavage pathway
    • Franklin, F. C. H., M. Bagdasarin, M. M. Bagdasarin, and K. N. Timmis. 1981. Molecular and functional analysis of the TOL plasmid pWWO from Pseudomonas putida and cloning of genes for the entire regulated aromatic ring meta cleavage pathway. Proc. Natl. Acad. Sci. USA 78:7458-7462.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 7458-7462
    • Franklin, F.C.H.1    Bagdasarin, M.2    Bagdasarin, M.M.3    Timmis, K.N.4
  • 6
    • 0001020596 scopus 로고
    • Protocatechuate 3,4-dioxygenase (Pseudomonas)
    • Fujisawa, H. 1970. Protocatechuate 3,4-dioxygenase (Pseudomonas). Methods Enzymol. 17A:526-529.
    • (1970) Methods Enzymol. , vol.17 A , pp. 526-529
    • Fujisawa, H.1
  • 7
    • 0026805891 scopus 로고
    • Functional and evolutionary relationships among diverse oxygenases
    • Harayama, S., and M. Kok. 1992. Functional and evolutionary relationships among diverse oxygenases. Annu. Rev. Microbiol. 46:565-601.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 565-601
    • Harayama, S.1    Kok, M.2
  • 8
    • 0029107745 scopus 로고
    • Efficacy in aquatic microcosms of a genetically engineered pseudomonad applicable for bioremediation
    • Heuer, H., D. F. Dwyer, K. N. Timmis, and I. Wagner-Döbler. 1995. Efficacy in aquatic microcosms of a genetically engineered pseudomonad applicable for bioremediation. Microb. Ecol. 29:203-220.
    • (1995) Microb. Ecol. , vol.29 , pp. 203-220
    • Heuer, H.1    Dwyer, D.F.2    Timmis, K.N.3    Wagner-Döbler, I.4
  • 9
    • 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
  • 10
    • 0026743341 scopus 로고
    • The electron transport proteins of hydroxylating bacterial dioxygenases
    • Mason, J. R., and R. Cammack. 1992. The electron transport proteins of hydroxylating bacterial dioxygenases. Annu. Rev. Microbiol. 46:277-305.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 277-305
    • Mason, J.R.1    Cammack, R.2
  • 12
    • 77956986735 scopus 로고
    • Pyrocatechase (Pseudomonas)
    • Nakazawa, T., and A. Nakazawa. 1970. Pyrocatechase (Pseudomonas). Methods Enzymol. 17A:518-522.
    • (1970) Methods Enzymol. , vol.17 A , pp. 518-522
    • Nakazawa, T.1    Nakazawa, A.2
  • 13
    • 77956993726 scopus 로고
    • Metapyrocatechase (Pseudomonas)
    • Nozaki, M. 1970. Metapyrocatechase (Pseudomonas). Methods Enzymol. Vol 17A:522-525.
    • (1970) Methods Enzymol. , vol.17 A , pp. 522-525
    • Nozaki, M.1
  • 14
  • 15
    • 0029670068 scopus 로고    scopus 로고
    • A high-affinity cbb3-type cytochrome oxidase terminates the symbiosis-specific respiratory chain of Bradyrhizobium japonicum
    • Preisig, O., R. Zuffrey, L. Thöny-Meyer, C. A. Appleby, and H. Hennecke. 1996. A high-affinity cbb3-type cytochrome oxidase terminates the symbiosis-specific respiratory chain of Bradyrhizobium japonicum. J. Bacteriol. 178: 1532-1538.
    • (1996) J. Bacteriol. , vol.178 , pp. 1532-1538
    • Preisig, O.1    Zuffrey, R.2    Thöny-Meyer, L.3    Appleby, C.A.4    Hennecke, H.5
  • 16
    • 0017858515 scopus 로고
    • Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli
    • Rice, C. W., and W. P. Hempfling. 1978. Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli. J. Bacteriol. 134:115-124.
    • (1978) J. Bacteriol. , vol.134 , pp. 115-124
    • Rice, C.W.1    Hempfling, W.P.2
  • 17
    • 0025866366 scopus 로고
    • Identification and molecular characterization of a transcriptional regulator from Pseudomonas aeruginosa PAO1 exhibiting structural and functional similarity to the FNR protein of Escherichia coli
    • Sawers, R. G. 1991. Identification and molecular characterization of a transcriptional regulator from Pseudomonas aeruginosa PAO1 exhibiting structural and functional similarity to the FNR protein of Escherichia coli. Mol. Microbiol. 5:1469-1481.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1469-1481
    • Sawers, R.G.1
  • 19
    • 0024989737 scopus 로고
    • FNR and its role in oxygen-regulated gene expression in Escherichia coli
    • Spiro. S., and J. R. Guest. 1990. FNR and its role in oxygen-regulated gene expression in Escherichia coli. FEMS Microbiol. Rev. 75:399-428.
    • (1990) FEMS Microbiol. Rev. , vol.75 , pp. 399-428
    • Spiro, S.1    Guest, J.R.2
  • 20
    • 0031047287 scopus 로고    scopus 로고
    • Requirement for the proton-pumping NADH dehydrogenase I of Escherichia coli in NADH→fumarate respiration and bioenergetic implications
    • Tran, Q. H., J. Bongaerts, D. Vlad, and G. Unden. 1997. Requirement for the proton-pumping NADH dehydrogenase I of Escherichia coli in NADH→fumarate respiration and bioenergetic implications. Eur. J. Biochem. 244:155-160.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 155-160
    • Tran, Q.H.1    Bongaerts, J.2    Vlad, D.3    Unden, G.4
  • 23
    • 0030756106 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. Mol. Microbiol. 25:205-210.
    • (1997) Mol. Microbiol. , vol.25 , pp. 205-210
    • Unden, G.1    Schirawski, J.2
  • 24
    • 0026615646 scopus 로고
    • Evaluation of aquatic sediment microcosms and their use in assessing effects on introduced microorganisms on ecosystem parameters
    • Wagner-Döbler, I., R. Pipke, K. N. Timmis, and D. F. Dwyer. 1992. Evaluation of aquatic sediment microcosms and their use in assessing effects on introduced microorganisms on ecosystem parameters. Appl. Environ. Microbiol. 58:1249-1258.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1249-1258
    • Wagner-Döbler, I.1    Pipke, R.2    Timmis, K.N.3    Dwyer, D.F.4
  • 25
    • 0025873743 scopus 로고
    • Anaerobic growth and cyanide synthesis of Pseudomonas aeruginosa depend on anr, a regulatory gene homologous with fnr of Escherichia coli
    • Zimmermann, A., C. Reimmann, M. Galimand, and D. Haas. 1991. Anaerobic growth and cyanide synthesis of Pseudomonas aeruginosa depend on anr, a regulatory gene homologous with fnr of Escherichia coli. Mol. Microbiol. 5:1483-1490.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1483-1490
    • Zimmermann, A.1    Reimmann, C.2    Galimand, M.3    Haas, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.