메뉴 건너뛰기




Volumn 145, Issue 7, 1999, Pages 1743-1748

Evidence for the presence of the reductive pentose phosphate cycle in a filamentous anoxygenic photosynthetic bacterium, Oscillochloris trichoides strain DG-6

Author keywords

CO2 fixation pathway; Green bacteria; Oscillochloris trichoides; Ribulose 1,5 bisphosphate carboxylase oxygenase; Tricarboxylic acid cycle

Indexed keywords

BACTERIAL ENZYME; CARBON DIOXIDE; PHOSPHORIBULOKINASE; POTASSIUM CYANIDE; RIBULOSEBISPHOSPHATE CARBOXYLASE;

EID: 0032800755     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/13500872-145-7-1743     Document Type: Article
Times cited : (64)

References (27)
  • 1
    • 0003172832 scopus 로고
    • The chromatographic identification of some biologically important phosphate esters
    • Bandurski, R. S. & Axelrod, B. (1951). The chromatographic identification of some biologically important phosphate esters. J Biol Chem 193, 405-411.
    • (1951) J Biol Chem , vol.193 , pp. 405-411
    • Bandurski, R.S.1    Axelrod, B.2
  • 3
    • 0000033162 scopus 로고
    • Acyladenylates: An enzymatic mechanism of acetate activation
    • Berg, P. (1956). Acyladenylates: an enzymatic mechanism of acetate activation. J Biol Chem 222, 991-1013.
    • (1956) J Biol Chem , vol.222 , pp. 991-1013
    • Berg, P.1
  • 4
    • 0016219695 scopus 로고
    • On the properties of Thiocapsa roseopersicina strain BBS isolated from White Sea estuarium
    • Bogorov, L. V. (1974). On the properties of Thiocapsa roseopersicina strain BBS isolated from White Sea estuarium. Mikrobiologiya 42, 326-330.
    • (1974) Mikrobiologiya , vol.42 , pp. 326-330
    • Bogorov, L.V.1
  • 6
    • 77957003761 scopus 로고
    • Isocitrate dehydrogenase (TPN-specific) from pig heart
    • Cleland, W. W., Thompson, V. W. & Barden, R. E. (1969). Isocitrate dehydrogenase (TPN-specific) from pig heart. Methods Enzymol 13, 30-33.
    • (1969) Methods Enzymol , vol.13 , pp. 30-33
    • Cleland, W.W.1    Thompson, V.W.2    Barden, R.E.3
  • 7
    • 39149130115 scopus 로고
    • Isotope standards for carbon and oxygen and correction factors for mass spectrometric analysis for carbon dioxide
    • Craig, H. (1957). Isotope standards for carbon and oxygen and correction factors for mass spectrometric analysis for carbon dioxide. Geochim Cosmochim Acta 12, 133-149.
    • (1957) Geochim Cosmochim Acta , vol.12 , pp. 133-149
    • Craig, H.1
  • 8
    • 0001904522 scopus 로고
    • Assay methods for key enzymes of glyoxylate cycle
    • Dixon, G. H. & Kornberg, H. L. (1959). Assay methods for key enzymes of glyoxylate cycle. Biochem J 72, 195-200.
    • (1959) Biochem J , vol.72 , pp. 195-200
    • Dixon, G.H.1    Kornberg, H.L.2
  • 9
    • 0013901576 scopus 로고
    • A new ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium
    • Evans, M. C. W., Buchanan, B. B. & Arnon, D. I. (1966). A new ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium. Proc Natl Acad Sci USA 55, 928-934.
    • (1966) Proc Natl Acad Sci USA , vol.55 , pp. 928-934
    • Evans, M.C.W.1    Buchanan, B.B.2    Arnon, D.I.3
  • 10
    • 0016418333 scopus 로고
    • Ribulose-5-phosphate kinase from Chromatium
    • Hart, B. A. & Gibson, J. (1975). Ribulose-5-phosphate kinase from Chromatium. Methods Enzymol 42, 115-119.
    • (1975) Methods Enzymol , vol.42 , pp. 115-119
    • Hart, B.A.1    Gibson, J.2
  • 11
    • 0000008274 scopus 로고
    • 2 and acetate
    • 2 and acetate. Arch Microbiol 151, 252-256.
    • (1989) Arch Microbiol , vol.151 , pp. 252-256
    • Holo, H.1
  • 12
    • 0022517262 scopus 로고
    • 2 fixation of Chloroflexus aurantiacus
    • 2 fixation of Chloroflexus aurantiacus. Arch Microbiol 145, 173-180.
    • (1986) Arch Microbiol , vol.145 , pp. 173-180
    • Holo, H.1    Sirevag, R.2
  • 16
    • 0042404150 scopus 로고
    • Light and dark metabolism in purple sulfur bacteria
    • Edited by V. P. Skulachev. Guildford, NY: IPC Science and Technology Press
    • Kondratieva, E. N., Ivanovsky, R. N. & Krasilnikova, E. N. (1981). Light and dark metabolism in purple sulfur bacteria. In Soviet Science Review, vol. 2, pp. 325-364. Edited by V. P. Skulachev. Guildford, NY: IPC Science and Technology Press.
    • (1981) Soviet Science Review , vol.2 , pp. 325-364
    • Kondratieva, E.N.1    Ivanovsky, R.N.2    Krasilnikova, E.N.3
  • 17
    • 0042683025 scopus 로고
    • On the culture and general physiology of the green sulfur bacteria
    • Larsen, H. (1952). On the culture and general physiology of the green sulfur bacteria. J Bacteriol 64, 187-196.
    • (1952) J Bacteriol , vol.64 , pp. 187-196
    • Larsen, H.1
  • 18
    • 0002097994 scopus 로고
    • Taxonomy and physiology of filamentous anoxygenic phototrophs
    • Edited by R. E. Blankenship, M. T. Madigan & C. E. Bauer. Dordrecht: Kluwer
    • Pierson, B. K. & Castenholz, R. W. (1995). Taxonomy and physiology of filamentous anoxygenic phototrophs. In Anoxygenic Photosynthetic Bacteria, pp. 31-47. Edited by R. E. Blankenship, M. T. Madigan & C. E. Bauer. Dordrecht: Kluwer.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 31-47
    • Pierson, B.K.1    Castenholz, R.W.2
  • 20
    • 77956995420 scopus 로고
    • α-Ketoglutarate dehydrogenase complex from Escherichia coli
    • Reed, L. J. & Mukherjee, B. B. (1969). α-Ketoglutarate dehydrogenase complex from Escherichia coli. Methods Enzymol 13, 55-61.
    • (1969) Methods Enzymol , vol.13 , pp. 55-61
    • Reed, L.J.1    Mukherjee, B.B.2
  • 21
    • 0000657055 scopus 로고
    • Carbon assimilation pathways in sulfate-reducing bacteria. II. Enzymes of a reductive citric acid cycle in the autotrophic Desulfobacter hydrogenophilus
    • Schauder, R., Widdel, F. & Fuchs, G. (1987). Carbon assimilation pathways in sulfate-reducing bacteria. II. Enzymes of a reductive citric acid cycle in the autotrophic Desulfobacter hydrogenophilus. Arch Microbiol 148, 218-225.
    • (1987) Arch Microbiol , vol.148 , pp. 218-225
    • Schauder, R.1    Widdel, F.2    Fuchs, G.3
  • 23
    • 77957010982 scopus 로고
    • Citrate synthase
    • Srere, P. A. (1969). Citrate synthase. Methods Enzymol 13, 3-11.
    • (1969) Methods Enzymol , vol.13 , pp. 3-11
    • Srere, P.A.1
  • 24
    • 0027181983 scopus 로고
    • 2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle
    • 2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle. Eur J Biochem 215, 633-643.
    • (1993) Eur J Biochem , vol.215 , pp. 633-643
    • Strauss, G.1    Fuchs, G.2
  • 25
    • 0042181877 scopus 로고
    • 2 on photosynthetic carbon metabolism by Chlorobium thiosulfatophilum and Chromatium vinosum
    • 2 on photosynthetic carbon metabolism by Chlorobium thiosulfatophilum and Chromatium vinosum. Plant Cell Physiol 18, 753-765.
    • (1977) Plant Cell Physiol , vol.18 , pp. 753-765
    • Takabe, T.1    Akazawa, T.2
  • 26
    • 0014422222 scopus 로고
    • The detection and identification of intermediates of the pentose phosphate cycle and related compounds
    • Wood, T. (1968). The detection and identification of intermediates of the pentose phosphate cycle and related compounds. J Chromatogr 35, 352-361.
    • (1968) J Chromatogr , vol.35 , pp. 352-361
    • Wood, T.1
  • 27
    • 0000770461 scopus 로고
    • L-Malate dehydrogenase from Bacillus subtilis
    • Yoshida, A. (1969). L-Malate dehydrogenase from Bacillus subtilis. Methods Enzymol 13, 141-145.
    • (1969) Methods Enzymol , vol.13 , pp. 141-145
    • Yoshida, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.