메뉴 건너뛰기




Volumn 170, Issue 4, 1998, Pages 297-303

Membrane-associated redox activities in Thermotoga neapolitana

Author keywords

Ferredoxin; Hydrogenase; Hyperthermophile; Membrane; Oxidoreductase

Indexed keywords

FERREDOXIN; HYDROGENASE; NITRITE; OXIDOREDUCTASE;

EID: 0031684658     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002030050645     Document Type: Article
Times cited : (10)

References (33)
  • 1
    • 0025000128 scopus 로고
    • The structure and mechanism of iron-hydrogenases
    • Adams MWW (1990) The structure and mechanism of iron-hydrogenases. Biochim Biophys Acta 1020:115-145
    • (1990) Biochim Biophys Acta , vol.1020 , pp. 115-145
    • Adams, M.W.W.1
  • 2
    • 0022541209 scopus 로고
    • A new sulfur-reducing, extremely thermophilic eubacterium from a submarine thermal vent
    • Belkin S, Wirsen CO, Jannasch HW (1986) A new sulfur-reducing, extremely thermophilic eubacterium from a submarine thermal vent. Appl Environ Microbiol 51:1180-1185
    • (1986) Appl Environ Microbiol , vol.51 , pp. 1180-1185
    • Belkin, S.1    Wirsen, C.O.2    Jannasch, H.W.3
  • 3
    • 0028085225 scopus 로고
    • Characterization of an ancestral type of pyruvate ferredoxin oxidoreductase from the hyperthermophilic bacterium. Thermotoga maritima
    • Blarney JM, Adams MW (1994) Characterization of an ancestral type of pyruvate ferredoxin oxidoreductase from the hyperthermophilic bacterium. Thermotoga maritima. Biochemistry 33: 1000-1007
    • (1994) Biochemistry , vol.33 , pp. 1000-1007
    • Blarney, J.M.1    Adams, M.W.2
  • 4
    • 0019484156 scopus 로고
    • A new, fast, and sensitive assay for NADH-ferredoxin oxidoreductase detection in clostridia
    • Blusson H, Petidemange H, Gay R (1981) A new, fast, and sensitive assay for NADH-ferredoxin oxidoreductase detection in clostridia. Anal Biochem 110:176-181
    • (1981) Anal Biochem , vol.110 , pp. 176-181
    • Blusson, H.1    Petidemange, H.2    Gay, R.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0028046167 scopus 로고
    • Vesicles prepared from Streptococcus mutans demonstrate the presence of a second glucose transport system
    • Buckley ND, Hamilton IR (1994) Vesicles prepared from Streptococcus mutans demonstrate the presence of a second glucose transport system. Microbiology 140:2639-2648
    • (1994) Microbiology , vol.140 , pp. 2639-2648
    • Buckley, N.D.1    Hamilton, I.R.2
  • 8
    • 0024724771 scopus 로고
    • + reductase from the methane oxidizer Methylosinus trichosporium OB3b
    • + reductase from the methane oxidizer Methylosinus trichosporium OB3b. J Bacteriol 171:5012-5016
    • (1989) J Bacteriol , vol.171 , pp. 5012-5016
    • Chen, Y.-P.1    Yoch, D.C.2
  • 10
    • 0028200560 scopus 로고
    • Characterization and regulation of sulfur reductase activity in Thermotoga neapolitana
    • Childers SE, Noll KM (1994) Characterization and regulation of sulfur reductase activity in Thermotoga neapolitana. Appl Environ Microbiol 60:2622-2626
    • (1994) Appl Environ Microbiol , vol.60 , pp. 2622-2626
    • Childers, S.E.1    Noll, K.M.2
  • 12
    • 7344234434 scopus 로고
    • Resolution of three oxidoreductase activities in extracts of the hyperthermophilic bacterium Thermotoga neapolitana
    • Washington, DC
    • Childers SE, Noll KM (1995b) Resolution of three oxidoreductase activities in extracts of the hyperthermophilic bacterium Thermotoga neapolitana (abstract). Annual Meeting American Society for Microbiology. Washington, DC
    • (1995) Annual Meeting American Society for Microbiology
    • Childers, S.E.1    Noll, K.M.2
  • 13
    • 0026484958 scopus 로고
    • Improved methods for cultivation of the extremely thermophilic bacterium Thermotoga neapolitana
    • Childers SE, Vargas M, Noll KM (1992) Improved methods for cultivation of the extremely thermophilic bacterium Thermotoga neapolitana. Appl Environ Microbiol 58:3949-3953
    • (1992) Appl Environ Microbiol , vol.58 , pp. 3949-3953
    • Childers, S.E.1    Vargas, M.2    Noll, K.M.3
  • 14
    • 0022468343 scopus 로고
    • Intracellular localization of the hydrogenase in Desulfotomaculum orientis
    • Cypionka H, Dilling W (1986) Intracellular localization of the hydrogenase in Desulfotomaculum orientis. FEMS Microbiol Lett 36:257-260
    • (1986) FEMS Microbiol Lett , vol.36 , pp. 257-260
    • Cypionka, H.1    Dilling, W.2
  • 15
    • 0028265821 scopus 로고
    • Sequence, assembly and evolution of a primordial ferredoxin from Thermotoga maritima
    • Darimont B, Sterner R (1994) Sequence, assembly and evolution of a primordial ferredoxin from Thermotoga maritima. EMBO J 13:1772-1781
    • (1994) EMBO J , vol.13 , pp. 1772-1781
    • Darimont, B.1    Sterner, R.2
  • 17
    • 0020570950 scopus 로고
    • Structure and function of protontranslocating adenosine triphosphatase (F0F1): Biochemical and molecular biological approaches
    • Futai M, Kanazawa H (1983) Structure and function of protontranslocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches. Microbiol Rev 47:285-312
    • (1983) Microbiol Rev , vol.47 , pp. 285-312
    • Futai, M.1    Kanazawa, H.2
  • 18
    • 0029803262 scopus 로고    scopus 로고
    • Sodium ion-dependent hydrogen production in Acidaminococcus fermentans
    • Hartel U, Buckel W (1996) Sodium ion-dependent hydrogen production in Acidaminococcus fermentans. Arch Microbiol 166: 350-356
    • (1996) Arch Microbiol , vol.166 , pp. 350-356
    • Hartel, U.1    Buckel, W.2
  • 19
    • 0001846919 scopus 로고
    • The order Thermotogales
    • Balows A, Trüper HG, Dworkin M, Harder W, Schleifer KH (eds) Springer, Berlin Heidelberg New York
    • Huber R, Stetter KO (1992) The order Thermotogales. In: Balows A, Trüper HG, Dworkin M, Harder W, Schleifer KH (eds) The prokaryotes. Springer, Berlin Heidelberg New York, pp 3809-3815
    • (1992) The Prokaryotes , pp. 3809-3815
    • Huber, R.1    Stetter, K.O.2
  • 20
    • 0022522022 scopus 로고
    • Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C
    • Huber R et al. (1986) Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C. Arch Microbiol 144:324-333
    • (1986) Arch Microbiol , vol.144 , pp. 324-333
    • Huber, R.1
  • 21
    • 0027120909 scopus 로고
    • Heterotrophic sulfur reduction by Thermotoga sp. strain FjSS3.B1
    • Janssen PH, Morgan HW (1992) Heterotrophic sulfur reduction by Thermotoga sp. strain FjSS3.B1. FEMS Microbiol Lett 96: 213-217
    • (1992) FEMS Microbiol Lett , vol.96 , pp. 213-217
    • Janssen, P.H.1    Morgan, H.W.2
  • 22
    • 0017616853 scopus 로고
    • Sites and specificity of the reaction of bipyridylium compounds with anaerobic respiratory enzymes of Escherichia coli
    • Jones RW, Garland PB (1977) Sites and specificity of the reaction of bipyridylium compounds with anaerobic respiratory enzymes of Escherichia coli. Biochem J 164:199-211
    • (1977) Biochem J , vol.164 , pp. 199-211
    • Jones, R.W.1    Garland, P.B.2
  • 23
    • 0015788525 scopus 로고
    • Function of reduced pyridine nucleotide-ferredoxin oxidoreductases in saccharolytic Clostridia
    • Jungermann K, Thauer RK, Leimenstoll G, Decker K (1973) Function of reduced pyridine nucleotide-ferredoxin oxidoreductases in saccharolytic Clostridia. Biochim Biophys Acta 305:268-280
    • (1973) Biochim Biophys Acta , vol.305 , pp. 268-280
    • Jungermann, K.1    Thauer, R.K.2    Leimenstoll, G.3    Decker, K.4
  • 24
    • 0026431593 scopus 로고
    • The extremely thermophilic eubacterium, Thermotoga maritima, contains a novel iron-hydrogenase whose cellular activity is dependent upon tungsten
    • Juszczak A, Aono S, Adams MW (1991) The extremely thermophilic eubacterium, Thermotoga maritima, contains a novel iron-hydrogenase whose cellular activity is dependent upon tungsten. J Biol Chem 266:13834-41
    • (1991) J Biol Chem , vol.266 , pp. 13834-13841
    • Juszczak, A.1    Aono, S.2    Adams, M.W.3
  • 25
    • 0027163125 scopus 로고
    • Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: Evidence for a sulfur-reducing hydrogenase ancestor
    • Ma K, Schicho RN, Kelly RM, Adams MWW (1993) Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor. Proc Natl Acad Sci USA 90:5341-5344
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5341-5344
    • Ma, K.1    Schicho, R.N.2    Kelly, R.M.3    Adams, M.W.W.4
  • 26
    • 0027989417 scopus 로고
    • Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: A key role for NADPH
    • Ma K, Zhou ZH, Adams MWW (1994) Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: a key role for NADPH. FEMS Mtcrobiol Lett 122:245-250
    • (1994) FEMS Mtcrobiol Lett , vol.122 , pp. 245-250
    • Ma, K.1    Zh, Z.2    Adams, M.W.W.3
  • 27
    • 0029688839 scopus 로고    scopus 로고
    • Respiratory metabolism in hyperthermophilic organisms: Hydrogenases, sulfur reductases, and electron transport factors that function at temperatures exceeding 100 degrees C
    • Maier RJ (1996) Respiratory metabolism in hyperthermophilic organisms: hydrogenases, sulfur reductases, and electron transport factors that function at temperatures exceeding 100 degrees C. Adv Protein Chem 48:35-99
    • (1996) Adv Protein Chem , vol.48 , pp. 35-99
    • Maier, R.J.1
  • 28
    • 0017295687 scopus 로고
    • Regulation of the NADH and NADPH-ferrodoxin oxidoreductases in clostridia of the butyric group
    • Petitdemange H, Cherrier C, Raval CT, Gay G (1976) Regulation of the NADH and NADPH-ferrodoxin oxidoreductases in clostridia of the butyric group. Biochim Biophys Acta 421:334-347
    • (1976) Biochim Biophys Acta , vol.421 , pp. 334-347
    • Petitdemange, H.1    Cherrier, C.2    Raval, C.T.3    Gay, G.4
  • 29
  • 30
    • 0027462194 scopus 로고
    • Bioenergelics of sulfur reduction in the hyperthermophilic archaeon Pyrococcus furiosus
    • Schicho RN, Ma K, Adams MWW, Kelly RM (1993) Bioenergelics of sulfur reduction in the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol 175:1823-1830
    • (1993) J Bacteriol , vol.175 , pp. 1823-1830
    • Schicho, R.N.1    Ma, K.2    Adams, M.W.W.3    Kelly, R.M.4
  • 31
    • 0028148806 scopus 로고
    • Energetics of syntropic fatty acid oxidation
    • Schink B, Friedrich M (1994) Energetics of syntropic fatty acid oxidation. FEMS Microbiol Rev 15:85-94
    • (1994) FEMS Microbiol Rev , vol.15 , pp. 85-94
    • Schink, B.1    Friedrich, M.2
  • 32
    • 0026762970 scopus 로고
    • + oxidoreductase in cyanobacteria: Cloning and sequence of the petH gene of Synechococcus sp. PCC 7002 and studies on the gene product
    • + oxidoreductase in cyanobacteria: cloning and sequence of the petH gene of Synechococcus sp. PCC 7002 and studies on the gene product. Biochemistry 31:3092-3102
    • (1992) Biochemistry , vol.31 , pp. 3092-3102
    • Schluchter, W.M.1    Bryant, D.A.2
  • 33
    • 0028356024 scopus 로고
    • 2 in the anaerobic hyperthermophilic eubacterium Thermotoga maritima: Involvement of the Embden-Meyerhof pathway
    • 2 in the anaerobic hyperthermophilic eubacterium Thermotoga maritima: involvement of the Embden-Meyerhof pathway. Arch Microbiol 161:460-470
    • (1994) Arch Microbiol , vol.161 , pp. 460-470
    • Schröder, C.1    Selig, M.2    Schönheit, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.