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Volumn 49, Issue 2, 1996, Pages 151-160

Intracellular expression of Vitreoscilla hemoglobin modifies microaerobic Escherichia coli metabolism through elevated concentration and specific activity of cytochrome o

Author keywords

cytochrome o; globin function; oxygen starvation; Vitreoscilla hemoglobin

Indexed keywords

CELL CULTURE; COLIFORM BACTERIA; GROWTH KINETICS; HEMOGLOBIN; HEMOGLOBIN OXYGEN SATURATION; METABOLISM;

EID: 0030034536     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19960120)49:2<151::AID-BIT4>3.0.CO;2-P     Document Type: Article
Times cited : (61)

References (54)
  • 3
    • 0001383847 scopus 로고
    • The aerobic respiratory chain of Escherichia coli
    • Anraku, Y., Gennis, R. B. 1987. The aerobic respiratory chain of Escherichia coli. Trends Biochem. Sci. 12: 262-266.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 262-266
    • Anraku, Y.1    Gennis, R.B.2
  • 4
    • 0023887173 scopus 로고
    • Bacterial electron transport chain
    • Anraku, Y. 1988. Bacterial electron transport chain. Ann. Rev. Biochem. 57: 101-132.
    • (1988) Ann. Rev. Biochem. , vol.57 , pp. 101-132
    • Anraku, Y.1
  • 6
    • 0025878646 scopus 로고
    • Kinetics and mechanisms of reduction of Cu(II) and Fe(II) complexes by soybean leghemoglobin
    • Bakan, D. A., Saltman, P., Theriault, Y., Wright, P. E. 1991. Kinetics and mechanisms of reduction of Cu(II) and Fe(II) complexes by soybean leghemoglobin. Biochim. Biophys. Acta 1079: 182-196.
    • (1991) Biochim. Biophys. Acta , vol.1079 , pp. 182-196
    • Bakan, D.A.1    Saltman, P.2    Theriault, Y.3    Wright, P.E.4
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 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
  • 8
    • 0027155827 scopus 로고
    • Energetic efficiency of Escherichia coli: Effects of mutants in components of the aerobic respiratory chain
    • Calhoun, M. W., Oden, K., Gennis, R. B., de Mattos, M. J. T., Neijssel, O. M. 1993. Energetic efficiency of Escherichia coli: Effects of mutants in components of the aerobic respiratory chain. J. Bacteriol. 175: 3020-3025.
    • (1993) J. Bacteriol. , vol.175 , pp. 3020-3025
    • Calhoun, M.W.1    Oden, K.2    Gennis, R.B.3    De Mattos, M.J.T.4    Neijssel, O.M.5
  • 10
    • 0025306403 scopus 로고
    • The use of gene fusions to determine the topology of all of the subunits of the cytochrome o terminal oxidase complex of Escherichia coli
    • Chepuri, V., Gennis, R. B. 1990. The use of gene fusions to determine the topology of all of the subunits of the cytochrome o terminal oxidase complex of Escherichia coli. J. Biol. Chem. 265: 12978-12986.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12978-12986
    • Chepuri, V.1    Gennis, R.B.2
  • 11
    • 0026533385 scopus 로고
    • The bacterial hemoglobin from Vitreoscilla can support the aerobic growth of Escherichia coli lacking terminal oxidases
    • Dikshit, R. P., Dikshit, K. L., Liu, Y., Webster, D. A. 1992. The bacterial hemoglobin from Vitreoscilla can support the aerobic growth of Escherichia coli lacking terminal oxidases. Arch. Biochem. Biophys. 293: 241-245.
    • (1992) Arch. Biochem. Biophys. , vol.293 , pp. 241-245
    • Dikshit, R.P.1    Dikshit, K.L.2    Liu, Y.3    Webster, D.A.4
  • 12
    • 0020505048 scopus 로고
    • Isolation and characterization of an Escherichia coli mutant lacking cytochrome d terminal oxidase
    • Green, G. N., Gennis, R. B. 1983. Isolation and characterization of an Escherichia coli mutant lacking cytochrome d terminal oxidase. J. Bacteriol. 154: 1269-1275.
    • (1983) J. Bacteriol. , vol.154 , pp. 1269-1275
    • Green, G.N.1    Gennis, R.B.2
  • 13
    • 0026442487 scopus 로고
    • Oxygen-regulated gene expression in Escherichia coli
    • Guest, J. R. 1992. Oxygen-regulated gene expression in Escherichia coli. J. Gen. Microbiol. 138: 2253-2263.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2253-2263
    • Guest, J.R.1
  • 14
    • 0026245037 scopus 로고
    • Purification and aqueous 2-phase partitioning properties of recombinant Vitreoscilla hemoglobin
    • Hart, R. A., Bailey, J. E. 1991. Purification and aqueous 2-phase partitioning properties of recombinant Vitreoscilla hemoglobin. Enz. Microb. Technol. 13: 788-795.
    • (1991) Enz. Microb. Technol. , vol.13 , pp. 788-795
    • Hart, R.A.1    Bailey, J.E.2
  • 16
    • 0001395234 scopus 로고
    • Non-inverted versus inverted plots in enzyme kinetics
    • Hofstee, B. H. J. 1959. Non-inverted versus inverted plots in enzyme kinetics. Nature 184: 1296-1298.
    • (1959) Nature , vol.184 , pp. 1296-1298
    • Hofstee, B.H.J.1
  • 17
    • 0021144978 scopus 로고
    • The respiratory chain of Escherichia coli
    • Ingledew, W. J., Poole, R. K. 1984. The respiratory chain of Escherichia coli. Microbiol. Rev. 48: 222-271.
    • (1984) Microbiol. Rev. , vol.48 , pp. 222-271
    • Ingledew, W.J.1    Poole, R.K.2
  • 18
    • 0026470012 scopus 로고
    • Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli
    • Ioannidis, N., Copper, C. E., Poole, R. K. 1992. Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli. Biochem. J. 288: 649-655.
    • (1992) Biochem. J. , vol.288 , pp. 649-655
    • Ioannidis, N.1    Copper, C.E.2    Poole, R.K.3
  • 19
    • 0025832166 scopus 로고
    • Adaptation of Escherichia coli to respiratory conditions: Regulation of gene expression
    • Iuchi, S., Lin, E. C. C. 1991. Adaptation of Escherichia coli to respiratory conditions: Regulation of gene expression. Cell 66: 5-7.
    • (1991) Cell , vol.66 , pp. 5-7
    • Iuchi, S.1    Lin, E.C.C.2
  • 20
    • 0025144171 scopus 로고
    • Requirement for terminal cytochromes in generation of the aerobic signal for the arc regulatory system in Escherichia coli: Study utilizing deletions and lac fusions of cyo and cyd
    • Iuchi, S., Chepuri, V., Fu, H.-A., Gennis, R. B., Lin, E. C. C. 1990. Requirement for terminal cytochromes in generation of the aerobic signal for the arc regulatory system in Escherichia coli: Study utilizing deletions and lac fusions of cyo and cyd. J. Bacteriol. 172: 6020-6025.
    • (1990) J. Bacteriol. , vol.172 , pp. 6020-6025
    • Iuchi, S.1    Chepuri, V.2    Fu, H.-A.3    Gennis, R.B.4    Lin, E.C.C.5
  • 21
    • 0027976409 scopus 로고
    • Intracellular expression of Vitreoscilla hemoglobin alters Escherichia coli energy metabolism under oxygen-limited conditions
    • Kallio, P. T., Kim, D. I., Tsai, P. S., Bailey, J. E. 1994. Intracellular expression of Vitreoscilla hemoglobin alters Escherichia coli energy metabolism under oxygen-limited conditions. Eur. J. Biochem. 219: 201-208.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 201-208
    • Kallio, P.T.1    Kim, D.I.2    Tsai, P.S.3    Bailey, J.E.4
  • 22
    • 0023874286 scopus 로고
    • Heterologous expression of a bacterial haemoglobin improves the growth properties of recombinant Escherichia coli
    • Khosla, C., Bailey, J. E. 1988. Heterologous expression of a bacterial haemoglobin improves the growth properties of recombinant Escherichia coli. Nature 331: 633-635.
    • (1988) Nature , vol.331 , pp. 633-635
    • Khosla, C.1    Bailey, J.E.2
  • 23
    • 0024428050 scopus 로고
    • Characterization of the oxygen-dependent promoter of the Vitreoscilla hemoglobin gene in Escherichia coli
    • Khosla, C., Bailey, J. E. 1989. Characterization of the oxygen-dependent promoter of the Vitreoscilla hemoglobin gene in Escherichia coli. J. Bacteriol. 171: 5995-6004.
    • (1989) J. Bacteriol. , vol.171 , pp. 5995-6004
    • Khosla, C.1    Bailey, J.E.2
  • 24
    • 0024449797 scopus 로고
    • Evidence for partial export of Vitreoscilla hemoglobin into the periplasmic space in Escherichia coli
    • Khosla, C., Bailey, J. E. 1989. Evidence for partial export of Vitreoscilla hemoglobin into the periplasmic space in Escherichia coli. J. Mol. Biol. 210: 79-90.
    • (1989) J. Mol. Biol. , vol.210 , pp. 79-90
    • Khosla, C.1    Bailey, J.E.2
  • 25
    • 0025050682 scopus 로고
    • Expression of intracellular hemoglobin improves protein synthesis in oxygen limited Escherichia coli
    • Khosla, C., Curtis, J. E., DeModena, J., Rinas, U., Bailey, J. E. 1990. Expression of intracellular hemoglobin improves protein synthesis in oxygen limited Escherichia coli. Bio/Technology 8: 849-853.
    • (1990) Bio/Technology , vol.8 , pp. 849-853
    • Khosla, C.1    Curtis, J.E.2    DeModena, J.3    Rinas, U.4    Bailey, J.E.5
  • 26
    • 0025645664 scopus 로고
    • Presence of bacterial hemoglobin gene improves α-amylase production of a recombinant Escherichia coli strain
    • Khosravi, M., Webster, D. A., Stark, B. C. 1990. Presence of bacterial hemoglobin gene improves α-amylase production of a recombinant Escherichia coli strain. Plasmid 24: 190-194.
    • (1990) Plasmid , vol.24 , pp. 190-194
    • Khosravi, M.1    Webster, D.A.2    Stark, B.C.3
  • 27
    • 0021280149 scopus 로고
    • Terminal oxidases of Escherichia coli aerobic respiratory chain, I
    • Kita, K., Konishi, K., Anraku, Y. 1984. Terminal oxidases of Escherichia coli aerobic respiratory chain, I. J. Biol. Chem. 259: 3368-3374.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3368-3374
    • Kita, K.1    Konishi, K.2    Anraku, Y.3
  • 28
    • 0021272743 scopus 로고
    • Terminal oxidases of Escherichia coli aerobic respiratory chain, II
    • Kita, K., Konishi, K., Anraku, Y. 1984b. Terminal oxidases of Escherichia coli aerobic respiratory chain, II. J. Biol. Chem. 259: 3375-3381.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3375-3381
    • Kita, K.1    Konishi, K.2    Anraku, Y.3
  • 30
    • 14744278506 scopus 로고
    • Actinorhodin production by Streptomyces coelicolor and growth of Streptomyces lividans are improved by the expression of a bacterial hemoglobin
    • Magnolo, S. K., Leenutaphong, D. L., DeModena, J. A., Curtis, J. E., Bailey, J. E., Galazzo, J. L., Hughes, D. E. 1991. Actinorhodin production by Streptomyces coelicolor and growth of Streptomyces lividans are improved by the expression of a bacterial hemoglobin. Bio/Technol. 9: 473-476.
    • (1991) Bio/Technol. , vol.9 , pp. 473-476
    • Magnolo, S.K.1    Leenutaphong, D.L.2    DeModena, J.A.3    Curtis, J.E.4    Bailey, J.E.5    Galazzo, J.L.6    Hughes, D.E.7
  • 32
    • 0021099774 scopus 로고
    • The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain
    • Miller, M. J., Gennis, R. B. 1983. The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain. J. Biol. Chem. 258: 9159-9165.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9159-9165
    • Miller, M.J.1    Gennis, R.B.2
  • 33
    • 0022383731 scopus 로고
    • The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli
    • Miller, M. J., Gennis, R. B. 1985. The cytochrome d complex is a coupling site in the aerobic respiratory chain of Escherichia coli. J. Biol. Chem. 260: 14003-14008.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14003-14008
    • Miller, M.J.1    Gennis, R.B.2
  • 34
    • 0014117544 scopus 로고
    • Acid-base titration across the membrane system of rat-liver mitochondria
    • Mitchell, P., Moyle, J. 1967. Acid-base titration across the membrane system of rat-liver mitochondria. Biochem. J. 104: 588-600.
    • (1967) Biochem. J. , vol.104 , pp. 588-600
    • Mitchell, P.1    Moyle, J.2
  • 35
    • 0000438245 scopus 로고
    • Respiration-driven proton translocation in rat liver mitochondria
    • Mitchell, P., Moyle, J. 1967b. Respiration-driven proton translocation in rat liver mitochondria. Biochem. J. 105: 1147-1162.
    • (1967) Biochem. J. , vol.105 , pp. 1147-1162
    • Mitchell, P.1    Moyle, J.2
  • 36
    • 0025805327 scopus 로고
    • In vivo assembly of the cytochrome d terminal oxidase complex of Escherichia coli from genes encoding the two subunits expressed on separate plasmids
    • Newton, G., Gennis, R. B. 1991. In vivo assembly of the cytochrome d terminal oxidase complex of Escherichia coli from genes encoding the two subunits expressed on separate plasmids. Biochim. Biophys. Acta 1089: 8-12.
    • (1991) Biochim. Biophys. Acta , vol.1089 , pp. 8-12
    • Newton, G.1    Gennis, R.B.2
  • 37
    • 0026009165 scopus 로고
    • Isolation and characterization of a new class of cytochrome d terminal oxidase mutants of Escherichia coli
    • Oden, K. L., Gennis, R. B. 1991. Isolation and characterization of a new class of cytochrome d terminal oxidase mutants of Escherichia coli. J. Bacteriol. 173: 6174-6183.
    • (1991) J. Bacteriol. , vol.173 , pp. 6174-6183
    • Oden, K.L.1    Gennis, R.B.2
  • 38
    • 0025643358 scopus 로고
    • Genomic replacement in Escherichia coli K-12 using covalently closed circular plasmid DNA
    • Oden, K. L., Deveaux, L. C., Vibat, C. R. T., Cronan, J. E., Jr., Gennis, R. B. 1990. Genomic replacement in Escherichia coli K-12 using covalently closed circular plasmid DNA. Gene 96: 29-36.
    • (1990) Gene , vol.96 , pp. 29-36
    • Oden, K.L.1    Deveaux, L.C.2    Vibat, C.R.T.3    Cronan Jr., J.E.4    Gennis, R.B.5
  • 39
    • 0023049253 scopus 로고
    • Photodissocation of oxygenated cytochrome o(s) (Vitreoscilla) and kinetic studies of reassociation
    • Orii, Y., Webster, D. A. 1986. Photodissocation of oxygenated cytochrome o(s) (Vitreoscilla) and kinetic studies of reassociation. J. Biol. Chem. 261: 3544-3547.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3544-3547
    • Orii, Y.1    Webster, D.A.2
  • 40
    • 40549137723 scopus 로고
    • Multicomponent-analysis computations based on Kalman filtering
    • Poulisse, H. N. J. 1979. Multicomponent-analysis computations based on Kalman filtering. Anal. Chim. Acta 112: 361-374.
    • (1979) Anal. Chim. Acta , vol.112 , pp. 361-374
    • Poulisse, H.N.J.1
  • 41
    • 0025796578 scopus 로고
    • Properties of the two terminal oxidases of Escherichia coli
    • Puustinen, A., Finel, M., Haltia, T., Gennis, R. B., Wikström, M. 1991. Properties of the two terminal oxidases of Escherichia coli. Biochem. 30: 3936-3942.
    • (1991) Biochem. , vol.30 , pp. 3936-3942
    • Puustinen, A.1    Finel, M.2    Haltia, T.3    Gennis, R.B.4    Wikström, M.5
  • 42
    • 0024962043 scopus 로고
    • Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli
    • Puustinen, A., Finel, M., Virkki, M., Wikström, M. 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    Wikström, M.4
  • 43
    • 0026438826 scopus 로고
    • The low-spin heme site of cytochrome o from Escherichia coli is promiscuous with respect to heme type
    • Puustinen, A., Morgan, J. E., Verkhovsky, M., Thomas, J. W., Gennis, R. B., Wikström, M. 1992. The low-spin heme site of cytochrome o from Escherichia coli is promiscuous with respect to heme type. Biochem 31: 10363-10369.
    • (1992) Biochem , vol.31 , pp. 10363-10369
    • Puustinen, A.1    Morgan, J.E.2    Verkhovsky, M.3    Thomas, J.W.4    Gennis, R.B.5    Wikström, M.6
  • 44
    • 0017858515 scopus 로고
    • Oxygen-limited continuous culture and respiratory energy conservation in Escherichia coli
    • Rice, C. W., Hempfling, W. P. 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
  • 45
    • 0029294091 scopus 로고
    • Fnr, the global transcriptional regulator of Escherichia coli, activates the Vitreoscilla hemoglobin (VHb) promoter and intracellular VHb expression increases cytochrome d promoter activity
    • Tsai, P. S., Kallio, P. T., Bailey, J. E. 1995. Fnr, the global transcriptional regulator of Escherichia coli, activates the Vitreoscilla hemoglobin (VHb) promoter and intracellular VHb expression increases cytochrome d promoter activity. Biotechnol. Prog. 11: 288-293.
    • (1995) Biotechnol. Prog. , vol.11 , pp. 288-293
    • Tsai, P.S.1    Kallio, P.T.2    Bailey, J.E.3
  • 46
    • 0018265593 scopus 로고
    • Electron-accepting properties of cytochrome o purified from Vitreoscilla
    • Tyree, B., Webster, D. A. 1978. Electron-accepting properties of cytochrome o purified from Vitreoscilla. J. Biol. Chem. 253: 6988-6991.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6988-6991
    • Tyree, B.1    Webster, D.A.2
  • 47
    • 0025764867 scopus 로고
    • Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12
    • Vasudevan, S. G., Armarego, W. L. F. Shaw, D. C., Lilley, P. E , Dixon, N. E., Poole, R. K. 1991. Isolation and nucleotide sequence of the hmp gene that encodes a haemoglobin-like protein in Escherichia coli K-12. Mol. Gen. Genet. 226: 49-58.
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 49-58
    • Vasudevan, S.G.1    Armarego, W.L.F.2    Shaw, D.C.3    Lilley, P.E.4    Dixon, N.E.5    Poole, R.K.6
  • 50
    • 0022486777 scopus 로고
    • Primary sequence of a dimeric bacterial hemoglobin from Vitreoscilla
    • Wakabayashi, S., Matsubara, H., Webster, D. A. 1986. Primary sequence of a dimeric bacterial hemoglobin from Vitreoscilla. Nature 322: 481-483.
    • (1986) Nature , vol.322 , pp. 481-483
    • Wakabayashi, S.1    Matsubara, H.2    Webster, D.A.3
  • 51
    • 0016192420 scopus 로고
    • Reduced nicotinamide adenine dinucleotide cytochrome o reductase associated with cytochrome o purified from Vitreoscilla
    • Webster, D. A., Liu, C. Y. 1974. Reduced nicotinamide adenine dinucleotide cytochrome o reductase associated with cytochrome o purified from Vitreoscilla. J. Biol. Chem. 249: 4257-4260.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4257-4260
    • Webster, D.A.1    Liu, C.Y.2
  • 52
    • 0025310053 scopus 로고
    • Mechanisms of cytoplasmic hemoglobin and myoglobin function
    • Wittenberg, J. B., Wittenberg, B. A. 1990. Mechanisms of cytoplasmic hemoglobin and myoglobin function. Ann. Rev. Biophys. Chem. 19: 217-241.
    • (1990) Ann. Rev. Biophys. Chem. , vol.19 , pp. 217-241
    • Wittenberg, J.B.1    Wittenberg, B.A.2
  • 54
    • 8944248653 scopus 로고
    • Formation of hemoglobin and cytochromes by yeast in the presence of antimycin A
    • Ycas, M. 1956. Formation of hemoglobin and cytochromes by yeast in the presence of antimycin A. Exp. Cell. Res. 11: 1-6.
    • (1956) Exp. Cell. Res. , vol.11 , pp. 1-6
    • Ycas, M.1


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