메뉴 건너뛰기




Volumn 24, Issue 4, 2000, Pages 321-333

Respiratory protection of nitrogenase in Azotobacter species: Is a widely held hypothesis unequivocally supported by experimental evidence?

Author keywords

Azotobacter; Energy regeneration; N status; Nitrogen fixation; Nitrogenase; Respiration; Respiratory protection

Indexed keywords

NITROGENASE;

EID: 0033818729     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-6445(00)00029-2     Document Type: Review
Times cited : (87)

References (63)
  • 2
    • 0002445136 scopus 로고
    • Nitrogenase: distribution, composition, structure and function
    • (Palacios, R., Mora, J. and Newton, W.E., Eds.), Kluwer Academic, Dordrecht
    • Newton, W.E. (1993) Nitrogenase: distribution, composition, structure and function. In: New Horizons in Nitrogen Fixation (Palacios, R., Mora, J. and Newton, W.E., Eds.), pp. 5-18. Kluwer Academic, Dordrecht.
    • (1993) In: New Horizons in Nitrogen Fixation , pp. 5-18
    • Newton, W.E.1
  • 3
    • 0019262924 scopus 로고
    • Oxygen and hydrogen in biological nitrogen fixation
    • Robson R.L., Postgate J.R. Oxygen and hydrogen in biological nitrogen fixation. Annu. Rev. Microbiol. 34:1980;183-207.
    • (1980) Annu. Rev. Microbiol. , vol.34 , pp. 183-207
    • Robson, R.L.1    Postgate, J.R.2
  • 8
    • 0001362237 scopus 로고
    • Environmental effects on the growth of nitrogen-fixing bacteria
    • Hill S., Drozd J.W., Postgate J.R. Environmental effects on the growth of nitrogen-fixing bacteria. J. Appl. Chem. Biotechnol. 22:1972;541-558.
    • (1972) J. Appl. Chem. Biotechnol. , vol.22 , pp. 541-558
    • Hill, S.1    Drozd, J.W.2    Postgate, J.R.3
  • 9
    • 0020543050 scopus 로고
    • Whole cell respiration and nitrogenase activities in Azotobacter vinelandii growing in oxygen controlled continuous culture
    • Post E., Kleiner D., Oelze J. Whole cell respiration and nitrogenase activities in Azotobacter vinelandii growing in oxygen controlled continuous culture. Arch. Microbiol. 134:1983;68-72.
    • (1983) Arch. Microbiol. , vol.134 , pp. 68-72
    • Post, E.1    Kleiner, D.2    Oelze, J.3
  • 10
    • 0014386264 scopus 로고
    • Effect of oxygen on growth of Azotobacter chroococcum in batch and continuous cultures
    • Dalton H., Postgate J.R. Effect of oxygen on growth of Azotobacter chroococcum in batch and continuous cultures. J. Gen. Microbiol. 54:1969;463-473.
    • (1969) J. Gen. Microbiol. , vol.54 , pp. 463-473
    • Dalton, H.1    Postgate, J.R.2
  • 11
    • 0021094198 scopus 로고
    • On the formation of an oxygen-tolerant three component nitrogenase complex from Azotobacter vinelandii
    • Scherings G., Haaker H., Wassink H., Veeger C. On the formation of an oxygen-tolerant three component nitrogenase complex from Azotobacter vinelandii. Eur. J. Biochem. 135:1983;591-599.
    • (1983) Eur. J. Biochem. , vol.135 , pp. 591-599
    • Scherings, G.1    Haaker, H.2    Wassink, H.3    Veeger, C.4
  • 12
    • 0021942870 scopus 로고
    • 2 sensitivity of Azotobater vineladii nitrogenase and its component proteins
    • 2 sensitivity of Azotobater vineladii nitrogenase and its component proteins. Biochemistry. 24:1985;214-221.
    • (1985) Biochemistry , vol.24 , pp. 214-221
    • Wang, Z.-C.1    Burns, A.2    Watt, G.D.3
  • 13
    • 0027971638 scopus 로고
    • The FeSII protein of Azotobacter vinelandii is not essential for aerobic nitrogen fixation, but confers significant protection to oxygen-mediated inactivation of nitrogenase in vitro and in vivo
    • Moshiri F., Kim J.W., Fu C., Maier R.J. The FeSII protein of Azotobacter vinelandii is not essential for aerobic nitrogen fixation, but confers significant protection to oxygen-mediated inactivation of nitrogenase in vitro and in vivo. Mol. Microbiol. 14:1994;101-114.
    • (1994) Mol. Microbiol. , vol.14 , pp. 101-114
    • Moshiri, F.1    Kim, J.W.2    Fu, C.3    Maier, R.J.4
  • 14
    • 0030663234 scopus 로고    scopus 로고
    • Respiratory protection of nitrogenase activity in Azotobacter vinelandii - roles of the terminal oxidases
    • Poole R.K., Hill S. Respiratory protection of nitrogenase activity in Azotobacter vinelandii - roles of the terminal oxidases. Biosci. Rep. 17:1997;303-317.
    • (1997) Biosci. Rep. , vol.17 , pp. 303-317
    • Poole, R.K.1    Hill, S.2
  • 16
    • 0001883695 scopus 로고
    • Physiology of nitrogen fixation in free-living heterotrophs
    • (Stacey, G., Burris, R.H. and Evans, H.J., Eds.), Chapman and Hall, London
    • Hill, S. (1992) Physiology of nitrogen fixation in free-living heterotrophs. In: Biological Nitrogen Fixation (Stacey, G., Burris, R.H. and Evans, H.J., Eds.), pp. 87-133. Chapman and Hall, London.
    • (1992) In: Biological Nitrogen Fixation , pp. 87-133
    • Hill, S.1
  • 17
    • 0032564865 scopus 로고    scopus 로고
    • Two NADH:ubiquinone reductases of Azotobacter vinelandii and their role in the respiratory protection
    • Bertsova Y.V., Bogachev A.V., Skulachev V.P. Two NADH:ubiquinone reductases of Azotobacter vinelandii and their role in the respiratory protection. Biochim. Biophys. Acta. 1363:1998;125-133.
    • (1998) Biochim. Biophys. Acta , vol.1363 , pp. 125-133
    • Bertsova, Y.V.1    Bogachev, A.V.2    Skulachev, V.P.3
  • 18
    • 0028263624 scopus 로고
    • Determination of the oxygen affinities of terminal oxidases in Azotobacter vinelandii using the deoxygenation of oxyhaemoglobin and oxymyoglobin: Cytochrome bd is a low-affinity oxidase
    • D'mello R., Hill S., Poole R.K. Determination of the oxygen affinities of terminal oxidases in Azotobacter vinelandii using the deoxygenation of oxyhaemoglobin and oxymyoglobin: cytochrome bd is a low-affinity oxidase. Microbiology. 140:1994;1395-1402.
    • (1994) Microbiology , vol.140 , pp. 1395-1402
    • D'Mello, R.1    Hill, S.2    Poole, R.K.3
  • 19
    • 0029123493 scopus 로고
    • 4 gene from Azotobacter vinelandii: Characterization of the mutant strain and a proposed new branch in the respiratory chain
    • 4 gene from Azotobacter vinelandii: characterization of the mutant strain and a proposed new branch in the respiratory chain. Biochim. Biophys. Acta. 1230:1995;119-129.
    • (1995) Biochim. Biophys. Acta , vol.1230 , pp. 119-129
    • Ng, T.C.N.1    Laheri, A.N.2    Maier, R.J.3
  • 20
    • 0031559960 scopus 로고    scopus 로고
    • Generation of protonic potential by the bd-type quinol oxidase of Azotobacter vinelandii
    • Bertsova Y.V., Bogachev A.V., Skulachev V.P. Generation of protonic potential by the bd-type quinol oxidase of Azotobacter vinelandii. FEBS Lett. 414:1997;369-372.
    • (1997) FEBS Lett. , vol.414 , pp. 369-372
    • Bertsova, Y.V.1    Bogachev, A.V.2    Skulachev, V.P.3
  • 21
    • 0030974371 scopus 로고    scopus 로고
    • Formation of pH and potential gradients by the reconstituted Azotobacter vinelandii cytochrome bd respiratory protection oxidase
    • Kolonay J.F., Maier R.J. Formation of pH and potential gradients by the reconstituted Azotobacter vinelandii cytochrome bd respiratory protection oxidase. J. Bacteriol. 179:1997;3813-3817.
    • (1997) J. Bacteriol. , vol.179 , pp. 3813-3817
    • Kolonay, J.F.1    Maier, R.J.2
  • 22
    • 4243672097 scopus 로고
    • Control of respiration and growth yield in ammonium-assimilating cultures of Azotobacter vinelandii
    • Bühler T., Monter U., Sann R., Kuhla J., Dingler C., Oelze J. Control of respiration and growth yield in ammonium-assimilating cultures of Azotobacter vinelandii. Arch. Microbiol. 148:1987;242-246.
    • (1987) Arch. Microbiol. , vol.148 , pp. 242-246
    • Bühler, T.1    Monter, U.2    Sann, R.3    Kuhla, J.4    Dingler, C.5    Oelze, J.6
  • 23
    • 4244021522 scopus 로고
    • Control of dinitrogen fixation in ammonium-assimilating cultures of Azotobacter vinelandii
    • Bühler T., Sann R., Monter U., Dingler C., Kuhla J., Oelze J. Control of dinitrogen fixation in ammonium-assimilating cultures of Azotobacter vinelandii. Arch. Microbiol. 148:1987;247-251.
    • (1987) Arch. Microbiol. , vol.148 , pp. 247-251
    • Bühler, T.1    Sann, R.2    Monter, U.3    Dingler, C.4    Kuhla, J.5    Oelze, J.6
  • 24
    • 0015823869 scopus 로고
    • The role and regulation of energy reserve material in microorganisms
    • Dawes E.A., Senior P.J. The role and regulation of energy reserve material in microorganisms. Adv. Microb. Phys. 10:1973;135-266.
    • (1973) Adv. Microb. Phys. , vol.10 , pp. 135-266
    • Dawes, E.A.1    Senior, P.J.2
  • 25
    • 0032427612 scopus 로고    scopus 로고
    • Determination of C/N ratios required for de-repression of nitrogenase in Rhodobacter capsulatus
    • Dörffler M., Steindorf A., Oelze J. Determination of C/N ratios required for de-repression of nitrogenase in Rhodobacter capsulatus. Z. Naturforsch. 53c:1998;961-967.
    • (1998) Z. Naturforsch. , vol.53 , pp. 961-967
    • Dörffler, M.1    Steindorf, A.2    Oelze, J.3
  • 26
    • 0009464363 scopus 로고
    • s-values on the dissolved oxygen concentration in continuous cultures of Azotobacter vinelandii
    • s-values on the dissolved oxygen concentration in continuous cultures of Azotobacter vinelandii. Arch. Microbiol. 149:1988;509-514.
    • (1988) Arch. Microbiol. , vol.149 , pp. 509-514
    • Kuhla, J.1    Oelze, J.2
  • 27
    • 0028839568 scopus 로고
    • Alternative function of the electron transport system in Azotobacter vinelandii: Removal of excess reductant by the cytochrome d pathway
    • Liu J.-K., Lee E.-T., Lin C.-S., Yao X.-T., Davenport J.W., Wong T.-Y. Alternative function of the electron transport system in Azotobacter vinelandii: removal of excess reductant by the cytochrome d pathway. Appl. Environ. Microbiol. 61:1995;3998-4003.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3998-4003
    • Liu, J.-K.1    Lee, E.-T.2    Lin, C.-S.3    Yao, X.-T.4    Davenport, J.W.5    Wong, T.-Y.6
  • 28
    • 0025155632 scopus 로고
    • Control of diauxic growth of Azotobacter vinelandii on acetate and glucose
    • Tauchert K., Jahn A., Oelze J. Control of diauxic growth of Azotobacter vinelandii on acetate and glucose. J. Bacteriol. 172:1990;6447-6451.
    • (1990) J. Bacteriol. , vol.172 , pp. 6447-6451
    • Tauchert, K.1    Jahn, A.2    Oelze, J.3
  • 29
    • 0028836983 scopus 로고
    • Diauxic growth of Azotobacter vinelandii on galactose and glucose: Regulation of glucose transport by another hexose
    • Wong T.-Y., Pei H., Bancroft K., Childers G.W. Diauxic growth of Azotobacter vinelandii on galactose and glucose: regulation of glucose transport by another hexose. Appl. Environ. Microbiol. 61:1995;430-433.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 430-433
    • Wong, T.-Y.1    Pei, H.2    Bancroft, K.3    Childers, G.W.4
  • 30
    • 0031038893 scopus 로고    scopus 로고
    • Nitrogenase activity and regeneration of the cellular ATP pool in Azotobacter vinelandii adapted to different oxygen concentrations
    • Linkerhägner K., Oelze J. Nitrogenase activity and regeneration of the cellular ATP pool in Azotobacter vinelandii adapted to different oxygen concentrations. J. Bacteriol. 179:1997;1362-1367.
    • (1997) J. Bacteriol. , vol.179 , pp. 1362-1367
    • Linkerhägner, K.1    Oelze, J.2
  • 31
    • 0342533259 scopus 로고
    • On the relationship of intracytoplasmic to cytoplasmic membranes in nitrogen-fixing Azotobacter vinelandii
    • Post E., Vakalopoulou E., Oelze J. On the relationship of intracytoplasmic to cytoplasmic membranes in nitrogen-fixing Azotobacter vinelandii. Arch. Microbiol. 134:1983;265-269.
    • (1983) Arch. Microbiol. , vol.134 , pp. 265-269
    • Post, E.1    Vakalopoulou, E.2    Oelze, J.3
  • 34
    • 0024377166 scopus 로고
    • Respiratory differences associated with culture aeration in Azotobacter vinelandii
    • Peterson J.B. Respiratory differences associated with culture aeration in Azotobacter vinelandii. Can. J. Microbiol. 35:1989;918-924.
    • (1989) Can. J. Microbiol. , vol.35 , pp. 918-924
    • Peterson, J.B.1
  • 35
    • 0030741757 scopus 로고    scopus 로고
    • The cydR gene product, required for cytochrome bd expression in the obligate aerobe Azotobacter vinelandii, is an Fnr-like protein
    • Wu G., Hill S., Kelly M.J.S., Sawers G., Poole R.K. The cydR gene product, required for cytochrome bd expression in the obligate aerobe Azotobacter vinelandii, is an Fnr-like protein. Microbiology. 143:1997;2197-2207.
    • (1997) Microbiology , vol.143 , pp. 2197-2207
    • Wu, G.1    Hill, S.2    Kelly, M.J.S.3    Sawers, G.4    Poole, R.K.5
  • 36
    • 0029664739 scopus 로고    scopus 로고
    • 2 as the regulatory signal for FNR-dependent gene regulation in Escherichia coli
    • 2 as the regulatory signal for FNR-dependent gene regulation in Escherichia coli. J. Bacteriol. 178:1996;4515-4521.
    • (1996) J. Bacteriol. , vol.178 , pp. 4515-4521
    • Becker, S.1    Holighaus, G.2    Gabrielczyk, T.3    Unden, G.4
  • 37
    • 0014841221 scopus 로고
    • Effect of oxygen on acetylene reduction, cytochrome content and respiratory activity of Azotobacter chroococcum
    • Drozd J.W., Postgate J.R. Effect of oxygen on acetylene reduction, cytochrome content and respiratory activity of Azotobacter chroococcum. J. Gen. Microbiol. 63:1970;36-73.
    • (1970) J. Gen. Microbiol. , vol.63 , pp. 36-73
    • Drozd, J.W.1    Postgate, J.R.2
  • 38
    • 0024110026 scopus 로고
    • Dependence of nitrogenase switch-off upon oxygen stress on the nitrogenase activity in Azotobacter vinelandii
    • Kuhla J., Oelze J. Dependence of nitrogenase switch-off upon oxygen stress on the nitrogenase activity in Azotobacter vinelandii. J. Bacteriol. 170:1988;5325-5329.
    • (1988) J. Bacteriol. , vol.170 , pp. 5325-5329
    • Kuhla, J.1    Oelze, J.2
  • 39
    • 0024003543 scopus 로고
    • Levels and activities of nitrogenase proteins in Azotobacter vinelandii grown at different dissolved oxygen concentrations
    • Dingler C., Kuhla J., Wassink H., Oelze J. Levels and activities of nitrogenase proteins in Azotobacter vinelandii grown at different dissolved oxygen concentrations. J. Bacteriol. 170:1988;2148-2152.
    • (1988) J. Bacteriol. , vol.170 , pp. 2148-2152
    • Dingler, C.1    Kuhla, J.2    Wassink, H.3    Oelze, J.4
  • 40
    • 0021907550 scopus 로고
    • Reversible and irreversible inactivation of cellular nitrogenase upon oxygen stress in Azotobacter vinelandii growing in oxygen controlled continuous culture
    • Dingler C., Oelze J. Reversible and irreversible inactivation of cellular nitrogenase upon oxygen stress in Azotobacter vinelandii growing in oxygen controlled continuous culture. Arch. Microbiol. 141:1985;80-84.
    • (1985) Arch. Microbiol. , vol.141 , pp. 80-84
    • Dingler, C.1    Oelze, J.2
  • 41
    • 0029087225 scopus 로고
    • Cellular ATP levels and nitrogenase switchoff upon oxygen stress in chemostat cultures of Azotobacter vinelandii
    • Linkerhägner K., Oelze J. Cellular ATP levels and nitrogenase switchoff upon oxygen stress in chemostat cultures of Azotobacter vinelandii. J. Bacteriol. 177:1995;5289-5293.
    • (1995) J. Bacteriol. , vol.177 , pp. 5289-5293
    • Linkerhägner, K.1    Oelze, J.2
  • 42
    • 0025030204 scopus 로고
    • Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: Mutants deficient in the cytochrome d complex are unable to fix nitrogen in air
    • Kelly M.J.S., Poole R.K., Yates M.G., Kennedy C. Cloning and mutagenesis of genes encoding the cytochrome bd terminal oxidase complex in Azotobacter vinelandii: mutants deficient in the cytochrome d complex are unable to fix nitrogen in air. J. Bacteriol. 172:1990;6010-6019.
    • (1990) J. Bacteriol. , vol.172 , pp. 6010-6019
    • Kelly, M.J.S.1    Poole, R.K.2    Yates, M.G.3    Kennedy, C.4
  • 43
    • 0022021252 scopus 로고
    • The catalytic activity of nitrogenase in intact Azotobacter vinelandii cells
    • Klugkist J., Haaker H., Wassink H., Veeger C. The catalytic activity of nitrogenase in intact Azotobacter vinelandii cells. Eur. J. Biochem. 146:1995;509-515.
    • (1995) Eur. J. Biochem. , vol.146 , pp. 509-515
    • Klugkist, J.1    Haaker, H.2    Wassink, H.3    Veeger, C.4
  • 44
    • 0028178937 scopus 로고
    • Mutagenesis of a gene encoding a cytochrome o-like terminal oxidase of Azotobacter vinelandii: A cytochrome o mutant is aerotolerant during nitrogen fixation
    • Leung D., van der Ost J., Kelly M.J.M., Saraste M., Hill S., Poole R.K. Mutagenesis of a gene encoding a cytochrome o-like terminal oxidase of Azotobacter vinelandii: a cytochrome o mutant is aerotolerant during nitrogen fixation. FEMS Microbiol. Lett. 119:1994;351-358.
    • (1994) FEMS Microbiol. Lett. , vol.119 , pp. 351-358
    • Leung, D.1    Van Der Ost, J.2    Kelly, M.J.M.3    Saraste, M.4    Hill, S.5    Poole, R.K.6
  • 45
    • 0008035381 scopus 로고
    • Para-Hydroxybenzoate supported nitrogen fixation in Azotobacter vinelandii strain OP (13705)
    • Peterson J.B., Peterson L.S. para-Hydroxybenzoate supported nitrogen fixation in Azotobacter vinelandii strain OP (13705). Can. J. Microbiol. 34:1988;1271-1275.
    • (1988) Can. J. Microbiol. , vol.34 , pp. 1271-1275
    • Peterson, J.B.1    Peterson, L.S.2
  • 46
    • 0031596608 scopus 로고    scopus 로고
    • 2 as a substrate in the cytoplasm of bacteria under aerobic and microaerobic conditions
    • 2 as a substrate in the cytoplasm of bacteria under aerobic and microaerobic conditions. J. Bacteriol. 180:1998;2133-2136.
    • (1998) J. Bacteriol. , vol.180 , pp. 2133-2136
    • Arras, T.1    Schirawski, J.2    Unden, G.3
  • 47
    • 0025966479 scopus 로고
    • Isolation and characterization of oxygen sensitive mutants of Azotobacter vinelandii
    • Iwahashi H., Hachiya Y., Someya J. Isolation and characterization of oxygen sensitive mutants of Azotobacter vinelandii. FEMS Microbiol. Lett. 77:1991;73-78.
    • (1991) FEMS Microbiol. Lett. , vol.77 , pp. 73-78
    • Iwahashi, H.1    Hachiya, Y.2    Someya, J.3
  • 48
    • 0024694549 scopus 로고
    • Oxidation of nitrogenase iron protein by dioxygen without inactivation could contribute to high respiration rates of Azotobacter species and facilitate nitrogen fixation in other aerobic environments
    • Thorneley R.N.F., Ashby G.A. Oxidation of nitrogenase iron protein by dioxygen without inactivation could contribute to high respiration rates of Azotobacter species and facilitate nitrogen fixation in other aerobic environments. Biochem. J. 261:1989;181-187.
    • (1989) Biochem. J. , vol.261 , pp. 181-187
    • Thorneley, R.N.F.1    Ashby, G.A.2
  • 49
    • 0021123538 scopus 로고
    • Superoxide dismutase of Azotobacter vinelandii and other aerobic, free-living nitrogen fixing bacteria
    • Moore E.R.B., Norrod E.P., Jurtshuk P.J.R. Superoxide dismutase of Azotobacter vinelandii and other aerobic, free-living nitrogen fixing bacteria. FEMS Microbiol. Lett. 24:1984;261-265.
    • (1984) FEMS Microbiol. Lett. , vol.24 , pp. 261-265
    • Moore, E.R.B.1    Norrod, E.P.2    Jurtshuk, P.J.R.3
  • 50
    • 0022515546 scopus 로고
    • Superoxide dismutase: An essential role in the protection of the nitrogen fixation process?
    • Puppo A., Rigaud J. Superoxide dismutase: an essential role in the protection of the nitrogen fixation process? FEBS Lett. 201:1986;187-189.
    • (1986) FEBS Lett. , vol.201 , pp. 187-189
    • Puppo, A.1    Rigaud, J.2
  • 51
    • 0023263604 scopus 로고
    • Superoxide dismutase and catalase in Azotobacter vinelandii grown in continuous culture at different dissolved oxygen concentrations
    • Dingler C., Oelze J. Superoxide dismutase and catalase in Azotobacter vinelandii grown in continuous culture at different dissolved oxygen concentrations. Arch. Microbiol. 147:1987;291-294.
    • (1987) Arch. Microbiol. , vol.147 , pp. 291-294
    • Dingler, C.1    Oelze, J.2
  • 53
    • 0022403870 scopus 로고
    • The beneficial effect of hydrogenase in Azotobacter chroococcum under nitrogen-fixing, carbon-limiting conditions in continuous and batch cultures
    • Aguilar O.M., Yates M.G., Postgate J.R. The beneficial effect of hydrogenase in Azotobacter chroococcum under nitrogen-fixing, carbon-limiting conditions in continuous and batch cultures. J. Gen. Microbiol. 131:1985;3141-3145.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 3141-3145
    • Aguilar, O.M.1    Yates, M.G.2    Postgate, J.R.3
  • 56
    • 0028889676 scopus 로고
    • Hydrogenase does not confer significant benefits to Azotobacter vinelandii growing diazotrophically under conditions of glucose limitation
    • Linkerhägner K., Oelze J. Hydrogenase does not confer significant benefits to Azotobacter vinelandii growing diazotrophically under conditions of glucose limitation. J. Bacteriol. 177:1995;6018-6020.
    • (1995) J. Bacteriol. , vol.177 , pp. 6018-6020
    • Linkerhägner, K.1    Oelze, J.2
  • 57
    • 0028339650 scopus 로고
    • Nitrogen fixation and hydrogen metabolism in relation to the dissolved oxygen tension in chemostat cultures of the wild-type and a hydrogenase-negative mutant of Azorhizobium caulinodans
    • Boogerd F.C., Ferdinandy-van Vlerken M.M.A., Mawadza C., Pronk A.F., Stouthamer A.H., van Verseveld H.W. Nitrogen fixation and hydrogen metabolism in relation to the dissolved oxygen tension in chemostat cultures of the wild-type and a hydrogenase-negative mutant of Azorhizobium caulinodans. Appl. Environ. Microbiol. 60:1994;1859-1866.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1859-1866
    • Boogerd, F.C.1    Ferdinandy-Van Vlerken, M.M.A.2    Mawadza, C.3    Pronk, A.F.4    Stouthamer, A.H.5    Van Verseveld, H.W.6
  • 59
    • 0023099175 scopus 로고
    • The bioenergetics of electron transport to nitrogenase
    • Haaker H., Klugkist J. The bioenergetics of electron transport to nitrogenase. FEMS Microbiol. Rev. 46:1987;57-71.
    • (1987) FEMS Microbiol. Rev. , vol.46 , pp. 57-71
    • Haaker, H.1    Klugkist, J.2
  • 60
    • 0021863915 scopus 로고
    • Lesions in citrate synthase that affect aerobic nitrogen fixation by Azotobacter chroococcum
    • Ramos J.L., Robson R.L. Lesions in citrate synthase that affect aerobic nitrogen fixation by Azotobacter chroococcum. J. Bacteriol. 162:1985;746-751.
    • (1985) J. Bacteriol. , vol.162 , pp. 746-751
    • Ramos, J.L.1    Robson, R.L.2
  • 61
    • 0031688794 scopus 로고    scopus 로고
    • Mutational inactivation of a gene homologous to Escherichia coli ptsP affects poly-β-hydroxybutyrate accumulation and nitrogen fixation in Azotobacter vinelandii
    • Segura D., Espin G. Mutational inactivation of a gene homologous to Escherichia coli ptsP affects poly-β-hydroxybutyrate accumulation and nitrogen fixation in Azotobacter vinelandii. J. Bacteriol. 180:1998;4790-4798.
    • (1998) J. Bacteriol. , vol.180 , pp. 4790-4798
    • Segura, D.1    Espin, G.2
  • 62
    • 0029976552 scopus 로고    scopus 로고
    • Control of nitrogen fixation by oxygen in the purple nonsulfur bacteria
    • Oelze J., Klein G. Control of nitrogen fixation by oxygen in the purple nonsulfur bacteria. Arch. Microbiol. 165:1996;219-225.
    • (1996) Arch. Microbiol. , vol.165 , pp. 219-225
    • Oelze, J.1    Klein, G.2
  • 63
    • 0031924101 scopus 로고    scopus 로고
    • The oxygen-responsive NIFL-NIFA complex: A novel two-component regulatory system controlling nitrogenase synthesis in γ-Proteobacteria
    • Dixon R. The oxygen-responsive NIFL-NIFA complex: a novel two-component regulatory system controlling nitrogenase synthesis in γ-Proteobacteria. Arch. Microbiol. 169:1998;371-380.
    • (1998) Arch. Microbiol. , vol.169 , pp. 371-380
    • Dixon, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.