메뉴 건너뛰기




Volumn 1827, Issue 2, 2013, Pages 136-144

Denitrification and aerobic respiration, hybrid electron transport chains and co-evolution

Author keywords

Aerobic denitrification; Denitrification; Nitric oxide dismutation; Respiratory chain

Indexed keywords

CYTOCHROME C; CYTOCHROME C OXIDASE; MULTIENZYME COMPLEX; NITRATE; NITRATE REDUCTASE; NITRIC OXIDE REDUCTASE; NITRITE REDUCTASE; NITROUS OXIDE REDUCTASE; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 84871715352     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2012.10.002     Document Type: Article
Times cited : (347)

References (94)
  • 1
    • 80051472442 scopus 로고    scopus 로고
    • Climate, fertilization, and the nitrogen cycle
    • A. Hanke, and M. Strous Climate, fertilization, and the nitrogen cycle J. Cosmol. 8 2010 1838 1845
    • (2010) J. Cosmol. , vol.8 , pp. 1838-1845
    • Hanke, A.1    Strous, M.2
  • 4
    • 0034152767 scopus 로고    scopus 로고
    • Oxidative stress in bacteria and protein damage by reactive oxygen species
    • E. Cabiscol, J. Tamarit, and J. Ros Oxidative stress in bacteria and protein damage by reactive oxygen species Int. Microbiol. 3 2000 3 8
    • (2000) Int. Microbiol. , vol.3 , pp. 3-8
    • Cabiscol, E.1    Tamarit, J.2    Ros, J.3
  • 5
    • 0030008268 scopus 로고    scopus 로고
    • Fenton chemistry: An introduction
    • P. Wardman, and L.P. Candeias Fenton chemistry: an introduction Radiat. Res. 145 1996 523 531
    • (1996) Radiat. Res. , vol.145 , pp. 523-531
    • Wardman, P.1    Candeias, L.P.2
  • 7
    • 79953131437 scopus 로고    scopus 로고
    • Evolution of respiratory complex i "supernumerary" subunits are present in the α-proteobacterial enzyme
    • C.Y. Yip, M.E. Harbour, K. Jayawardena, I.M. Fearnley, and L.A. Sazanov Evolution of respiratory complex I "supernumerary" subunits are present in the α-proteobacterial enzyme J. Biol. Chem. 286 2011 5023 5033
    • (2011) J. Biol. Chem. , vol.286 , pp. 5023-5033
    • Yip, C.Y.1    Harbour, M.E.2    Jayawardena, K.3    Fearnley, I.M.4    Sazanov, L.A.5
  • 8
    • 0037418550 scopus 로고    scopus 로고
    • The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: The secret unlocked
    • T. Yagi, and A. Matsuno-Yagi The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: the secret unlocked Biochemistry 42 2003 2266 2274
    • (2003) Biochemistry , vol.42 , pp. 2266-2274
    • Yagi, T.1    Matsuno-Yagi, A.2
  • 9
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex i from Thermus thermophilus
    • L.A. Sazanov, and P. Hinchliffe Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus Science 311 2006 1430 1436
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 10
    • 77952979824 scopus 로고    scopus 로고
    • The architecture of respiratory complex i
    • R.G. Efremov, R. Baradaran, and L.A. Sazanov The architecture of respiratory complex I Nature 465 2010 441 445
    • (2010) Nature , vol.465 , pp. 441-445
    • Efremov, R.G.1    Baradaran, R.2    Sazanov, L.A.3
  • 11
    • 80052068980 scopus 로고    scopus 로고
    • Structure of the membrane domain of respiratory complex i
    • R.G. Efremov, and L.A. Sazanov Structure of the membrane domain of respiratory complex I Nature 476 2011 414 420
    • (2011) Nature , vol.476 , pp. 414-420
    • Efremov, R.G.1    Sazanov, L.A.2
  • 12
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH: Quinone oxidoreductase (complex I)
    • U. Brandt Energy converting NADH: quinone oxidoreductase (complex I) Annu. Rev. Biochem. 2006 69 92
    • (2006) Annu. Rev. Biochem. , pp. 69-92
    • Brandt, U.1
  • 13
    • 77954848120 scopus 로고    scopus 로고
    • Functional modules and structural basis of conformational coupling in mitochondrial complex i
    • C. Hunte, V. Zickermann, and U. Brandt Functional modules and structural basis of conformational coupling in mitochondrial complex I Science 329 2010 448 451
    • (2010) Science , vol.329 , pp. 448-451
    • Hunte, C.1    Zickermann, V.2    Brandt, U.3
  • 18
    • 0016690480 scopus 로고
    • 1 complex in the respiratory chain: Protonmotive ubiquinone cycle
    • 1 complex in the respiratory chain: protonmotive ubiquinone cycle FEBS Lett. 56 1975 1 6
    • (1975) FEBS Lett. , vol.56 , pp. 1-6
    • Mitchell, P.1
  • 19
    • 36749045913 scopus 로고    scopus 로고
    • The twin-arginine transport system: Moving folded proteins across membranes
    • F. Sargent The twin-arginine transport system: moving folded proteins across membranes Biochem. Soc. Trans. 35 2007 835 847
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 835-847
    • Sargent, F.1
  • 20
    • 0033573140 scopus 로고    scopus 로고
    • Still a puzzle: Why is haem covalently attached in c-type cytochromes?
    • P.D. Barker, and S.J. Ferguson Still a puzzle: why is haem covalently attached in c-type cytochromes? Structure 7 1999 R281 R290
    • (1999) Structure , vol.7
    • Barker, P.D.1    Ferguson, S.J.2
  • 24
    • 80255137210 scopus 로고    scopus 로고
    • Composition and function of cytochrome c biogenesis system II
    • J. Simon, and L. Hederstedt Composition and function of cytochrome c biogenesis system II FEBS J. 278 2011 4179 4188
    • (2011) FEBS J. , vol.278 , pp. 4179-4188
    • Simon, J.1    Hederstedt, L.2
  • 25
    • 70349309436 scopus 로고    scopus 로고
    • Cytochrome c biogenesis: Mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control
    • R.G. Kranz, C. Richard-Fogal, J.S. Taylor, and E.R. Frawley Cytochrome c biogenesis: mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control Microbiol. Mol. Biol. Rev. 73 2009 510 528
    • (2009) Microbiol. Mol. Biol. Rev. , vol.73 , pp. 510-528
    • Kranz, R.G.1    Richard-Fogal, C.2    Taylor, J.S.3    Frawley, E.R.4
  • 27
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • S. Iwata, C. Ostermeier, B. Ludwig, and H. Michel Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans Nature 376 1995 660 669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 28
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • M. Svensson-Ek, J. Abramson, G. Larsson, S. Tornroth, P. Brzezinski, and S. Iwata The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides J. Mol. Biol. 321 2002 329 339
    • (2002) J. Mol. Biol. , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Tornroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 29
    • 84857913190 scopus 로고    scopus 로고
    • Cytochrome bd oxidase and nitric oxide: From reaction mechanisms to bacterial physiology
    • A. Giuffre, V.B. Borisov, D. Mastronicola, P. Sarti, and E. Forte Cytochrome bd oxidase and nitric oxide: from reaction mechanisms to bacterial physiology FEBS Lett. 586 2012 622 629
    • (2012) FEBS Lett. , vol.586 , pp. 622-629
    • Giuffre, A.1    Borisov, V.B.2    Mastronicola, D.3    Sarti, P.4    Forte, E.5
  • 33
    • 0034015380 scopus 로고    scopus 로고
    • Bacterial respiration: A flexible process for a changing environment
    • D.J. Richardson Bacterial respiration: a flexible process for a changing environment Microbiology-UK 146 2000 551 571
    • (2000) Microbiology-UK , vol.146 , pp. 551-571
    • Richardson, D.J.1
  • 34
    • 56449092797 scopus 로고    scopus 로고
    • The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems
    • J. Simon, R.J.M. van Spanning, and D.J. Richardson The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems BBA-Bioenergetics 1777 2008 1480 1490
    • (2008) BBA-Bioenergetics , vol.1777 , pp. 1480-1490
    • Simon, J.1    Van Spanning, R.J.M.2    Richardson, D.J.3
  • 35
    • 79955478107 scopus 로고    scopus 로고
    • The crystal structure of cupriavidus necator nitrate reductase in oxidized and partially reduced states
    • C. Coelho, P.J. Gonzalez, J.J.G. Moura, I. Moura, J. Trincao, and M.J. Romao The crystal structure of cupriavidus necator nitrate reductase in oxidized and partially reduced states J. Mol. Biol. 408 2011 932 948
    • (2011) J. Mol. Biol. , vol.408 , pp. 932-948
    • Coelho, C.1    Gonzalez, P.J.2    Moura, J.J.G.3    Moura, I.4    Trincao, J.5    Romao, M.J.6
  • 38
    • 0036182372 scopus 로고    scopus 로고
    • Periplasmic nitrate reductase (NapABC enzyme) supports anaerobic respiration by Escherichia coli K-12
    • V. Stewart, Y.R. Lu, and A.J. Darwin Periplasmic nitrate reductase (NapABC enzyme) supports anaerobic respiration by Escherichia coli K-12 J. Bacteriol. 184 2002 1314 1323
    • (2002) J. Bacteriol. , vol.184 , pp. 1314-1323
    • Stewart, V.1    Lu, Y.R.2    Darwin, A.J.3
  • 39
    • 0025283445 scopus 로고
    • In vivo redox poising of the cyclic electron transport system of Rhodobacter capsulatus and the effects of the auxiliary oxidants, nitrate, nitrous oxide and trimethylamine N-oxide, as revealed by multiple short flash excitation
    • M.R. Jones, D.J. Richardson, A.G. McEwan, S.J. Ferguson, and J.B. Jackson In vivo redox poising of the cyclic electron transport system of Rhodobacter capsulatus and the effects of the auxiliary oxidants, nitrate, nitrous oxide and trimethylamine N-oxide, as revealed by multiple short flash excitation BBA-Bioenergetics 1017 1990 209 216
    • (1990) BBA-Bioenergetics , vol.1017 , pp. 209-216
    • Jones, M.R.1    Richardson, D.J.2    McEwan, A.G.3    Ferguson, S.J.4    Jackson, J.B.5
  • 40
    • 43049177140 scopus 로고    scopus 로고
    • The denitrifying prokaryotes
    • M. Dworkin, S. Falkow, E. Rosenberg, K.H. Schleifer, E. Stackebrandt, Springer New York
    • J.P. Shapleigh The denitrifying prokaryotes M. Dworkin, S. Falkow, E. Rosenberg, K.H. Schleifer, E. Stackebrandt, The prokaryotes 2006 Springer New York 769 792
    • (2006) The Prokaryotes , pp. 769-792
    • Shapleigh, J.P.1
  • 41
    • 0026353602 scopus 로고
    • The 2.3 angstrom X-ray structure of nitrite reductase from achromobacter-cycloclastes
    • J.W. Godden, S. Turley, D.C. Teller, E.T. Adman, M.Y. Liu, W.J. Payne, and J. Legall The 2.3 angstrom X-ray structure of nitrite reductase from achromobacter-cycloclastes Science 253 1991 438 442
    • (1991) Science , vol.253 , pp. 438-442
    • Godden, J.W.1    Turley, S.2    Teller, D.C.3    Adman, E.T.4    Liu, M.Y.5    Payne, W.J.6    Legall, J.7
  • 42
    • 0027340210 scopus 로고
    • 1-type nitrite reductase from, and the absence of a copper-type nitrite reductase from, the aerobic denitrifier Thiosphaera pantotropha; The role of pseudoazurin as an electron donor
    • 1-type nitrite reductase from, and the absence of a copper-type nitrite reductase from, the aerobic denitrifier Thiosphaera pantotropha; the role of pseudoazurin as an electron donor Eur. J. Biochem. 212 1993 377 385
    • (1993) Eur. J. Biochem. , vol.212 , pp. 377-385
    • Moir, J.W.B.1    Baratta, D.2    Richardson, D.J.3    Ferguson, S.J.4
  • 46
    • 10444275550 scopus 로고    scopus 로고
    • Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme-copper oxidase type
    • W.G. Zumft Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme-copper oxidase type J. Inorg. Biochem. 99 2005 194 215
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 194-215
    • Zumft, W.G.1
  • 48
    • 84857911507 scopus 로고    scopus 로고
    • Molecular structure and function of bacterial nitric oxide reductase
    • T. Hino, S. Nagano, H. Sugimoto, T. Tosha, and Y. Shiro Molecular structure and function of bacterial nitric oxide reductase BBA-Bioenergetics 1817 2012 680 687
    • (2012) BBA-Bioenergetics , vol.1817 , pp. 680-687
    • Hino, T.1    Nagano, S.2    Sugimoto, H.3    Tosha, T.4    Shiro, Y.5
  • 51
    • 0028811652 scopus 로고
    • Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions
    • B.C. Berks, S.J. Ferguson, J.W.B. Moir, and D.J. Richardson Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions BBA-Bioenergetics 1232 1995 97 173
    • (1995) BBA-Bioenergetics , vol.1232 , pp. 97-173
    • Berks, B.C.1    Ferguson, S.J.2    Moir, J.W.B.3    Richardson, D.J.4
  • 52
  • 53
    • 0029865750 scopus 로고    scopus 로고
    • Identification and analysis of the dissimilatory nitrous oxide reduction genes, nosRZDFY, of Rhizobium meliloti
    • P. Holloway, W. McCormick, R.J. Watson, and Y.K. Chan Identification and analysis of the dissimilatory nitrous oxide reduction genes, nosRZDFY, of Rhizobium meliloti J. Bacteriol. 178 1996 1505 1514
    • (1996) J. Bacteriol. , vol.178 , pp. 1505-1514
    • Holloway, P.1    McCormick, W.2    Watson, R.J.3    Chan, Y.K.4
  • 54
    • 0037337265 scopus 로고    scopus 로고
    • Operon structure and regulation of the Nos gene region of Pseudomonas stutzeri, encoding an ABC-type ATPase for maturation of nitrous oxide reductase
    • U. Honisch, and W.G. Zumft Operon structure and regulation of the Nos gene region of Pseudomonas stutzeri, encoding an ABC-type ATPase for maturation of nitrous oxide reductase J. Bacteriol. 185 2003 1895 1902
    • (2003) J. Bacteriol. , vol.185 , pp. 1895-1902
    • Honisch, U.1    Zumft, W.G.2
  • 55
    • 64449084988 scopus 로고    scopus 로고
    • Exploring the terminal region of the proton pathway in the bacterial nitric oxide reductase
    • U. Flock, P. Lachmann, J. Reimann, N.J. Watmough, and P. Adelroth Exploring the terminal region of the proton pathway in the bacterial nitric oxide reductase J. Inorg. Biochem. 103 2009 845 850
    • (2009) J. Inorg. Biochem. , vol.103 , pp. 845-850
    • Flock, U.1    Lachmann, P.2    Reimann, J.3    Watmough, N.J.4    Adelroth, P.5
  • 56
    • 0036717906 scopus 로고    scopus 로고
    • Hierarchy of carbon source selection in Paracoccus pantotrophus: Strict correlation between reduction state of the carbon substrate and aerobic expression of the nap operon
    • M.J.K. Ellington, K.K. Bhakoo, G. Sawers, D.J. Richardson, and S.J. Ferguson Hierarchy of carbon source selection in Paracoccus pantotrophus: strict correlation between reduction state of the carbon substrate and aerobic expression of the nap operon J. Bacteriol. 184 2002 4767 4774
    • (2002) J. Bacteriol. , vol.184 , pp. 4767-4774
    • Ellington, M.J.K.1    Bhakoo, K.K.2    Sawers, G.3    Richardson, D.J.4    Ferguson, S.J.5
  • 57
    • 0038480728 scopus 로고    scopus 로고
    • Characterization of the expression and activity of the periplasmic nitrate reductase of Paracoccus pantotrophus in chemostat cultures
    • M.J.K. Ellington, G. Sawers, H.J. Sears, S. Spiro, D.J. Richardson, and S.J. Ferguson Characterization of the expression and activity of the periplasmic nitrate reductase of Paracoccus pantotrophus in chemostat cultures Microbiology 149 2003 1533 1540
    • (2003) Microbiology , vol.149 , pp. 1533-1540
    • Ellington, M.J.K.1    Sawers, G.2    Sears, H.J.3    Spiro, S.4    Richardson, D.J.5    Ferguson, S.J.6
  • 58
    • 0035105613 scopus 로고    scopus 로고
    • Nitrate and nitrite transport in bacteria
    • J.W.B. Moir, and N.J. Wood Nitrate and nitrite transport in bacteria Cell. Mol. Life Sci. 58 2001 215 224
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 215-224
    • Moir, J.W.B.1    Wood, N.J.2
  • 59
  • 60
    • 0345863540 scopus 로고    scopus 로고
    • Metabolism of inorganic N compounds by ammonia-oxidizing bacteria
    • D.J. Arp, and L.Y. Stein Metabolism of inorganic N compounds by ammonia-oxidizing bacteria Crit. Rev. Biochem. Mol. Biol. 38 2003 471 495
    • (2003) Crit. Rev. Biochem. Mol. Biol. , vol.38 , pp. 471-495
    • Arp, D.J.1    Stein, L.Y.2
  • 61
    • 0018654333 scopus 로고
    • Hydroxylamine oxidoreductase of Nitrosomonas production of nitric-oxide from hydroxylamine
    • A.B. Hooper, and K.R. Terry Hydroxylamine oxidoreductase of Nitrosomonas production of nitric-oxide from hydroxylamine BBA-Enzymology 571 1979 12 20
    • (1979) BBA-Enzymology , vol.571 , pp. 12-20
    • Hooper, A.B.1    Terry, K.R.2
  • 62
    • 0034129355 scopus 로고    scopus 로고
    • Aerobic denitrifiers isolated from diverse natural and managed ecosystems
    • D. Patureau, E. Zumstein, J.P. Delgenes, and R. Moletta Aerobic denitrifiers isolated from diverse natural and managed ecosystems Microb. Ecol. 39 2000 145 152
    • (2000) Microb. Ecol. , vol.39 , pp. 145-152
    • Patureau, D.1    Zumstein, E.2    Delgenes, J.P.3    Moletta, R.4
  • 63
    • 3743072781 scopus 로고
    • Persistence of bacterial denitrification capacity under aerobic conditions - The rule rather than the exception
    • D. Lloyd, L. Boddy, and K.J.P. Davies Persistence of bacterial denitrification capacity under aerobic conditions - the rule rather than the exception FEMS Microbiol. Ecol. 45 1987 185 190
    • (1987) FEMS Microbiol. Ecol. , vol.45 , pp. 185-190
    • Lloyd, D.1    Boddy, L.2    Davies, K.J.P.3
  • 64
    • 0028323351 scopus 로고
    • Denitrification under various aeration conditions in Comamonas sp., strain SGLY2
    • D. Patureau, J. Davison, N. Bernet, and R. Moletta Denitrification under various aeration conditions in Comamonas sp., strain SGLY2 FEMS Microbiol. Ecol. 14 1994 71 78
    • (1994) FEMS Microbiol. Ecol. , vol.14 , pp. 71-78
    • Patureau, D.1    Davison, J.2    Bernet, N.3    Moletta, R.4
  • 65
    • 0029669924 scopus 로고    scopus 로고
    • Effect of oxygen on denitrification in continuous chemostat culture with Comamonas sp SGLY2
    • D. Patureau, N. Bernet, and R. Moletta Effect of oxygen on denitrification in continuous chemostat culture with Comamonas sp SGLY2 J. Ind. Microbiol. Biotechnol. 16 1996 124 128
    • (1996) J. Ind. Microbiol. Biotechnol. , vol.16 , pp. 124-128
    • Patureau, D.1    Bernet, N.2    Moletta, R.3
  • 66
    • 0031852636 scopus 로고    scopus 로고
    • Microvirgula aerodenitrificans gen. nov., sp. nov., a new gram-negative bacterium exhibiting co-respiration of oxygen and nitrogen oxides up to oxygen-saturated conditions
    • D. Patureau, J.J. Godon, P. Dabert, T. Bouchez, N. Bernet, J.P. Delgenes, and R. Moletta Microvirgula aerodenitrificans gen. nov., sp. nov., a new gram-negative bacterium exhibiting co-respiration of oxygen and nitrogen oxides up to oxygen-saturated conditions Int. J. Syst. Bacteriol. 48 1998 775 782
    • (1998) Int. J. Syst. Bacteriol. , vol.48 , pp. 775-782
    • Patureau, D.1    Godon, J.J.2    Dabert, P.3    Bouchez, T.4    Bernet, N.5    Delgenes, J.P.6    Moletta, R.7
  • 68
    • 0029622346 scopus 로고
    • Nitrification and denitrification by Thiosphaera pantotropha in aerobic chemostat cultures
    • P.A.M. Arts, L.A. Robertson, and J.G. Kuenen Nitrification and denitrification by Thiosphaera pantotropha in aerobic chemostat cultures FEMS Microbiol. Ecol. 18 1995 305 315
    • (1995) FEMS Microbiol. Ecol. , vol.18 , pp. 305-315
    • Arts, P.A.M.1    Robertson, L.A.2    Kuenen, J.G.3
  • 69
    • 0031455507 scopus 로고    scopus 로고
    • Aerobic denitrifiers isolated from an alternating activated sludge system
    • L. Frette, B. Gejlsbjerg, and P. Westermann Aerobic denitrifiers isolated from an alternating activated sludge system FEMS Microbiol. Ecol. 24 1997 363 370
    • (1997) FEMS Microbiol. Ecol. , vol.24 , pp. 363-370
    • Frette, L.1    Gejlsbjerg, B.2    Westermann, P.3
  • 70
    • 0035106652 scopus 로고    scopus 로고
    • Nitrate reduction by Citrobacter diversus under aerobic environment
    • H.K. Huang, and S.K. Tseng Nitrate reduction by Citrobacter diversus under aerobic environment Appl. Microbiol. Biotechnol. 55 2001 90 94
    • (2001) Appl. Microbiol. Biotechnol. , vol.55 , pp. 90-94
    • Huang, H.K.1    Tseng, S.K.2
  • 71
    • 0001328962 scopus 로고
    • Thiosphaera pantotropha gen. nov. sp. nov., a facultatively anaerobic, facultatively autotrophic sulfur bacterium
    • L.A. Robertson, and J.G. Kuenen Thiosphaera pantotropha gen. nov. sp. nov., a facultatively anaerobic, facultatively autotrophic sulfur bacterium J. Gen. Microbiol. 129 1983 2847 2855
    • (1983) J. Gen. Microbiol. , vol.129 , pp. 2847-2855
    • Robertson, L.A.1    Kuenen, J.G.2
  • 72
    • 34250119426 scopus 로고
    • Aerobic denitrification and heterotrophic nitrification by Thiosphaera pantotropha
    • L.A. Robertson, J.G. Kuenen, and R. Kleijntjens Aerobic denitrification and heterotrophic nitrification by Thiosphaera pantotropha Anton. Leeuw. Int. J. G. 51 1985 445-445
    • (1985) Anton. Leeuw. Int. J. G. , vol.51 , pp. 445-445
    • Robertson, L.A.1    Kuenen, J.G.2    Kleijntjens, R.3
  • 73
    • 0000169202 scopus 로고
    • Aerobic denitrification: A controversy revived
    • L.A. Robertson, and J.G. Kuenen Aerobic denitrification: a controversy revived Arch. Microbiol. 139 1984 351 354
    • (1984) Arch. Microbiol. , vol.139 , pp. 351-354
    • Robertson, L.A.1    Kuenen, J.G.2
  • 74
    • 34250118118 scopus 로고
    • Further evidence for aerobic denitrification by Thiosphaera pantotropha
    • L.A. Robertson, and J.G. Kuenen Further evidence for aerobic denitrification by Thiosphaera pantotropha Anton. Leeuw. Int. J. G. 51 1985 561-561
    • (1985) Anton. Leeuw. Int. J. G. , vol.51 , pp. 561-561
    • Robertson, L.A.1    Kuenen, J.G.2
  • 77
    • 34447254553 scopus 로고    scopus 로고
    • Characterization of efficient aerobic denitrifiers isolated from two different sequencing batch reactors by 16S-rRNA analysis
    • P. Wang, X. Li, M. Xiang, and Q. Zhai Characterization of efficient aerobic denitrifiers isolated from two different sequencing batch reactors by 16S-rRNA analysis J. Biosci. Bioeng. 103 2007 563 567
    • (2007) J. Biosci. Bioeng. , vol.103 , pp. 563-567
    • Wang, P.1    Li, X.2    Xiang, M.3    Zhai, Q.4
  • 81
    • 0030832853 scopus 로고    scopus 로고
    • Aerobic denitrification by a newly isolated heterotrophic bacterium strain TL1
    • T. Lukow, and H. Diekmann Aerobic denitrification by a newly isolated heterotrophic bacterium strain TL1 Biotechnol. Lett. 19 1997 1157 1159
    • (1997) Biotechnol. Lett. , vol.19 , pp. 1157-1159
    • Lukow, T.1    Diekmann, H.2
  • 82
    • 0025765210 scopus 로고
    • A direct demonstration of "co-respiration" of oxygen and nitrogen oxides by Pseudomonas nautica: Some spectral and kinetic properties of the respiratory components
    • P. Bonin, and M. Gilewicz A direct demonstration of "co- respiration" of oxygen and nitrogen oxides by Pseudomonas nautica: some spectral and kinetic properties of the respiratory components FEMS Microbiol. Lett. 80 1991 183 188
    • (1991) FEMS Microbiol. Lett. , vol.80 , pp. 183-188
    • Bonin, P.1    Gilewicz, M.2
  • 84
    • 0242405665 scopus 로고    scopus 로고
    • Aerobic denitrification of Pseudomonas aeruginosa monitored by online NAD(P)H fluorescence
    • F. Chen, Q. Xia, and L.K. Ju Aerobic denitrification of Pseudomonas aeruginosa monitored by online NAD(P)H fluorescence Appl. Environ. Microbiol. 69 2003 6715 6722
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 6715-6722
    • Chen, F.1    Xia, Q.2    Ju, L.K.3
  • 86
    • 80052477164 scopus 로고    scopus 로고
    • Heterotrophic nitrification-aerobic denitrification by novel isolated bacteria
    • C. Qian, and N. Jinren Heterotrophic nitrification-aerobic denitrification by novel isolated bacteria J. Ind. Microbiol. Biotechnol. 38 2011 1305 1310
    • (2011) J. Ind. Microbiol. Biotechnol. , vol.38 , pp. 1305-1310
    • Qian, C.1    Jinren, N.2
  • 87
    • 70249096626 scopus 로고    scopus 로고
    • Early earth: Oxygen for heavy-metal fans
    • T.W. Lyons, and C.T. Reinhard Early earth: oxygen for heavy-metal fans Nature 461 2009 179 181
    • (2009) Nature , vol.461 , pp. 179-181
    • Lyons, T.W.1    Reinhard, C.T.2
  • 89
    • 0035811503 scopus 로고    scopus 로고
    • A possible nitrogen crisis for Archaean life due to reduced nitrogen fixation by lightning
    • R. Navarro-Gonzalez, C.P. McKay, and D.N. Mvondo A possible nitrogen crisis for Archaean life due to reduced nitrogen fixation by lightning Nature 412 2001 61 64
    • (2001) Nature , vol.412 , pp. 61-64
    • Navarro-Gonzalez, R.1    McKay, C.P.2    Mvondo, D.N.3
  • 90
    • 4544356069 scopus 로고    scopus 로고
    • The transition to a sulphidic ocean similar to 1.84 billion years ago
    • S.W. Poulton, P.W. Fralick, and D.E. Canfield The transition to a sulphidic ocean similar to 1.84 billion years ago Nature 431 2004 173 177
    • (2004) Nature , vol.431 , pp. 173-177
    • Poulton, S.W.1    Fralick, P.W.2    Canfield, D.E.3
  • 92
    • 79958824271 scopus 로고    scopus 로고
    • Ferruginous conditions: A dominant feature of the ocean through Earth's history
    • S.W. Poulton, and D.E. Canfield Ferruginous conditions: a dominant feature of the ocean through Earth's history Elements 7 2011 107 112
    • (2011) Elements , vol.7 , pp. 107-112
    • Poulton, S.W.1    Canfield, D.E.2
  • 93
    • 0037119593 scopus 로고    scopus 로고
    • Proterozoic ocean chemistry and evolution: A bioinorganic bridge?
    • A.D. Anbar, and A.H. Knoll Proterozoic ocean chemistry and evolution: a bioinorganic bridge? Science 297 2002 1137 1142
    • (2002) Science , vol.297 , pp. 1137-1142
    • Anbar, A.D.1    Knoll, A.H.2
  • 94
    • 14644444229 scopus 로고    scopus 로고
    • Membrane-bound denitrification in the Gram-positive bacterium Bacillus azotoformans
    • S. de Vries Suharti Membrane-bound denitrification in the Gram-positive bacterium Bacillus azotoformans Biochem. Soc. Trans. 33 2005 130 133
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 130-133
    • De Vries Suharti, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.