메뉴 건너뛰기




Volumn 586, Issue 11, 2012, Pages 1658-1663

Anammox organism KSU-1 expresses a NirK-type copper-containing nitrite reductase instead of a NirS-type with cytochrome cd 1

Author keywords

Anammox; Copper containing nitrite reductase; Denitrification; Dissimilatory nitrite reductase

Indexed keywords

CYTOCHROME P450; NIRK TYPE COPPER CONTAINING NITRITE REDUCTASE; NIRS TYPE COPPER CONTAINING NITRITE REDUCTASE; NITRIC OXIDE; NITRITE; NITRITE REDUCTASE; NITROGEN; UNCLASSIFIED DRUG;

EID: 84861623768     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.04.041     Document Type: Article
Times cited : (126)

References (31)
  • 1
    • 25144475996 scopus 로고    scopus 로고
    • Marine microorganisms and global nutrient cycles
    • K.R. Arrigo Marine microorganisms and global nutrient cycles Nature 437 2005 349 355
    • (2005) Nature , vol.437 , pp. 349-355
    • Arrigo, K.R.1
  • 2
    • 33847752606 scopus 로고    scopus 로고
    • New developments in the marine nitrogen cycle
    • J.A. Brandes, A.H. Devol, and C. Deutsch New developments in the marine nitrogen cycle Chem. Rev. 107 2007 577 589
    • (2007) Chem. Rev. , vol.107 , pp. 577-589
    • Brandes, J.A.1    Devol, A.H.2    Deutsch, C.3
  • 3
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • W.G. Zumft Cell biology and molecular basis of denitrification Microbiol. Mol. Biol. Rev. 61 1997 533 616
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 533-616
    • Zumft, W.G.1
  • 4
    • 49749112308 scopus 로고    scopus 로고
    • Phylogenetic analysis of nitrite, nitric oxide, and nitrous oxide respiratory enzymes reveal a complex evolutionary history for denitrification
    • C.M. Jones, B. Stres, M. Rosenquist, and S. Hallin Phylogenetic analysis of nitrite, nitric oxide, and nitrous oxide respiratory enzymes reveal a complex evolutionary history for denitrification Mol. Biol. Evol. 25 2008 1955 1966
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 1955-1966
    • Jones, C.M.1    Stres, B.2    Rosenquist, M.3    Hallin, S.4
  • 5
    • 0028940437 scopus 로고
    • Anaerobic ammonium oxidation discovered in a denitrifying fluidized-bed reactor
    • A. Mulder, A.A. Vandergraaf, L.A. Robertson, and J.G. Kuenen Anaerobic ammonium oxidation discovered in a denitrifying fluidized-bed reactor FEMS Microbiol. Ecol. 16 1995 177 183
    • (1995) FEMS Microbiol. Ecol. , vol.16 , pp. 177-183
    • Mulder, A.1    Vandergraaf, A.A.2    Robertson, L.A.3    Kuenen, J.G.4
  • 8
    • 0034625054 scopus 로고    scopus 로고
    • Involvement of a novel hydroxylamine oxidoreductase in anaerobic ammonium oxidation
    • J. Schalk, S. de Vries, J.G. Kuenen, and M.S. Jetten Involvement of a novel hydroxylamine oxidoreductase in anaerobic ammonium oxidation Biochemistry 39 2000 5405 5412
    • (2000) Biochemistry , vol.39 , pp. 5405-5412
    • Schalk, J.1    De Vries, S.2    Kuenen, J.G.3    Jetten, M.S.4
  • 10
    • 33847233302 scopus 로고    scopus 로고
    • Isolation of a multiheme protein with features of a hydrazine oxidizing enzyme from an anaerobic ammonium-oxidizing enrichment culture
    • M. Shimamura, T. Nishiyama, H. Shigetomo, T. Toyomoto, Y. Kawahara, K. Furukawa, and T. Fujii Isolation of a multiheme protein with features of a hydrazine oxidizing enzyme from an anaerobic ammonium-oxidizing enrichment culture Appl. Environ. Microbiol. 73 2007 1065 1072
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 1065-1072
    • Shimamura, M.1    Nishiyama, T.2    Shigetomo, H.3    Toyomoto, T.4    Kawahara, Y.5    Furukawa, K.6    Fujii, T.7
  • 11
    • 41549140435 scopus 로고    scopus 로고
    • Another multiheme protein, hydroxylamine oxidoreductase, abundantly produced in an anammox bacterium besides the hydrazine-oxidizing enzyme
    • M. Shimamura, T. Nishiyama, K. Shinya, Y. Kawahara, K. Furukawa, and T. Fujii Another multiheme protein, hydroxylamine oxidoreductase, abundantly produced in an anammox bacterium besides the hydrazine-oxidizing enzyme J. Biosci. Bioeng. 105 2008 243 248
    • (2008) J. Biosci. Bioeng. , vol.105 , pp. 243-248
    • Shimamura, M.1    Nishiyama, T.2    Shinya, K.3    Kawahara, Y.4    Furukawa, K.5    Fujii, T.6
  • 12
    • 78349267920 scopus 로고    scopus 로고
    • A heterodimeric cytochrome c complex with a very low redox potential from an anaerobic ammonium-oxidizing enrichment culture
    • S. Ukita, T. Fujii, D. Hira, T. Nishiyama, T. Kawase, C.T. Migita, and K. Furukawa A heterodimeric cytochrome c complex with a very low redox potential from an anaerobic ammonium-oxidizing enrichment culture FEMS Microbiol. Lett. 313 2010 61 67
    • (2010) FEMS Microbiol. Lett. , vol.313 , pp. 61-67
    • Ukita, S.1    Fujii, T.2    Hira, D.3    Nishiyama, T.4    Kawase, T.5    Migita, C.T.6    Furukawa, K.7
  • 13
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • O. Emanuelsson, S. Brunak, G. von Heijne, and H. Nielsen Locating proteins in the cell using TargetP, SignalP and related tools Nat. Protoc. 2 2007 953 971
    • (2007) Nat. Protoc. , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 14
    • 0034097583 scopus 로고    scopus 로고
    • Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase
    • K. Kataoka, H. Furusawa, K. Takagi, K. Yamaguchi, and S. Suzuki Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase J. Biochem. (Tokyo) 127 2000 345 350
    • (2000) J. Biochem. (Tokyo) , vol.127 , pp. 345-350
    • Kataoka, K.1    Furusawa, H.2    Takagi, K.3    Yamaguchi, K.4    Suzuki, S.5
  • 15
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace. A web-based environment for protein structure homology modelling
    • K. Arnold, L. Bordoli, J. Kopp, and T. Schwede The SWISS-MODEL Workspace. A web-based environment for protein structure homology modelling Bioinformatics 22 2006 195 201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 16
    • 0036306042 scopus 로고    scopus 로고
    • Crystal structure of the soluble domain of the major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria: A new class of copper-containing nitrite reductases
    • M.J. Boulanger, and M.E. Murphy Crystal structure of the soluble domain of the major anaerobically induced outer membrane protein (AniA) from pathogenic Neisseria: a new class of copper-containing nitrite reductases J. Mol. Biol. 315 2002 1111 1127
    • (2002) J. Mol. Biol. , vol.315 , pp. 1111-1127
    • Boulanger, M.J.1    Murphy, M.E.2
  • 17
    • 0019457194 scopus 로고
    • Purification and properties of a copper-containing nitrite reductase from a denitrifying bacterium, Alcaligenes faecalis strain S-6
    • T. Kakutani, H. Watanabe, K. Arima, and T. Beppu Purification and properties of a copper-containing nitrite reductase from a denitrifying bacterium, Alcaligenes faecalis strain S-6 J. Biochem. (Tokyo) 89 1981 453 461
    • (1981) J. Biochem. (Tokyo) , vol.89 , pp. 453-461
    • Kakutani, T.1    Watanabe, H.2    Arima, K.3    Beppu, T.4
  • 18
    • 0021478113 scopus 로고
    • Characterization of nitrite reductase from a denitrifier, Alcaligenes Sp. NCIB 11015. A novel copper protein
    • M. Masuko, H. Iwasaki, T. Sakurai, S. Suzuki, and A. Nakahara Characterization of nitrite reductase from a denitrifier, Alcaligenes Sp. NCIB 11015. A novel copper protein J. Biochem. 96 1984 447 454
    • (1984) J. Biochem. , vol.96 , pp. 447-454
    • Masuko, M.1    Iwasaki, H.2    Sakurai, T.3    Suzuki, S.4    Nakahara, A.5
  • 19
    • 0031963258 scopus 로고    scopus 로고
    • Ammonification in Bacillus subtilis utilizing dissimilatory nitrite reductase is dependent on resDE
    • T. Hoffmann, N. Frankenberg, M. Marino, and D. Jahn Ammonification in Bacillus subtilis utilizing dissimilatory nitrite reductase is dependent on resDE J. Bacteriol. 180 1998 186 189
    • (1998) J. Bacteriol. , vol.180 , pp. 186-189
    • Hoffmann, T.1    Frankenberg, N.2    Marino, M.3    Jahn, D.4
  • 20
    • 0028985478 scopus 로고
    • The copper-containing dissimilatory nitrite reductase involved in the denitrifying system of the fungus Fusarium oxysporum
    • M. Kobayashi, and H. Shoun The copper-containing dissimilatory nitrite reductase involved in the denitrifying system of the fungus Fusarium oxysporum J. Biol. Chem. 270 1995 4146 4151
    • (1995) J. Biol. Chem. , vol.270 , pp. 4146-4151
    • Kobayashi, M.1    Shoun, H.2
  • 21
    • 17944403239 scopus 로고    scopus 로고
    • Structure-function relationships of copper-containing nitrite reductases
    • S. Suzuki, K. Kataoka, K. Yamaguchi, T. Inoue, and Y. Kai Structure-function relationships of copper-containing nitrite reductases Coord. Chem. Rev. 190-192 1999 245 265
    • (1999) Coord. Chem. Rev. , vol.190-192 , pp. 245-265
    • Suzuki, S.1    Kataoka, K.2    Yamaguchi, K.3    Inoue, T.4    Kai, Y.5
  • 22
    • 84857917046 scopus 로고    scopus 로고
    • Gating mechanisms for biological electron transfer: Integrating structure with biophysics reveals the nature of redox control in cytochrome P450 reductase and copper-dependent nitrite reductase
    • N.G. Leferink, C.R. Pudney, S. Brenner, D.J. Heyes, R.R. Eady, S. Samar Hasnain, S. Hay, S.E. Rigby, and N.S. Scrutton Gating mechanisms for biological electron transfer: Integrating structure with biophysics reveals the nature of redox control in cytochrome P450 reductase and copper-dependent nitrite reductase FEBS Lett. 586 2012 578 584
    • (2012) FEBS Lett. , vol.586 , pp. 578-584
    • Leferink, N.G.1    Pudney, C.R.2    Brenner, S.3    Heyes, D.J.4    Eady, R.R.5    Samar Hasnain, S.6    Hay, S.7    Rigby, S.E.8    Scrutton, N.S.9
  • 23
    • 70449116515 scopus 로고    scopus 로고
    • Structural basis of inter-protein electron transfer for nitrite reduction in denitrification
    • M. Nojiri, H. Koteishi, T. Nakagami, K. Kobayashi, T. Inoue, K. Yamaguchi, and S. Suzuki Structural basis of inter-protein electron transfer for nitrite reduction in denitrification Nature 462 2009 117 120
    • (2009) Nature , vol.462 , pp. 117-120
    • Nojiri, M.1    Koteishi, H.2    Nakagami, T.3    Kobayashi, K.4    Inoue, T.5    Yamaguchi, K.6    Suzuki, S.7
  • 25
    • 1542378734 scopus 로고    scopus 로고
    • Electronic structures of metal sites in proteins and models: Contributions to function in blue copper proteins
    • E.I. Solomon, R.K. Szilagyi, S. DeBeer George, and L. Basumallick Electronic structures of metal sites in proteins and models: contributions to function in blue copper proteins Chem. Rev. 104 2004 419 458
    • (2004) Chem. Rev. , vol.104 , pp. 419-458
    • Solomon, E.I.1    Szilagyi, R.K.2    Debeer George, S.3    Basumallick, L.4
  • 26
    • 0030920834 scopus 로고    scopus 로고
    • PH-dependance for binding a single nitrite ion to each type-2 copper center in the copper-containing nitrite reductase of Alcaligenes xylosoxidans
    • Z.H.L. Abraham, B.E. Smith, B.D. Howes, D.J. Lowe, and R.R. Eady PH-dependance for binding a single nitrite ion to each type-2 copper center in the copper-containing nitrite reductase of Alcaligenes xylosoxidans Biochem. J. 324 1997 511 516
    • (1997) Biochem. J. , vol.324 , pp. 511-516
    • Abraham, Z.H.L.1    Smith, B.E.2    Howes, B.D.3    Lowe, D.J.4    Eady, R.R.5
  • 27
    • 0030599129 scopus 로고    scopus 로고
    • Site-directed mutagenesis of azurin from Pseudomonas aeruginosa enhances the formation of an electron-transfer complex with a copper-containing nitrite reductase from Alcaligenes faecalis S-6
    • M. Kukimoto, M. Nishiyama, M. Tanokura, M.E. Murphy, E.T. Adman, and S. Horinouchi Site-directed mutagenesis of azurin from Pseudomonas aeruginosa enhances the formation of an electron-transfer complex with a copper-containing nitrite reductase from Alcaligenes faecalis S-6 FEBS Lett. 394 1996 87 90
    • (1996) FEBS Lett. , vol.394 , pp. 87-90
    • Kukimoto, M.1    Nishiyama, M.2    Tanokura, M.3    Murphy, M.E.4    Adman, E.T.5    Horinouchi, S.6
  • 28
    • 0028958832 scopus 로고
    • Identification of interaction site of pseudoazurin with its redox partner, copper-containing nitrite reductase from Alcaligenes faecalis S-6
    • M. Kukimoto, M. Nishiyama, T. Ohnuki, S. Turley, E.T. Adman, S. Horinouchi, and T. Beppu Identification of interaction site of pseudoazurin with its redox partner, copper-containing nitrite reductase from Alcaligenes faecalis S-6 Protein Eng. 8 1995 153 158
    • (1995) Protein Eng. , vol.8 , pp. 153-158
    • Kukimoto, M.1    Nishiyama, M.2    Ohnuki, T.3    Turley, S.4    Adman, E.T.5    Horinouchi, S.6    Beppu, T.7
  • 29
    • 24744461441 scopus 로고    scopus 로고
    • Pseudoazurin-nitrite reductase interactions
    • A. Impagliazzo, L. Krippahl, and M. Ubbink Pseudoazurin-nitrite reductase interactions ChemBioChem 6 2005 1648 1653
    • (2005) ChemBioChem , vol.6 , pp. 1648-1653
    • Impagliazzo, A.1    Krippahl, L.2    Ubbink, M.3
  • 30
    • 37549050579 scopus 로고    scopus 로고
    • Conformation of pseudoazurin in the 152 kDa electron transfer complex with nitrite reductase determined by paramagnetic NMR
    • M.D. Vlasie, R. Fernandez-Busnadiego, M. Prudencio, and M. Ubbink Conformation of pseudoazurin in the 152 kDa electron transfer complex with nitrite reductase determined by paramagnetic NMR J. Mol. Biol. 375 2008 1405 1415
    • (2008) J. Mol. Biol. , vol.375 , pp. 1405-1415
    • Vlasie, M.D.1    Fernandez-Busnadiego, R.2    Prudencio, M.3    Ubbink, M.4
  • 31
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.