메뉴 건너뛰기




Volumn 62, Issue , 2008, Pages 93-111

Biosynthesis of the iron-molybdenum cofactor of nitrogenase

Author keywords

FeMo co; Iron sulfur; Mofe protein; nif; NifDK; Nitrogen fixation

Indexed keywords

IRON MOLYBDENUM COFACTOR; IRON SULFUR PROTEIN; MOLYBDENUM IRON PROTEIN; MOLYBDENUM NITROGENASE; NITROGENASE; PROTEIN NIFB; PROTEIN NIFEN; PROTEIN NIFH; PROTEIN NIFS; PROTEIN NIFU; UNCLASSIFIED DRUG;

EID: 50149115452     PISSN: 00664227     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.micro.62.081307.162737     Document Type: Review
Times cited : (347)

References (88)
  • 1
    • 0034112046 scopus 로고    scopus 로고
    • Modular organization and identification of a mononuclear iron-binding site within the NifU protein
    • Agar JN, Yuvaniyama P, Jack RF, Cash VL, Smith AD, et al. 2000. Modular organization and identification of a mononuclear iron-binding site within the NifU protein. J. Biol. Inorg. Chem. 5:167-77
    • (2000) J. Biol. Inorg. Chem , vol.5 , pp. 167-177
    • Agar, J.N.1    Yuvaniyama, P.2    Jack, R.F.3    Cash, V.L.4    Smith, A.D.5
  • 2
    • 0028882748 scopus 로고
    • Incorporation of iron and sulfur from NifB cofactor into the iron-molybdenum cofactor of dinitrogenase
    • Allen RM, Chatterjee R, Ludden PW, Shah VK. 1995. Incorporation of iron and sulfur from NifB cofactor into the iron-molybdenum cofactor of dinitrogenase. J. Biol. Chem. 270:26890-96
    • (1995) J. Biol. Chem , vol.270 , pp. 26890-26896
    • Allen, R.M.1    Chatterjee, R.2    Ludden, P.W.3    Shah, V.K.4
  • 4
    • 0023701258 scopus 로고
    • Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire nitrogen fixation gene cluster of Klebsiella pneumoniae
    • Arnold W, Rump A, Klipp W, Priefer UB, Pühler A. 1988. Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire nitrogen fixation gene cluster of Klebsiella pneumoniae. J. Mol. Biol. 203:715-38
    • (1988) J. Mol. Biol , vol.203 , pp. 715-738
    • Arnold, W.1    Rump, A.2    Klipp, W.3    Priefer, U.B.4    Pühler, A.5
  • 5
    • 11144229617 scopus 로고    scopus 로고
    • Substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis
    • Barney BM, Igarashi RY, Dos Santos PC, Dean DR, Seefeldt LC. 2004. Substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis. J. Biol. Chem. 279:53621-24
    • (2004) J. Biol. Chem , vol.279 , pp. 53621-53624
    • Barney, B.M.1    Igarashi, R.Y.2    Dos Santos, P.C.3    Dean, D.R.4    Seefeldt, L.C.5
  • 7
    • 0000421181 scopus 로고
    • Genetics and molecular biology of alternative nitrogen fixation systems
    • Bishop PE, Joerger RD. 1990. Genetics and molecular biology of alternative nitrogen fixation systems. Annu. Rev. Plant Physiol. Plant Mol. Biol. 41:109-25
    • (1990) Annu. Rev. Plant Physiol. Plant Mol. Biol , vol.41 , pp. 109-125
    • Bishop, P.E.1    Joerger, R.D.2
  • 8
    • 0023178462 scopus 로고
    • Products of the iron-molybdenum cofactor-specific biosynthetic genes, nifE and nifN, are structurally homologous to the products of the nitrogenase molybdenum-iron protein genes, nifD and nifK
    • Brigle KE, Weiss MC, Newton WE, Dean DR. 1987. Products of the iron-molybdenum cofactor-specific biosynthetic genes, nifE and nifN, are structurally homologous to the products of the nitrogenase molybdenum-iron protein genes, nifD and nifK. J. Bacteriol. 169:1547-53
    • (1987) J. Bacteriol , vol.169 , pp. 1547-1553
    • Brigle, K.E.1    Weiss, M.C.2    Newton, W.E.3    Dean, D.R.4
  • 9
    • 33845598693 scopus 로고    scopus 로고
    • Variable-temperature, variable-field magnetic circular dichroism spectroscopic study of the metal clusters in the ΔnifB and ΔnifH MoFe proteins of nitrogenase from Azotobacter vinelandii
    • Broach RB, Rupnik K, Hu Y, Fay AW, Cotton M, et al. 2006. Variable-temperature, variable-field magnetic circular dichroism spectroscopic study of the metal clusters in the ΔnifB and ΔnifH MoFe proteins of nitrogenase from Azotobacter vinelandii. Biochemistry 45:15039-48
    • (2006) Biochemistry , vol.45 , pp. 15039-15048
    • Broach, R.B.1    Rupnik, K.2    Hu, Y.3    Fay, A.W.4    Cotton, M.5
  • 11
    • 0027159222 scopus 로고
    • The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures
    • Chan MK, Kim J, Rees DC. 1993. The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures. Science 260:792-94
    • (1993) Science , vol.260 , pp. 792-794
    • Chan, M.K.1    Kim, J.2    Rees, D.C.3
  • 12
    • 0035678686 scopus 로고    scopus 로고
    • Nitrogen-fixation genes and nitrogenase activity in Clostridium acetobutylicum and Clostridium beijerinckii
    • Chen JS, Toth J, Kasap M. 2001. Nitrogen-fixation genes and nitrogenase activity in Clostridium acetobutylicum and Clostridium beijerinckii. J. Ind. Microbiol. Biotechnol. 27:281-86
    • (2001) J. Ind. Microbiol. Biotechnol , vol.27 , pp. 281-286
    • Chen, J.S.1    Toth, J.2    Kasap, M.3
  • 14
    • 18144416241 scopus 로고    scopus 로고
    • Genes required for rapid expression of nitrogenase activity in Azotobacter vinelandii
    • Curatti L, Brown CS, Ludden PW, Rubio LM. 2005. Genes required for rapid expression of nitrogenase activity in Azotobacter vinelandii. Proc. Natl. Acad. Sci. USA 102:6291-96
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6291-6296
    • Curatti, L.1    Brown, C.S.2    Ludden, P.W.3    Rubio, L.M.4
  • 15
    • 36749042644 scopus 로고    scopus 로고
    • In vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum and homocitrate using purified proteins
    • Curatti L, Hernandez JA, Igarashi RY, Soboh B, Zhao D, Rubio LM. 2007. In vitro synthesis of the iron-molybdenum cofactor of nitrogenase from iron, sulfur, molybdenum and homocitrate using purified proteins. Proc. Natl. Acad. Sci. USA 104:17626-31
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 17626-17631
    • Curatti, L.1    Hernandez, J.A.2    Igarashi, R.Y.3    Soboh, B.4    Zhao, D.5    Rubio, L.M.6
  • 16
    • 33645784842 scopus 로고    scopus 로고
    • NifB-dependent in vitro synthesis of the iron-molybdenum cofactor of nitrogenase
    • Curatti L, Ludden PW, Rubio LM. 2006. NifB-dependent in vitro synthesis of the iron-molybdenum cofactor of nitrogenase. Proc. Natl. Acad. Sci. USA 103:5297-301
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 5297-5301
    • Curatti, L.1    Ludden, P.W.2    Rubio, L.M.3
  • 17
    • 1542304548 scopus 로고    scopus 로고
    • Formation and insertion of the nitrogenase iron-molybdenum cofactor
    • Dos Santos PC, Dean DR, Hu Y, Ribbe MW. 2004. Formation and insertion of the nitrogenase iron-molybdenum cofactor. Chem. Rev. 104:1159-74
    • (2004) Chem. Rev , vol.104 , pp. 1159-1174
    • Dos Santos, P.C.1    Dean, D.R.2    Hu, Y.3    Ribbe, M.W.4
  • 18
    • 34147189950 scopus 로고    scopus 로고
    • Controlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems
    • Dos Santos PC, Johnson DC, Ragle BE, Unciuleac MC, Dean DR. 2007. Controlled expression of nif and isc iron-sulfur protein maturation components reveals target specificity and limited functional replacement between the two systems. J. Bacteriol. 189:2854-62
    • (2007) J. Bacteriol , vol.189 , pp. 2854-2862
    • Dos Santos, P.C.1    Johnson, D.C.2    Ragle, B.E.3    Unciuleac, M.C.4    Dean, D.R.5
  • 20
    • 0041856106 scopus 로고    scopus 로고
    • The three-dimensional structure of the core domain of NafY from Azotobacter vinelandii determined at 1.8-A resolution
    • Dyer DH, Rubio LM, Thoden JB, Holden HM, Ludden PW, Rayment I. 2003. The three-dimensional structure of the core domain of NafY from Azotobacter vinelandii determined at 1.8-A resolution. J. Biol. Chem. 278:32150-56
    • (2003) J. Biol. Chem , vol.278 , pp. 32150-32156
    • Dyer, D.H.1    Rubio, L.M.2    Thoden, J.B.3    Holden, H.M.4    Ludden, P.W.5    Rayment, I.6
  • 21
    • 0037031703 scopus 로고    scopus 로고
    • Nitrogenase MoFe-protein at 1.16 A resolution: A central ligand in the FeMo-cofactor
    • Einsle O, Tezcan FA, Andrade SL, Schmid B, Yoshida M, et al. 2002. Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor. Science 297:1696-700
    • (2002) Science , vol.297 , pp. 1696-1700
    • Einsle, O.1    Tezcan, F.A.2    Andrade, S.L.3    Schmid, B.4    Yoshida, M.5
  • 22
    • 21144443933 scopus 로고    scopus 로고
    • A new type of metalloprotein: The Mo storage protein from Azotobacter vinelandii contains a polynuclear molybdenum-oxide cluster
    • Fenske D, Gnida M, Schneider K, Meyer-Klaucke W, Schemberg J, et al. 2005. A new type of metalloprotein: The Mo storage protein from Azotobacter vinelandii contains a polynuclear molybdenum-oxide cluster. ChemBioChem 6:405-13
    • (2005) ChemBioChem , vol.6 , pp. 405-413
    • Fenske, D.1    Gnida, M.2    Schneider, K.3    Meyer-Klaucke, W.4    Schemberg, J.5
  • 23
    • 0027959635 scopus 로고
    • nifU gene product from Azotobacter vinelandii is a homodimer that contains two identical [2Fe-2S] clusters
    • Fu W, Jack RF, Morgan TV, Dean DR, Johnson MK. 1994. nifU gene product from Azotobacter vinelandii is a homodimer that contains two identical [2Fe-2S] clusters. Biochemistry 33:13455-63
    • (1994) Biochemistry , vol.33 , pp. 13455-13463
    • Fu, W.1    Jack, R.F.2    Morgan, T.V.3    Dean, D.R.4    Johnson, M.K.5
  • 24
    • 0026775088 scopus 로고
    • FeMo cofactor synthesis by a nifH mutant with altered Mg·ATP reactivity
    • Gavini N, Burgess BK. 1992. FeMo cofactor synthesis by a nifH mutant with altered Mg·ATP reactivity. J. Biol. Chem. 267:21179-86
    • (1992) J. Biol. Chem , vol.267 , pp. 21179-21186
    • Gavini, N.1    Burgess, B.K.2
  • 25
    • 33947398756 scopus 로고    scopus 로고
    • Identification of a Mo-Fe-S cluster on NifEN by Mo K-edge extended X-ray absorption fine structure
    • George SJ, Igarashi RY, Piamonteze C, Soboh B, Cramer SP, Rubio LM. 2007. Identification of a Mo-Fe-S cluster on NifEN by Mo K-edge extended X-ray absorption fine structure. J. Am. Chem. Soc. 129:3060-61
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 3060-3061
    • George, S.J.1    Igarashi, R.Y.2    Piamonteze, C.3    Soboh, B.4    Cramer, S.P.5    Rubio, L.M.6
  • 26
    • 53849103841 scopus 로고    scopus 로고
    • EXAFS and NRVS reveal that NifB-co, a FeMo-co precursor, comprises a 6 Fe core with an interstitial light atom
    • In press
    • George SJ, Igarashi RY, Xiao Y, Hernandez JA, Demuez M, et al. 2008. EXAFS and NRVS reveal that NifB-co, a FeMo-co precursor, comprises a 6 Fe core with an interstitial light atom. J. Am. Chem. Soc. In press
    • (2008) J. Am. Chem. Soc
    • George, S.J.1    Igarashi, R.Y.2    Xiao, Y.3    Hernandez, J.A.4    Demuez, M.5
  • 27
    • 0026662162 scopus 로고
    • Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii
    • Georgiadis MM, Komiya H, Chakrabarti P, Woo D, Kornuc JJ, Rees DC. 1992. Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Science 257:1653-59
    • (1992) Science , vol.257 , pp. 1653-1659
    • Georgiadis, M.M.1    Komiya, H.2    Chakrabarti, P.3    Woo, D.4    Kornuc, J.J.5    Rees, D.C.6
  • 30
    • 0030726129 scopus 로고    scopus 로고
    • Molybdate transport and regulation in bacteria
    • Grunden AM, Shanmugam KT. 1997. Molybdate transport and regulation in bacteria. Arch. Microbiol. 168:345-54
    • (1997) Arch. Microbiol , vol.168 , pp. 345-354
    • Grunden, A.M.1    Shanmugam, K.T.2
  • 31
    • 0040412793 scopus 로고
    • Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle
    • Hageman RV, Burris RH. 1978. Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle. Proc. Natl. Acad. Sci. USA 75:2699-702
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 2699-2702
    • Hageman, R.V.1    Burris, R.H.2
  • 32
    • 33845706832 scopus 로고    scopus 로고
    • NifX and NifEN exchange NifB cofactor and the VK-cluster, a newly isolated intermediate of the iron-molybdenum cofactor biosynthetic pathway
    • Hernandez JA, Igarashi RY, Soboh B, Curatti L, Dean DR, et al. 2007. NifX and NifEN exchange NifB cofactor and the VK-cluster, a newly isolated intermediate of the iron-molybdenum cofactor biosynthetic pathway. Mol. Microbiol. 63:177-92
    • (2007) Mol. Microbiol , vol.63 , pp. 177-192
    • Hernandez, J.A.1    Igarashi, R.Y.2    Soboh, B.3    Curatti, L.4    Dean, D.R.5
  • 33
    • 0028792366 scopus 로고
    • Characterization of the γ protein and its involvement in the metallocluster assembly and maturation of dinitrogenase from Azotobacter vinelandii
    • Homer MJ, Dean DR, Roberts GP. 1995. Characterization of the γ protein and its involvement in the metallocluster assembly and maturation of dinitrogenase from Azotobacter vinelandii. J. Biol. Chem. 270:24745-52
    • (1995) J. Biol. Chem , vol.270 , pp. 24745-24752
    • Homer, M.J.1    Dean, D.R.2    Roberts, G.P.3
  • 34
    • 0023990921 scopus 로고
    • Homocitrate cures the NifV-phenotype in Klebsiella pneumoniae
    • Hoover TR, Imperial J, Ludden PW, Shah VK. 1988. Homocitrate cures the NifV-phenotype in Klebsiella pneumoniae. J. Bacteriol. 170:1978-79
    • (1988) J. Bacteriol , vol.170 , pp. 1978-1979
    • Hoover, T.R.1    Imperial, J.2    Ludden, P.W.3    Shah, V.K.4
  • 35
    • 0023616333 scopus 로고
    • Identification of the V factor needed for synthesis of the iron-molybdenum cofactor of nitrogenase as homocitrate
    • Hoover TR, Robertson AD, Cerny RL, Hayes RN, Imperial J, et al. 1987. Identification of the V factor needed for synthesis of the iron-molybdenum cofactor of nitrogenase as homocitrate. Nature 329:855-57
    • (1987) Nature , vol.329 , pp. 855-857
    • Hoover, T.R.1    Robertson, A.D.2    Cerny, R.L.3    Hayes, R.N.4    Imperial, J.5
  • 37
    • 14744279761 scopus 로고    scopus 로고
    • Identification of a nitrogenase FeMo cofactor precursor on NifEN complex
    • Hu Y, Fay AW, Ribbe MW. 2005. Identification of a nitrogenase FeMo cofactor precursor on NifEN complex. Proc. Natl. Acad. Sci. USA 102:3236-41
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3236-3241
    • Hu, Y.1    Fay, A.W.2    Ribbe, M.W.3
  • 39
    • 0142106006 scopus 로고    scopus 로고
    • Nitrogen fixation: The mechanism of the Mo-dependent nitrogenase
    • Igarashi RY, Seefeldt LC. 2003. Nitrogen fixation: the mechanism of the Mo-dependent nitrogenase. Crit. Rev. Biochem. Mol. Biol. 38:351-84
    • (2003) Crit. Rev. Biochem. Mol. Biol , vol.38 , pp. 351-384
    • Igarashi, R.Y.1    Seefeldt, L.C.2
  • 40
    • 0024974058 scopus 로고
    • Substrate reduction properties of dinitrogenase activated in vitro are dependent upon the presence of homocitrate or its analogues during iron-molybdenum cofactor synthesis
    • Imperial J, Hoover TR, Madden MS, Ludden PW, Shah VK. 1989. Substrate reduction properties of dinitrogenase activated in vitro are dependent upon the presence of homocitrate or its analogues during iron-molybdenum cofactor synthesis. Biochemistry 28:7796-99
    • (1989) Biochemistry , vol.28 , pp. 7796-7799
    • Imperial, J.1    Hoover, T.R.2    Madden, M.S.3    Ludden, P.W.4    Shah, V.K.5
  • 41
    • 0021183145 scopus 로고
    • Role of the nifQ gene product in the incorporation of molybdenum into nitrogenase in Klebsiella pneumoniae
    • Imperial J, Ugalde RA, Shah VK, Brill WJ. 1984. Role of the nifQ gene product in the incorporation of molybdenum into nitrogenase in Klebsiella pneumoniae. J. Bacteriol. 158:187-94
    • (1984) J. Bacteriol , vol.158 , pp. 187-194
    • Imperial, J.1    Ugalde, R.A.2    Shah, V.K.3    Brill, W.J.4
  • 44
    • 0023989461 scopus 로고
    • Nucleotide sequence and genetic analysis of the nifB-nifQ region from Azotobacter vinelandii
    • Joerger RD, Bishop PE. 1988. Nucleotide sequence and genetic analysis of the nifB-nifQ region from Azotobacter vinelandii. J. Bacteriol. 170:1475-87
    • (1988) J. Bacteriol , vol.170 , pp. 1475-1487
    • Joerger, R.D.1    Bishop, P.E.2
  • 45
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson DC, Dean DR, Smith AD, Johnson MK. 2005. Structure, function, and formation of biological iron-sulfur clusters. Annu. Rev. Biochem. 74:247-81
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 46
    • 14644425981 scopus 로고    scopus 로고
    • NifU and NifS are required for the maturation of nitrogenase and cannot replace the function of isc-gene products in Azotobacter vinelandii
    • Johnson DC, Dos Santos PC, Dean DR. 2005. NifU and NifS are required for the maturation of nitrogenase and cannot replace the function of isc-gene products in Azotobacter vinelandii. Biochem. Soc. Trans. 33:90-93
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 90-93
    • Johnson, D.C.1    Dos Santos, P.C.2    Dean, D.R.3
  • 47
    • 0026734002 scopus 로고
    • Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii
    • Kim J, Rees DC. 1992. Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii. Nature 360:553-60
    • (1992) Nature , vol.360 , pp. 553-560
    • Kim, J.1    Rees, D.C.2
  • 48
    • 0029929865 scopus 로고    scopus 로고
    • Evidence for electron transfer from the nitrogenase iron protein to the molybdenum-iron protein without Mg·ATP hydrolysis: Characterization of a tight protein-protein complex
    • Lanzilotta WN, Fisher K, Seefeldt LC. 1996. Evidence for electron transfer from the nitrogenase iron protein to the molybdenum-iron protein without Mg·ATP hydrolysis: characterization of a tight protein-protein complex. Biochemistry 35:7188-96
    • (1996) Biochemistry , vol.35 , pp. 7188-7196
    • Lanzilotta, W.N.1    Fisher, K.2    Seefeldt, L.C.3
  • 49
    • 0032488605 scopus 로고    scopus 로고
    • Electron transfer in nitrogenase analyzed by Marcus theory: Evidence for gating by Mg·ATP
    • Lanzilotta WN, Parker VD, Seefeldt LC. 1998. Electron transfer in nitrogenase analyzed by Marcus theory: evidence for gating by Mg·ATP. Biochemistry 37:399-407
    • (1998) Biochemistry , vol.37 , pp. 399-407
    • Lanzilotta, W.N.1    Parker, V.D.2    Seefeldt, L.C.3
  • 50
    • 11844251701 scopus 로고    scopus 로고
    • Biosynthesis of the iron-molybdenum and iron-vanadium cofactors of the nif- and vnf-encoded nitrogenases
    • ed. BE Smith, RL Richards, WE Newton, pp, Dordretch, The Neth, Kluwer
    • Ludden PW, Rangaraj P, Rubio LM. 2004. Biosynthesis of the iron-molybdenum and iron-vanadium cofactors of the nif- and vnf-encoded nitrogenases. In Catalysts for Nitrogen Fixation: Nitrogenases, Relevant Chemical Models, and Commercial Processes, ed. BE Smith, RL Richards, WE Newton, pp. 219-53. Dordretch, The Neth.: Kluwer
    • (2004) Catalysts for Nitrogen Fixation: Nitrogenases, Relevant Chemical Models, and Commercial Processes , pp. 219-253
    • Ludden, P.W.1    Rangaraj, P.2    Rubio, L.M.3
  • 51
    • 0018171975 scopus 로고
    • Fine-structure mapping and complementation analysis of nif (nitrogen fixation) genes in Klebsiella pneumoniae
    • MacNeil T, MacNeil D, Roberts GP, Supiano MA, Brill WJ. 1978. Fine-structure mapping and complementation analysis of nif (nitrogen fixation) genes in Klebsiella pneumoniae. J. Bacteriol. 136:253-66
    • (1978) J. Bacteriol , vol.136 , pp. 253-266
    • MacNeil, T.1    MacNeil, D.2    Roberts, G.P.3    Supiano, M.A.4    Brill, W.J.5
  • 52
    • 1642500165 scopus 로고    scopus 로고
    • The NifL-NifA system: A multidomain transcriptional regulatory complex that integrates environmental signals
    • Martinez-Argudo I, Little R, Shearer N, Johnson P, Dixon RA. 2004. The NifL-NifA system: a multidomain transcriptional regulatory complex that integrates environmental signals. J. Bacteriol. 186:601-10
    • (2004) J. Bacteriol , vol.186 , pp. 601-610
    • Martinez-Argudo, I.1    Little, R.2    Shearer, N.3    Johnson, P.4    Dixon, R.A.5
  • 54
    • 0037144602 scopus 로고    scopus 로고
    • Crystallographic analysis of the MoFe protein of nitrogenase from a nifV mutant of Klebsiella pneumoniae identifies citrate as a ligand to the molybdenum of iron molybdenum cofactor (FeMoco)
    • Mayer SM, Gormal CA, Smith BE, Lawson DM. 2002. Crystallographic analysis of the MoFe protein of nitrogenase from a nifV mutant of Klebsiella pneumoniae identifies citrate as a ligand to the molybdenum of iron molybdenum cofactor (FeMoco). J. Biol. Chem. 277:35263-66
    • (2002) J. Biol. Chem , vol.277 , pp. 35263-35266
    • Mayer, S.M.1    Gormal, C.A.2    Smith, B.E.3    Lawson, D.M.4
  • 55
    • 0020776180 scopus 로고
    • Nitrogenase of Klebsiella pneumoniae nifV mutants
    • McLean PA, Smith BE, Dixon RA. 1983. Nitrogenase of Klebsiella pneumoniae nifV mutants. Biochem. J. 211:589-97
    • (1983) Biochem. J , vol.211 , pp. 589-597
    • McLean, P.A.1    Smith, B.E.2    Dixon, R.A.3
  • 56
    • 0024709552 scopus 로고
    • Purification and characterization of the nifN and nifE gene products from Azotobacter vinelandii mutant UW45
    • Paustian TD, Shah VK, Roberts GP. 1989. Purification and characterization of the nifN and nifE gene products from Azotobacter vinelandii mutant UW45. Proc. Natl. Acad. Sci. USA 86:6082-86
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6082-6086
    • Paustian, T.D.1    Shah, V.K.2    Roberts, G.P.3
  • 57
    • 0037130956 scopus 로고    scopus 로고
    • 99Mo-containing iron-molybdenum cofactor precursors of nitrogenase on NifNE, NifH, and NifX of Azotobacter vinelandii
    • 99Mo-containing iron-molybdenum cofactor precursors of nitrogenase on NifNE, NifH, and NifX of Azotobacter vinelandii. J. Biol. Chem. 277:40106-11
    • (2002) J. Biol. Chem , vol.277 , pp. 40106-40111
    • Rangaraj, P.1    Ludden, P.W.2
  • 58
    • 0035844146 scopus 로고    scopus 로고
    • 55Fe-labeled precursors of the iron-molybdenum cofactor of nitrogenase on NifH and NifX of Azotobacter vinelandii
    • 55Fe-labeled precursors of the iron-molybdenum cofactor of nitrogenase on NifH and NifX of Azotobacter vinelandii. J. Biol. Chem. 276:15968-74
    • (2001) J. Biol. Chem , vol.276 , pp. 15968-15974
    • Rangaraj, P.1    Ruttimann-Johnson, C.2    Shah, V.K.3    Ludden, P.W.4
  • 59
    • 0032879462 scopus 로고    scopus 로고
    • Inhibition of iron-molybdenum cofactor biosynthesis by L127Δ NifH and evidence for a complex formation between L127Δ NifH and NifNE
    • Rangaraj P, Ryle MJ, Lanzilotta WN, Goodwin PJ, Dean DR, et al. 1999. Inhibition of iron-molybdenum cofactor biosynthesis by L127Δ NifH and evidence for a complex formation between L127Δ NifH and NifNE. J. Biol. Chem. 274:29413-19
    • (1999) J. Biol. Chem , vol.274 , pp. 29413-29419
    • Rangaraj, P.1    Ryle, M.J.2    Lanzilotta, W.N.3    Goodwin, P.J.4    Dean, D.R.5
  • 60
    • 0033538446 scopus 로고    scopus 로고
    • In vitro biosynthesis of iron-molybdenum cofactor and maturation of the nif-encoded apodinitrogenase. Effect of substitution for NifH with site-specifically altered forms of NifH
    • Rangaraj P, Ryle MJ, Lanzilotta WN, Ludden PW, Shah VK. 1999. In vitro biosynthesis of iron-molybdenum cofactor and maturation of the nif-encoded apodinitrogenase. Effect of substitution for NifH with site-specifically altered forms of NifH. J. Biol. Chem. 274:19778-84
    • (1999) J. Biol. Chem , vol.274 , pp. 19778-19784
    • Rangaraj, P.1    Ryle, M.J.2    Lanzilotta, W.N.3    Ludden, P.W.4    Shah, V.K.5
  • 61
    • 0030826663 scopus 로고    scopus 로고
    • ApoNifH functions in iron-molybdenum cofactor synthesis and apodinitrogenase maturation
    • Rangaraj P, Shah VK, Ludden PW. 1997. ApoNifH functions in iron-molybdenum cofactor synthesis and apodinitrogenase maturation. Proc. Natl. Acad. Sci. USA 94:11250-55
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11250-11255
    • Rangaraj, P.1    Shah, V.K.2    Ludden, P.W.3
  • 63
    • 0037189539 scopus 로고    scopus 로고
    • The FeMoco-deficient MoFe protein produced by a nifH deletion strain of Azotobacter vinelandii shows unusual P-cluster features
    • Ribbe MW, Hu Y, Guo M, Schmid B, Burgess BK. 2002. The FeMoco-deficient MoFe protein produced by a nifH deletion strain of Azotobacter vinelandii shows unusual P-cluster features. J. Biol. Chem. 277:23469-76
    • (2002) J. Biol. Chem , vol.277 , pp. 23469-23476
    • Ribbe, M.W.1    Hu, Y.2    Guo, M.3    Schmid, B.4    Burgess, B.K.5
  • 64
    • 0018167549 scopus 로고
    • Regulation and characterization of protein products coded by the nif (nitrogen fixation) genes of Klebsiella pneumoniae
    • Roberts GP, MacNeil T, MacNeil D, Brill WJ. 1978. Regulation and characterization of protein products coded by the nif (nitrogen fixation) genes of Klebsiella pneumoniae. J. Bacteriol. 136:267-79
    • (1978) J. Bacteriol , vol.136 , pp. 267-279
    • Roberts, G.P.1    MacNeil, T.2    MacNeil, D.3    Brill, W.J.4
  • 65
    • 0027241148 scopus 로고
    • Expression of the nifBfdxNnifOQ region of Azotobacter vinelandii and its role in nitrogenase activity
    • Rodríguez-Quiñones F, Bosch R, Imperial J. 1993. Expression of the nifBfdxNnifOQ region of Azotobacter vinelandii and its role in nitrogenase activity. J. Bacteriol. 175:2926-35
    • (1993) J. Bacteriol , vol.175 , pp. 2926-2935
    • Rodríguez-Quiñones, F.1    Bosch, R.2    Imperial, J.3
  • 66
    • 0028924262 scopus 로고
    • Characteristics of NIFNE in Azotobacter vinelandii strains. Implications for the synthesis of the iron-molybdenum cofactor of dinitrogenase
    • Roll JT, Shah VK, Dean DR, Roberts GP. 1995. Characteristics of NIFNE in Azotobacter vinelandii strains. Implications for the synthesis of the iron-molybdenum cofactor of dinitrogenase. J. Biol. Chem. 270:4432-37
    • (1995) J. Biol. Chem , vol.270 , pp. 4432-4437
    • Roll, J.T.1    Shah, V.K.2    Dean, D.R.3    Roberts, G.P.4
  • 67
    • 0042898981 scopus 로고    scopus 로고
    • The gene products of the nif regulon
    • ed. GJ Leigh, pp, Amsterdam: Elsevier
    • Rubio LM, Ludden PW. 2002. The gene products of the nif regulon. In Nitrogen Fixation at the Millenium, ed. GJ Leigh, pp. 101-36. Amsterdam: Elsevier
    • (2002) Nitrogen Fixation at the Millenium , pp. 101-136
    • Rubio, L.M.1    Ludden, P.W.2
  • 68
    • 11844270546 scopus 로고    scopus 로고
    • Maturation of nitrogenase: A biochemical puzzle
    • Rubio LM, Ludden PW. 2005. Maturation of nitrogenase: a biochemical puzzle. J. Bacteriol. 187:405-14
    • (2005) J. Bacteriol , vol.187 , pp. 405-414
    • Rubio, L.M.1    Ludden, P.W.2
  • 69
    • 0037134499 scopus 로고    scopus 로고
    • Cloning and mutational analysis of the γ gene from Azotobacter vinelandii defines a new family of proteins capable of metallocluster-binding and protein stabilization
    • Rubio LM, Rangaraj P, Homer MJ, Roberts GP, Ludden PW. 2002. Cloning and mutational analysis of the γ gene from Azotobacter vinelandii defines a new family of proteins capable of metallocluster-binding and protein stabilization. J. Biol. Chem. 277:14299-305
    • (2002) J. Biol. Chem , vol.277 , pp. 14299-14305
    • Rubio, L.M.1    Rangaraj, P.2    Homer, M.J.3    Roberts, G.P.4    Ludden, P.W.5
  • 70
    • 2442425301 scopus 로고    scopus 로고
    • Purification and characterization of NafY (apodinitrogenase γ subunit) from Azotobacter vinelandii
    • Rubio LM, Singer SW, Ludden PW. 2004. Purification and characterization of NafY (apodinitrogenase γ subunit) from Azotobacter vinelandii. J. Biol. Chem. 279:19739-46
    • (2004) J. Biol. Chem , vol.279 , pp. 19739-19746
    • Rubio, L.M.1    Singer, S.W.2    Ludden, P.W.3
  • 71
    • 0037377874 scopus 로고    scopus 로고
    • VnfY is required for full activity of the vanadium-containing dinitrogenase in Azotobacter vinelandii
    • Ruttimann-Johnson C, Rubio LM, Dean DR, Ludden PW. 2003. VnfY is required for full activity of the vanadium-containing dinitrogenase in Azotobacter vinelandii. J. Bacteriol. 185:2383-86
    • (2003) J. Bacteriol , vol.185 , pp. 2383-2386
    • Ruttimann-Johnson, C.1    Rubio, L.M.2    Dean, D.R.3    Ludden, P.W.4
  • 72
    • 0028057466 scopus 로고
    • In vitro synthesis of the iron-molybdenum cofactor of nitrogenase. Purification and characterization of NifB cofactor, the product of NIFB protein
    • Shah VK, Allen JR, Spangler NJ, Ludden PW. 1994. In vitro synthesis of the iron-molybdenum cofactor of nitrogenase. Purification and characterization of NifB cofactor, the product of NIFB protein. J. Biol. Chem. 269:1154-58
    • (1994) J. Biol. Chem , vol.269 , pp. 1154-1158
    • Shah, V.K.1    Allen, J.R.2    Spangler, N.J.3    Ludden, P.W.4
  • 73
    • 0006156895 scopus 로고
    • Isolation of an iron-molybdenum cofactor from nitrogenase
    • Shah VK, Brill WJ. 1977. Isolation of an iron-molybdenum cofactor from nitrogenase. Proc. Natl. Acad. Sci. USA 74:3249-53
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3249-3253
    • Shah, V.K.1    Brill, W.J.2
  • 75
    • 0021100144 scopus 로고
    • Electron transport to nitrogenase. Purification and characterization of pyruvate:flavodoxin oxidoreductase. The nifJ gene product
    • Shah VK, Stacey G, Brill WJ. 1983. Electron transport to nitrogenase. Purification and characterization of pyruvate:flavodoxin oxidoreductase. The nifJ gene product. J. Biol. Chem. 258:12064-68
    • (1983) J. Biol. Chem , vol.258 , pp. 12064-12068
    • Shah, V.K.1    Stacey, G.2    Brill, W.J.3
  • 76
    • 0021757851 scopus 로고
    • A nitrogen pressure of 50 atmospheres does not prevent evolution of hydrogen by nitrogenase
    • Simpson FB, Burris RH. 1984. A nitrogen pressure of 50 atmospheres does not prevent evolution of hydrogen by nitrogenase. Science 224:1095-97
    • (1984) Science , vol.224 , pp. 1095-1097
    • Simpson, F.B.1    Burris, R.H.2
  • 77
    • 25444446576 scopus 로고    scopus 로고
    • NifS-mediated assembly of [4Fe-4S] clusters in the N- and C-terminal domains of the NifU scaffold protein
    • Smith AD, Jameson GN, Dos Santos PC, Agar JN, Naik S, et al. 2005. NifS-mediated assembly of [4Fe-4S] clusters in the N- and C-terminal domains of the NifU scaffold protein. Biochemistry 44:12955-69
    • (2005) Biochemistry , vol.44 , pp. 12955-12969
    • Smith, A.D.1    Jameson, G.N.2    Dos Santos, P.C.3    Agar, J.N.4    Naik, S.5
  • 78
    • 33845686746 scopus 로고    scopus 로고
    • Purification of a NifEN protein complex that contains bound Mo and a FeMo-co precursor from an Azotobacter vinelandii ΔnifHDK strain
    • Soboh B, Igarashi RY, Hernandez JA, Rubio LM. 2006. Purification of a NifEN protein complex that contains bound Mo and a FeMo-co precursor from an Azotobacter vinelandii ΔnifHDK strain. J. Biol. Chem. 281:36701-9
    • (2006) J. Biol. Chem , vol.281 , pp. 36701-36709
    • Soboh, B.1    Igarashi, R.Y.2    Hernandez, J.A.3    Rubio, L.M.4
  • 79
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
    • Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE. 2001. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res. 29:1097-106
    • (2001) Nucleic Acids Res , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 80
    • 0021218602 scopus 로고
    • Biosynthesis of iron-molybdenum cofactor in the absence of nitrogenase
    • Ugalde RA, Imperial J, Shah VK, Brill WJ. 1984. Biosynthesis of iron-molybdenum cofactor in the absence of nitrogenase. J. Bacteriol. 159:888-93
    • (1984) J. Bacteriol , vol.159 , pp. 888-893
    • Ugalde, R.A.1    Imperial, J.2    Shah, V.K.3    Brill, W.J.4
  • 81
    • 0022386747 scopus 로고
    • Biosynthesis of the iron-molybdenum cofactor and the molybdenum cofactor in Klebsiella pneumoniae: Effect of sulfur source
    • Ugalde RA, Imperial J, Shah VK, Brill WJ. 1985. Biosynthesis of the iron-molybdenum cofactor and the molybdenum cofactor in Klebsiella pneumoniae: effect of sulfur source. J. Bacteriol. 164:1081-87
    • (1985) J. Bacteriol , vol.164 , pp. 1081-1087
    • Ugalde, R.A.1    Imperial, J.2    Shah, V.K.3    Brill, W.J.4
  • 82
    • 33847635732 scopus 로고    scopus 로고
    • S-adenosylmethionine as an oxidant: The radical SAM superfamily
    • Wang SC, Frey PA. 2007. S-adenosylmethionine as an oxidant: the radical SAM superfamily. Trends Biochem. Sci. 32:101-10
    • (2007) Trends Biochem. Sci , vol.32 , pp. 101-110
    • Wang, S.C.1    Frey, P.A.2
  • 84
    • 37549064005 scopus 로고    scopus 로고
    • Evidence for nifU and nifS participation in the biosynthesis of the iron-molybdenum cofactor of nitrogenase
    • Zhao D, Curatti L, Rubio LM. 2007. Evidence for nifU and nifS participation in the biosynthesis of the iron-molybdenum cofactor of nitrogenase. J. Biol. Chem. 282:37016-25
    • (2007) J. Biol. Chem , vol.282 , pp. 37016-37025
    • Zhao, D.1    Curatti, L.2    Rubio, L.M.3
  • 85
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • Zheng L, Cash VL, Flint DH, Dean DR. 1998. Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. J. Biol. Chem. 273:13264-72
    • (1998) J. Biol. Chem , vol.273 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4
  • 86
    • 0028265941 scopus 로고
    • Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product
    • Zheng L, White RH, Cash VL, Dean DR. 1994. Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product. Biochemistry 33:4714-20
    • (1994) Biochemistry , vol.33 , pp. 4714-4720
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Dean, D.R.4
  • 87
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • Zheng L, White RH, Cash VL, Jack RF, Dean DR. 1993. Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc. Natl. Acad. Sci. USA 90:2754-58
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5
  • 88
    • 0030885159 scopus 로고    scopus 로고
    • Purification of the Azotobacter vinelandii nifV-encoded homocitrate synthase
    • Zheng L, White RH, Dean DR. 1997. Purification of the Azotobacter vinelandii nifV-encoded homocitrate synthase. J. Bacteriol. 179:5963-66
    • (1997) J. Bacteriol , vol.179 , pp. 5963-5966
    • Zheng, L.1    White, R.H.2    Dean, D.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.