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Volumn 187, Issue 2, 2005, Pages 405-414

Maturation of nitrogenase: A biochemical puzzle

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHAPERONIN; DINITROGENASE REDUCTASE; GENE PRODUCT; METALLOPROTEIN; MOLYBDENUM IRON PROTEIN; NITROGENASE;

EID: 11844270546     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.2.405-414.2005     Document Type: Review
Times cited : (168)

References (82)
  • 1
    • 0027505027 scopus 로고
    • Dinitrogenase reductase- and MgATP-dependent maturation of apodinitrogenase from Azotobacter vinelandii
    • Allen, R. M., M. J. Homer, R. Chatterjee, P. W. Ludden, G. P. Roberts, and V. K. Shah. 1993. Dinitrogenase reductase- and MgATP-dependent maturation of apodinitrogenase from Azotobacter vinelandii. J. Biol. Chem. 268:23670-23674.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23670-23674
    • Allen, R.M.1    Homer, M.J.2    Chatterjee, R.3    Ludden, P.W.4    Roberts, G.P.5    Shah, V.K.6
  • 2
    • 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., A. Rump, W. Klipp, U. B. Priefer, and A. Puhler. 1988. Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire nitrogen fixation gene cluster of Klebsiella pneumoniae. J. Mol. Biol. 203:715-738.
    • (1988) J. Mol. Biol. , vol.203 , pp. 715-738
    • Arnold, W.1    Rump, A.2    Klipp, W.3    Priefer, U.B.4    Puhler, A.5
  • 3
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert, H., R. H. Holm, and E. Munck. 1997. Iron-sulfur clusters: nature's modular, multipurpose structures. Science 277:653-659.
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Munck, E.3
  • 4
    • 0346596604 scopus 로고
    • Evidence for an alternative nitrogen fixation system in Azotobacter vinelandii
    • Bishop, P. E., D. M. L. Jarlenski, and D. R. Hetherington. 1980. Evidence for an alternative nitrogen fixation system in Azotobacter vinelandii. Proc. Natl. Acad. Sci. USA 77:7342-7346.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 7342-7346
    • Bishop, P.E.1    Jarlenski, D.M.L.2    Hetherington, D.R.3
  • 5
    • 0000421181 scopus 로고
    • Genetics and molecular biology of alternative nitrogen fixation systems
    • Bishop, P. E., and R. D. Joerger. 1990. Genetics and molecular biology of alternative nitrogen fixation systems. Annu. Rev. Plant Physiol. Plant Mol. Biol. 41:109-125.
    • (1990) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.41 , pp. 109-125
    • Bishop, P.E.1    Joerger, R.D.2
  • 6
    • 0022551370 scopus 로고
    • Nitrogen fixation by Azotobacter vinelandii strains having deletions in structural genes for nitrogenase
    • Bishop, P. E., R. Premakumar, D. R. Dean, M. R. Jacobson, J. R. Chisnell, T. M. Rizzo, and J. Kopczynski. 1986. Nitrogen fixation by Azotobacter vinelandii strains having deletions in structural genes for nitrogenase. Science 232:92-94.
    • (1986) Science , vol.232 , pp. 92-94
    • Bishop, P.E.1    Premakumar, R.2    Dean, D.R.3    Jacobson, M.R.4    Chisnell, J.R.5    Rizzo, T.M.6    Kopczynski, J.7
  • 7
    • 0027439505 scopus 로고
    • The unusual metal clusters of nitrogenase: Structural features revealed by X-ray anomalous diffraction studies of the MoFe protein from Clostridium pasteurianum
    • Bolin, J. T., A. E. Ronco, T. V. Morgan, L. E. Mortenson, and N.-H. Xuong. 1993. The unusual metal clusters of nitrogenase: structural features revealed by X-ray anomalous diffraction studies of the MoFe protein from Clostridium pasteurianum. Proc. Natl. Acad. Sci. USA 90:1078-1082.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1078-1082
    • Bolin, J.T.1    Ronco, A.E.2    Morgan, T.V.3    Mortenson, L.E.4    Xuong, N.-H.5
  • 9
    • 0000703950 scopus 로고    scopus 로고
    • Mechanism of molybdenum nitrogenase
    • Burgess, B. K., and D. J. Lowe. 1996. Mechanism of molybdenum nitrogenase. Chem. Rev. 96:2983-3011.
    • (1996) Chem. Rev. , vol.96 , pp. 2983-3011
    • Burgess, B.K.1    Lowe, D.J.2
  • 10
    • 0027159222 scopus 로고
    • The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 Å resolution structures
    • Chan, M. K., J. Kim, and D. C. Rees. 1993. The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 Å resolution structures. Science 260:792-794.
    • (1993) Science , vol.260 , pp. 792-794
    • Chan, M.K.1    Kim, J.2    Rees, D.C.3
  • 11
    • 0030881852 scopus 로고    scopus 로고
    • In vitro synthesis of the iron-molybdenum cofactor and maturation of the nif-encoded apodinitrogenase. Effect of substitution of VNFH for NIFH
    • Chatterjee, R., R. M. Allen, P. W. Ludden, and V. K. Shah. 1997. In vitro synthesis of the iron-molybdenum cofactor and maturation of the nif-encoded apodinitrogenase. Effect of substitution of VNFH for NIFH. J. Biol. Chem. 272:21604-21608.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21604-21608
    • Chatterjee, R.1    Allen, R.M.2    Ludden, P.W.3    Shah, V.K.4
  • 12
    • 0031021946 scopus 로고    scopus 로고
    • Characterization of VNFG, the delta subunit of the vnf-encoded apodinitrogenase from Azotobacter vinelandii. Implications for its role in the formation of functional dinitrogenase 2
    • Chatterjee, R., P. W. Ludden, and V. K. Shah. 1997. Characterization of VNFG, the delta subunit of the vnf-encoded apodinitrogenase from Azotobacter vinelandii. Implications for its role in the formation of functional dinitrogenase 2. J. Biol. Chem. 272:3758-3765.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3758-3765
    • Chatterjee, R.1    Ludden, P.W.2    Shah, V.K.3
  • 13
    • 0023706247 scopus 로고
    • Purification of a second alternative nitrogenase from a nifHDK deletion strain of Azotobacter vinelandii
    • Chisnell, J. R., R. Premakumar, and P. E. Bishop. 1988. Purification of a second alternative nitrogenase from a nifHDK deletion strain of Azotobacter vinelandii. J. Bacteriol. 170:27-33.
    • (1988) J. Bacteriol. , vol.170 , pp. 27-33
    • Chisnell, J.R.1    Premakumar, R.2    Bishop, P.E.3
  • 15
    • 0032497358 scopus 로고    scopus 로고
    • Catalytic and biophysical properties of a nitrogenase Apo-MoFe protein produced by a nifB-deletion mutant of Azotobacter vinelandii
    • Christiansen, J., P. J. Goodwin, W. N. Lanzilotta, L. C. Seefeldt, and D. R. Dean. 1998. Catalytic and biophysical properties of a nitrogenase Apo-MoFe protein produced by a nifB-deletion mutant of Azotobacter vinelandii. Biochemistry 37:12611-12623.
    • (1998) Biochemistry , vol.37 , pp. 12611-12623
    • Christiansen, J.1    Goodwin, P.J.2    Lanzilotta, W.N.3    Seefeldt, L.C.4    Dean, D.R.5
  • 16
    • 3142543276 scopus 로고    scopus 로고
    • Comparison of iron-molybdenum cofactor deficient nitrogenase MoFe proteins by X-ray absorption spectroscopy: Implications for P-cluster biosynthesis
    • Corbett, M. C., Y. Hu, F. Naderi, M. W. Ribbe, B. Hedman, and K. O. Hodgson. 2004. Comparison of iron-molybdenum cofactor deficient nitrogenase MoFe proteins by X-ray absorption spectroscopy: implications for P-cluster biosynthesis. J. Biol. Chem. 279:28276-28282.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28276-28282
    • Corbett, M.C.1    Hu, Y.2    Naderi, F.3    Ribbe, M.W.4    Hedman, B.5    Hodgson, K.O.6
  • 17
    • 0029914814 scopus 로고    scopus 로고
    • Purification and characterization of the alternative nitrogenase from the photosynthetic bacterium Rhodospirillum rubrum
    • Davis, R., L. Lehman, R. Petrovich, V. K. Shah, G. P. Roberts, and P. W. Ludden. 1996. Purification and characterization of the alternative nitrogenase from the photosynthetic bacterium Rhodospirillum rubrum. J. Bacteriol. 178:1445-1450.
    • (1996) J. Bacteriol. , vol.178 , pp. 1445-1450
    • Davis, R.1    Lehman, L.2    Petrovich, R.3    Shah, V.K.4    Roberts, G.P.5    Ludden, P.W.6
  • 18
    • 1542304548 scopus 로고    scopus 로고
    • Formation and insertion of the nitrogenase iron-molybdenum cofactor
    • Dos Santos, P. C., D. R. Dean, Y. Hu, and M. W. Ribbe. 2004. Formation and insertion of the nitrogenase iron-molybdenum cofactor. Chem. Rev. 104:1159-1173.
    • (2004) Chem. Rev. , vol.104 , pp. 1159-1173
    • Dos Santos, P.C.1    Dean, D.R.2    Hu, Y.3    Ribbe, M.W.4
  • 19
    • 2442473182 scopus 로고    scopus 로고
    • Iron-sulfur cluster assembly, NifU-directed activation of the nitrogenase Fe protein
    • Dos Santos, P. C., A. D. Schmid, J. Frazzon, V. L. Cash, M. K. Johnson, and D. R. Dean. 2004. Iron-sulfur cluster assembly, NifU-directed activation of the nitrogenase Fe protein. J. Biol. Chem. 279:19705-19711.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19705-19711
    • Dos Santos, P.C.1    Schmid, A.D.2    Frazzon, J.3    Cash, V.L.4    Johnson, M.K.5    Dean, D.R.6
  • 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, D. H., L. M. Rubio, J. B. Thoden, H. M. Holden, P. W. Ludden, and I. Rayment. 2003. The three-dimensional structure of the core domain of NafY from Azotobacter vinelandii determined at 1.8-A resolution. J. Biol. Chem. 278:32150-32156.
    • (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., F. A. Tezcan, S. L. Andrade, B. Schmid, M. Yoshida, J. B. Howard, and D. C. Rees. 2002. Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor. Science 297:1696-1700.
    • (2002) Science , vol.297 , pp. 1696-1700
    • Einsle, O.1    Tezcan, F.A.2    Andrade, S.L.3    Schmid, B.4    Yoshida, M.5    Howard, J.B.6    Rees, D.C.7
  • 22
    • 0022964472 scopus 로고
    • The nifH gene product is required for the synthesis or stability of the iron-molybdenum cofactor of nitrogenase from Klebsiella pneumoniae
    • Filler, W. A., R. M. Kemp, J. C. Ng, T. R. Hawkes, R. A. Dixon, and B. E. Smith. 1986. The nifH gene product is required for the synthesis or stability of the iron-molybdenum cofactor of nitrogenase from Klebsiella pneumoniae. Eur. J. Biochem. 160:371-377.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 371-377
    • Filler, W.A.1    Kemp, R.M.2    Ng, J.C.3    Hawkes, T.R.4    Dixon, R.A.5    Smith, B.E.6
  • 23
    • 0037397764 scopus 로고    scopus 로고
    • Formation of iron-sulfur clusters in bacteria: An emerging field in bioinorganic chemistry
    • Frazzon, J., and D. R. Dean. 2003. Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry. Curr. Opin. Chem. Biol. 7:166-173.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 166-173
    • Frazzon, J.1    Dean, D.R.2
  • 24
    • 0036670725 scopus 로고    scopus 로고
    • Biosynthesis of iron-sulphur clusters is a complex and highly conserved process
    • Frazzon, J., J. R. Fick, and D. R. Dean. 2002. Biosynthesis of iron-sulphur clusters is a complex and highly conserved process. Biochem. Soc. Trans. 30:680-685.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 680-685
    • Frazzon, J.1    Fick, J.R.2    Dean, D.R.3
  • 25
    • 0027959635 scopus 로고
    • nifU gene product from Azotobacter vinelandii is a homodimer that contains two identical [2Fe-2S] clusters
    • Fu, W., R. F. Jack, T. V. Morgan, D. R. Dean, and M. K. Johnson. 1994. nifU gene product from Azotobacter vinelandii is a homodimer that contains two identical [2Fe-2S] clusters. Biochemistry 33:13455-13463.
    • (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
  • 26
    • 0027943060 scopus 로고
    • Purification and characterization of a FeMo cofactor-deficient MoFe protein
    • Gavini, N., L. Ma, G. Watt, and B. K. Burgess. 1994. Purification and characterization of a FeMo cofactor-deficient MoFe protein. Biochemistry 33:11842-11849.
    • (1994) Biochemistry , vol.33 , pp. 11842-11849
    • Gavini, N.1    Ma, L.2    Watt, G.3    Burgess, B.K.4
  • 28
    • 0026662162 scopus 로고
    • Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii
    • Georgiadis, M. M., H. Komiya, P. Chakrabarti, D. Woo, J. J. Kornuc, and D. C. Rees. 1992. Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Science 257:1653-1659.
    • (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
  • 29
    • 0028287365 scopus 로고
    • Chaperonins as potential gene regulatory factors. In vitro interaction and solubilization of NifA, the nif transcriptional activator, with GroEL
    • Govezensky, D., E. S. Bochkareva, A. Zamir, and A. S. Girshovich. 1994. Chaperonins as potential gene regulatory factors. In vitro interaction and solubilization of NifA, the nif transcriptional activator, with GroEL. J. Biol. Chem. 269:14003-14006.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14003-14006
    • Govezensky, D.1    Bochkareva, E.S.2    Zamir, A.3    Girshovich, A.S.4
  • 30
    • 0025992976 scopus 로고
    • Involvement of GroEL in nif gene regulation and nitrogenase assembly
    • Govezensky, D., T. Greener, G. Segal, and A. Zamir. 1991. Involvement of GroEL in nif gene regulation and nitrogenase assembly. J. Bacteriol. 173: 6339-6346.
    • (1991) J. Bacteriol. , vol.173 , pp. 6339-6346
    • Govezensky, D.1    Greener, T.2    Segal, G.3    Zamir, A.4
  • 31
    • 0040412793 scopus 로고
    • Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle
    • Hageman, R. V., and R. H. Burris. 1978. Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle. Proc. Natl. Acad. Sci. USA 75:2699-2702.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 2699-2702
    • Hageman, R.V.1    Burris, R.H.2
  • 32
    • 0020679403 scopus 로고
    • Purification and characterization of the inactive MoFe protein (MfB-Kpl) of the nitrogenase from nifB mutants of Klebsiella pneumoniae
    • Hawkes, T. R., and B. E. Smith. 1983. Purification and characterization of the inactive MoFe protein (MfB-Kpl) of the nitrogenase from nifB mutants of Klebsiella pneumoniae. Biochem. J. 209:43-50.
    • (1983) Biochem. J. , vol.209 , pp. 43-50
    • Hawkes, T.R.1    Smith, B.E.2
  • 33
    • 0028792366 scopus 로고
    • Characterization of the gamma protein and its involvement in the metallocluster assembly and maturation of dinitrogenase from Azotobacter vinelandii
    • Homer, M. J., D. R. Dean, and G. P. Roberts. 1995. Characterization of the gamma protein and its involvement in the metallocluster assembly and maturation of dinitrogenase from Azotobacter vinelandii. J. Biol. Chem. 270: 24745-24752.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24745-24752
    • Homer, M.J.1    Dean, D.R.2    Roberts, G.P.3
  • 34
    • 0027296628 scopus 로고
    • The nifY product of Klebsiella pneumoniae is associated with apodinitrogenase and dissociates upon activation with the iron-molybdenum cofactor
    • Homer, M. J., T. D. Paustian, V. K. Shah, and G. P. Roberts. 1993. The nifY product of Klebsiella pneumoniae is associated with apodinitrogenase and dissociates upon activation with the iron-molybdenum cofactor. J. Bacteriol. 175:4907-4910.
    • (1993) J. Bacteriol. , vol.175 , pp. 4907-4910
    • Homer, M.J.1    Paustian, T.D.2    Shah, V.K.3    Roberts, G.P.4
  • 35
    • 0022607892 scopus 로고
    • The Klebsiella pneumoniae nifM gene product is required for stabilization and activation of nitrogenase iron protein in Escherichia coli
    • Howard, K. S., P. A. McLean, F. B. Hansen, P. V. Lemley, K. S. Koblan, and W. H. Orme-Johnson. 1986. The Klebsiella pneumoniae nifM gene product is required for stabilization and activation of nitrogenase iron protein in Escherichia coli. J. Biol. Chem. 261:772-778.
    • (1986) J. Biol. Chem. , vol.261 , pp. 772-778
    • Howard, K.S.1    McLean, P.A.2    Hansen, F.B.3    Lemley, P.V.4    Koblan, K.S.5    Orme-Johnson, W.H.6
  • 38
    • 0024743814 scopus 로고
    • Biochemical and genetic analysis of the nifUSVWZM cluster from Azotobacter vinelandii
    • Jacobson, M. R., V. L. Cash, M. C. Weiss, N. F. Laird, W. E. Newton, and D. R. Dean. 1989. Biochemical and genetic analysis of the nifUSVWZM cluster from Azotobacter vinelandii. Mol. Gen. Genet. 219:49-57.
    • (1989) Mol. Gen. Genet. , vol.219 , pp. 49-57
    • Jacobson, M.R.1    Cash, V.L.2    Weiss, M.C.3    Laird, N.F.4    Newton, W.E.5    Dean, D.R.6
  • 39
    • 0025369091 scopus 로고
    • Nucleotide sequences and mutational analysis of the structural genes for nitrogenase 2 of Azotobacter vinelandii
    • Joerger, R. D., T. M. Loveless, R. N. Pau, L. A. Mitchenall, B. H. Simon, and P. E. Bishop. 1990. Nucleotide sequences and mutational analysis of the structural genes for nitrogenase 2 of Azotobacter vinelandii. J. Bacteriol. 172:3400-3408.
    • (1990) J. Bacteriol. , vol.172 , pp. 3400-3408
    • Joerger, R.D.1    Loveless, T.M.2    Pau, R.N.3    Mitchenall, L.A.4    Simon, B.H.5    Bishop, P.E.6
  • 40
    • 0026548467 scopus 로고
    • The nifU, nifS and nifV Kgene products are required for activity of all three nitrogenases of Azotobacter vinelandii
    • Kennedy, C., and D. Dean. 1992. The nifU, nifS and nifV Kgene products are required for activity of all three nitrogenases of Azotobacter vinelandii. Mol. Gen. Genet. 231:494-498.
    • (1992) Mol. Gen. Genet. , vol.231 , pp. 494-498
    • Kennedy, C.1    Dean, D.2
  • 41
    • 0022870670 scopus 로고
    • The nifH, nifM and nifN genes of Azotobacter vinelandii. Characterization by Tn5 mutagenesis and isolation from pLAFR1 gene banks
    • Kennedy, C., R. Gamal, R. Humphrey, J. Ramos, K. Brigle, and D. Dean. 1986. The nifH, nifM and nifN genes of Azotobacter vinelandii. Characterization by Tn5 mutagenesis and isolation from pLAFR1 gene banks. Mol. Gen. Genet. 205:318-325.
    • (1986) Mol. Gen. Genet. , vol.205 , pp. 318-325
    • Kennedy, C.1    Gamal, R.2    Humphrey, R.3    Ramos, J.4    Brigle, K.5    Dean, D.6
  • 42
    • 0024422619 scopus 로고
    • Site-directed mutagenesis of the Klebsiella pneumoniae nitrogenase. Effects of modifying conserved cysteine residues in the α and β-subunits
    • Kent, H. M., I. Ioannidis, C. Gormal, B. E. Smith, and M. Buck. 1989. Site-directed mutagenesis of the Klebsiella pneumoniae nitrogenase. Effects of modifying conserved cysteine residues in the α and β-subunits. Biochem. J. 264:257-264.
    • (1989) Biochem. J. , vol.264 , pp. 257-264
    • Kent, H.M.1    Ioannidis, I.2    Gormal, C.3    Smith, B.E.4    Buck, M.5
  • 43
    • 0026734002 scopus 로고
    • Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii
    • Kim, J., and D. C. Rees. 1992. Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii. Nature (London) 360:553-560.
    • (1992) Nature (London) , vol.360 , pp. 553-560
    • Kim, J.1    Rees, D.C.2
  • 44
    • 0026705527 scopus 로고
    • Structural models for the metal centers in the nitrogenase molybdenum-iron protein
    • Kim, J., and D. C. Rees. 1992. Structural models for the metal centers in the nitrogenase molybdenum-iron protein. Science 257:1677-1682.
    • (1992) Science , vol.257 , pp. 1677-1682
    • Kim, J.1    Rees, D.C.2
  • 45
    • 0027222119 scopus 로고
    • X-ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0-A resolution
    • Kim, J., D. Woo, and D. C. Rees. 1993. X-ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0-A resolution. Biochemistry 32:7104-7115.
    • (1993) Biochemistry , vol.32 , pp. 7104-7115
    • Kim, J.1    Woo, D.2    Rees, D.C.3
  • 46
    • 0028146634 scopus 로고
    • Purification and characterization of nitrogenase from a ΔnifW strain of Azotobacter vinelandii
    • Kim, S., and B. K. Burgess. 1994. Purification and characterization of nitrogenase from a ΔnifW strain of Azotobacter vinelandii. J. Biol. Chem. 269:4215-4220.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4215-4220
    • Kim, S.1    Burgess, B.K.2
  • 47
    • 0032539750 scopus 로고    scopus 로고
    • Genetic analysis on the NifW by utilizing the yeast two-hybrid system revealed that the NifW of Azotobacter vinelandii interacts with the NifZ to form higher-order complexes
    • Lee, S. H., L. Pulakat, K. C. Parker, and N. Gavini. 1998. Genetic analysis on the NifW by utilizing the yeast two-hybrid system revealed that the NifW of Azotobacter vinelandii interacts with the NifZ to form higher-order complexes. Biochem. Biophys. Res. Commun. 244:498-504.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 498-504
    • Lee, S.H.1    Pulakat, L.2    Parker, K.C.3    Gavini, N.4
  • 48
    • 11844251701 scopus 로고    scopus 로고
    • Biosynthesis of the iron-molybdenum and iron-vanadium cofactors of the nif- and vnf-encoded nitrogenases
    • B. E. Smith, R. L. Richards, and W. E. Newton (ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Ludden, P. W., P. Rangaraj, and L. M. Rubio. 2004. Biosynthesis of the iron-molybdenum and iron-vanadium cofactors of the nif- and vnf-encoded nitrogenases, p. 219-253. In B. E. Smith, R. L. Richards, and W. E. Newton (ed.), Catalysts for nitrogen fixation: nitrogenases, relevant chemical models and commercial processes. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (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
  • 49
    • 0030764543 scopus 로고    scopus 로고
    • Nitrogenase iron-molybdenum cofactor binding site: Protein conformational changes associated with cofactor binding
    • Magnuson, J. K., T. D. Paustian, V. K. Shah, D. R. Dean, G. P. Roberts, D. C. Rees, and J. B. Howard. 1997. Nitrogenase iron-molybdenum cofactor binding site: protein conformational changes associated with cofactor binding. Tetrahedron 53:11971-11984.
    • (1997) Tetrahedron , vol.53 , pp. 11971-11984
    • Magnuson, J.K.1    Paustian, T.D.2    Shah, V.K.3    Dean, D.R.4    Roberts, G.P.5    Rees, D.C.6    Howard, J.B.7
  • 50
    • 0027152184 scopus 로고
    • Nucleotide sequence and genetic analysis of the Rhodobacter capsulatus ORF6-nifUISVW gene region: Possible role of NifW in homocitrate processing
    • Masepohl, B., S. Angermuller, S. Hennecke, P. Hubner, C Moreno-Vivián, and W. Klipp. 1993. Nucleotide sequence and genetic analysis of the Rhodobacter capsulatus ORF6-nifUISVW gene region: possible role of NifW in homocitrate processing. Mol. Gen. Genet. 238:369-382.
    • (1993) Mol. Gen. Genet. , vol.238 , pp. 369-382
    • Masepohl, B.1    Angermuller, S.2    Hennecke, S.3    Hubner, P.4    Moreno-Vivián, C.5    Klipp, W.6
  • 52
    • 0033215327 scopus 로고    scopus 로고
    • New insights into structure-function relationships in nitrogenase: A 1.6 A resolution X-ray crystallographic study of Klebsiella pneumoniae MoFe-protein
    • Mayer, S. M., D. M. Lawson, C. A. Gormal, S. M. Roe, and B. E. Smith. 1999. New insights into structure-function relationships in nitrogenase: a 1.6 A resolution X-ray crystallographic study of Klebsiella pneumoniae MoFe-protein. J. Mol. Biol. 292:871-891.
    • (1999) J. Mol. Biol. , vol.292 , pp. 871-891
    • Mayer, S.M.1    Lawson, D.M.2    Gormal, C.A.3    Roe, S.M.4    Smith, B.E.5
  • 53
    • 0024586983 scopus 로고
    • The roles of the nifW, nifZ and nifM genes of Klebsiella pneumoniae in nitrogenase biosynthesis
    • Paul, W., and M. Merrick. 1989. The roles of the nifW, nifZ and nifM genes of Klebsiella pneumoniae in nitrogenase biosynthesis. Eur. J. Biochem. 178:675-682.
    • (1989) Eur. J. Biochem. , vol.178 , pp. 675-682
    • Paul, W.1    Merrick, M.2
  • 54
    • 0025254057 scopus 로고
    • Apodinitrogenase: Purification, association with a 20-kilodalton protein, and activation by the iron-molybdenum cofactor in the absence of dinitrogenase reductase
    • Paustian, T. D., V. K. Shah, and G. P. Roberts. 1990. Apodinitrogenase: purification, association with a 20-kilodalton protein, and activation by the iron-molybdenum cofactor in the absence of dinitrogenase reductase. Biochemistry 29:3515-3522.
    • (1990) Biochemistry , vol.29 , pp. 3515-3522
    • Paustian, T.D.1    Shah, V.K.2    Roberts, G.P.3
  • 55
    • 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. 276:15968-15974.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15968-15974
    • Rangaraj, P.1    Rüttimann-Johnson, C.2    Shah, V.K.3    Ludden, P.W.4
  • 56
    • 0002915659 scopus 로고    scopus 로고
    • Biosynthesis of the iron-molybdenum and iron-vanadium cofactors of the nif- And vnf-encoded nitrogenases
    • E. W. Triplett (ed.), Horizon Scientific Press, Wymondham, United Kingdom
    • Rangaraj, P., C. Rüttimann-Johnson, V. K. Shah, and P. W. Ludden. 2000. Biosynthesis of the iron-molybdenum and iron-vanadium cofactors of the nif- and vnf-encoded nitrogenases, p. 55-79. In E. W. Triplett (ed.), Prokaryotic nitrogen fixation: a model system for analysis of a biochemical process. Horizon Scientific Press, Wymondham, United Kingdom.
    • (2000) Prokaryotic Nitrogen Fixation: A Model System for Analysis of a Biochemical Process , pp. 55-79
    • Rangaraj, P.1    Rüttimann-Johnson, C.2    Shah, V.K.3    Ludden, P.W.4
  • 57
    • 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., M. J. Ryle, W. N. Lanzilotta, P. W. Ludden, and V. K. Shah. 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. 274:19778-19784.
    • (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
  • 58
    • 0030826663 scopus 로고    scopus 로고
    • ApoNifH functions in iron-molybdenum cofactor synthesis and apodinitrogenase maturation
    • Rangaraj, P., V. K. Shah, and P. W. Ludden. 1997. ApoNifH functions in iron-molybdenum cofactor synthesis and apodinitrogenase maturation. Proc. Natl. Acad. Sci. USA 94:11250-11255.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11250-11255
    • Rangaraj, P.1    Shah, V.K.2    Ludden, P.W.3
  • 60
    • 0035826893 scopus 로고    scopus 로고
    • The chaperone GroEL is required for the final assembly of the molybdenum-iron protein of nitrogenase
    • Ribbe, M. W., and B. K. Burgess. 2001. The chaperone GroEL is required for the final assembly of the molybdenum-iron protein of nitrogenase. Proc. Natl. Acad. Sci. USA 98:5521-5525.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5521-5525
    • Ribbe, M.W.1    Burgess, B.K.2
  • 61
    • 0034625445 scopus 로고    scopus 로고
    • Identification of an Fe protein residue (Glu146) of Azotobacter vinelandii nitrogenase that is specifically involved in FeMo cofactor insertion
    • Ribbe, M. W., E. H. Bursey, and B. K. Burgess. 2000. Identification of an Fe protein residue (Glu146) of Azotobacter vinelandii nitrogenase that is specifically involved in FeMo cofactor insertion. J. Biol. Chem. 275:17631-17638.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17631-17638
    • Ribbe, M.W.1    Bursey, E.H.2    Burgess, B.K.3
  • 62
    • 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, M. W., Y. Hu, M. Guo, B. Schmid, and B. K. Burgess. 2002. The FeMoco-deficient MoFe protein produced by a nifH deletion strain of Azotobacter vinelandii shows unusual P-cluster features. J. Biol. Chem. 277:23469-23476.
    • (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
  • 63
    • 0018167549 scopus 로고
    • Regulation and characterization of protein products coded by the nif (nitrogen fixation) genes of Klebsiella pneumoniae
    • Roberts, G. P., T. MacNeil, D. MacNeil, and W. J. Brill. 1978. Regulation and characterization of protein products coded by the nif (nitrogen fixation) genes of Klebsiella pneumoniae. J. Bacteriol. 136:267-279.
    • (1978) J. Bacteriol. , vol.136 , pp. 267-279
    • Roberts, G.P.1    MacNeil, T.2    MacNeil, D.3    Brill, W.J.4
  • 64
    • 0022517403 scopus 로고
    • Activity, reconstitution, and accumulation of nitrogenase components in Azotobacter vinelandii mutant strains containing defined deletions within the nitrogenase structural gene cluster
    • Robinson, A. C., B. K. Burgess, and D. R. Dean. 1986. Activity, reconstitution, and accumulation of nitrogenase components in Azotobacter vinelandii mutant strains containing defined deletions within the nitrogenase structural gene cluster. J. Bacteriol. 166:180-186.
    • (1986) J. Bacteriol. , vol.166 , pp. 180-186
    • Robinson, A.C.1    Burgess, B.K.2    Dean, D.R.3
  • 65
    • 0024356199 scopus 로고
    • Iron-molybdenum cofactor insertion into the ApO-MoFe protein of nitrogenase involves the iron protein-MgATP complex
    • Robinson, A. C., T. W. Chun, J. G. Li, and B. K. Burgess. 1989. Iron-molybdenum cofactor insertion into the ApO-MoFe protein of nitrogenase involves the iron protein-MgATP complex. J. Biol. Chem. 264:10088-10095.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10088-10095
    • Robinson, A.C.1    Chun, T.W.2    Li, J.G.3    Burgess, B.K.4
  • 67
    • 0042898981 scopus 로고    scopus 로고
    • The gene products of the nif regulon
    • G. J. Leigh (ed.), Elsevier, Amsterdam, The Netherlands
    • Rubio, L. M., and P. W. Ludden. 2002. The gene products of the nif regulon, p. 101-136. In G. J. Leigh (ed.), Nitrogen fixation at the millenium. Elsevier, Amsterdam, The Netherlands.
    • (2002) Nitrogen Fixation at the Millenium , pp. 101-136
    • Rubio, L.M.1    Ludden, P.W.2
  • 68
    • 0037134499 scopus 로고    scopus 로고
    • Cloning and mutational analysis of the gamma gene from Azotobacter vinelandii defines a new family of proteins capable of metallocluster binding and protein stabilization
    • Rubio, L. M., P. Rangaraj, M. J. Homer, G. P. Roberts, and P. W. Ludden. 2002. Cloning and mutational analysis of the gamma gene from Azotobacter vinelandii defines a new family of proteins capable of metallocluster binding and protein stabilization. J. Biol. Chem. 277:14299-14305.
    • (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
  • 69
    • 2442425301 scopus 로고    scopus 로고
    • Purification and characterization of NafY (apodinitrogenase gamma subunit) from Azotobacter vinelandii
    • Rubio, L. M., S. W. Singer, and P. W. Ludden. 2004. Purification and characterization of NafY (apodinitrogenase gamma subunit) from Azotobacter vinelandii. J. Biol. Chem. 279:19739-19746.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19739-19746
    • Rubio, L.M.1    Singer, S.W.2    Ludden, P.W.3
  • 70
    • 0037377874 scopus 로고    scopus 로고
    • VnfY is required for full activity of the vanadium-containing dinitrogenase in Azotobacter vinelandii
    • Ruttimann-Johnson, C., L. M. Rubio, D. R. Dean, and P. W. Ludden. 2003. VnfY is required for full activity of the vanadium-containing dinitrogenase in Azotobacter vinelandii. J. Bacteriol. 185:2383-2386.
    • (2003) J. Bacteriol. , vol.185 , pp. 2383-2386
    • Ruttimann-Johnson, C.1    Rubio, L.M.2    Dean, D.R.3    Ludden, P.W.4
  • 71
    • 0040962336 scopus 로고    scopus 로고
    • A vanadium and iron cluster accumulates on VnfX during iron-vanadium-cofactor synthesis for the vanadium nitrogenase in Azotobacter vinelandii
    • Rüttimann-Johnson, C., C. R. Staples, P. Rangaraj, V. K. Shah, and P. W. Ludden. 1999. A vanadium and iron cluster accumulates on VnfX during iron-vanadium-cofactor synthesis for the vanadium nitrogenase in Azotobacter vinelandii. J. Biol. Chem. 274:18087-18092.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18087-18092
    • Rüttimann-Johnson, C.1    Staples, C.R.2    Rangaraj, P.3    Shah, V.K.4    Ludden, P.W.5
  • 73
    • 0026063694 scopus 로고
    • Demonstration of a molybdenum- and vanadium-independent nitrogenase in a nifHDK-deletion mutant of Rhodobacter capsulatus
    • Schneider, K., A. Muller, U. Schramm, and W. Klipp. 1991. Demonstration of a molybdenum- and vanadium-independent nitrogenase in a nifHDK-deletion mutant of Rhodobacter capsulatus. Eur. J. Biochem. 195:653-661.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 653-661
    • Schneider, K.1    Muller, A.2    Schramm, U.3    Klipp, W.4
  • 74
    • 0015833602 scopus 로고
    • Nitrogenase. IV. Simple method of purification to homogeneity of nitrogenase components from Azotobacter vinelandii
    • Shah, V. K., and W. J. Brill. 1973. Nitrogenase. IV. Simple method of purification to homogeneity of nitrogenase components from Azotobacter vinelandii. Biochim. Biophys. Acta 305:445-454.
    • (1973) Biochim. Biophys. Acta , vol.305 , pp. 445-454
    • Shah, V.K.1    Brill, W.J.2
  • 75
    • 0025914460 scopus 로고
    • The ΔnifB (or ΔnifE) FeMo cofactor-deficient MoFe protein is different from the ΔnifH protein
    • Tal, S., T. W. Chun, N. Gavini, and B. K. Burgess. 1991. The ΔnifB (or ΔnifE) FeMo cofactor-deficient MoFe protein is different from the ΔnifH protein. J. Biol. Chem. 266:10654-10657.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10654-10657
    • Tal, S.1    Chun, T.W.2    Gavini, N.3    Burgess, B.K.4
  • 76
    • 0027495919 scopus 로고
    • Characterization of genes for an alternative nitrogenase in the cyanobacterium Anabaena variabilis
    • Thiel, T. 1993. Characterization of genes for an alternative nitrogenase in the cyanobacterium Anabaena variabilis. J. Bacteriol. 175:6276-6286.
    • (1993) J. Bacteriol. , vol.175 , pp. 6276-6286
    • Thiel, T.1
  • 77
    • 0021218602 scopus 로고
    • Biosynthesis of iron-molybdenum cofactor in the absence of nitrogenase
    • Ugalde, R. A., J. Imperial, V. K. Shah, and W. J. Brill. 1984. Biosynthesis of iron-molybdenum cofactor in the absence of nitrogenase. J. Bacteriol. 159:888-893.
    • (1984) J. Bacteriol. , vol.159 , pp. 888-893
    • Ugalde, R.A.1    Imperial, J.2    Shah, V.K.3    Brill, W.J.4
  • 78
    • 0027082786 scopus 로고
    • Electrophoretic studies on the assembly of the nitrogenase molybdenum-iron protein from the Kiebsiella pneumoniae nifD and nifK gene products
    • White, T. C., G. S. Harris, and W. H. Orme-Johnson. 1992. Electrophoretic studies on the assembly of the nitrogenase molybdenum-iron protein from the Kiebsiella pneumoniae nifD and nifK gene products. J. Biol. Chem. 267:24007-24016.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24007-24016
    • White, T.C.1    Harris, G.S.2    Orme-Johnson, W.H.3
  • 79
    • 0001975986 scopus 로고
    • Phylogenetic classification of nitrogen-fixing organisms
    • G. Stacey, R. H. Burris, and H. J. Evans (ed.), Chapman and Hall, New York, N.Y.
    • Young, J. P. W. 1992. Phylogenetic classification of nitrogen-fixing organisms, p. 43-86. In G. Stacey, R. H. Burris, and H. J. Evans (ed.), Biological nitrogen fixation. Chapman and Hall, New York, N.Y.
    • (1992) Biological Nitrogen Fixation , pp. 43-86
    • Young, J.P.W.1
  • 81
    • 0028339794 scopus 로고
    • Catalytic formation of a nitrogenase iron-sulfur cluster
    • Zheng, L., and D. R. Dean. 1994. Catalytic formation of a nitrogenase iron-sulfur cluster. J. Biol. Chem. 269:18723-18726.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18723-18726
    • Zheng, L.1    Dean, D.R.2
  • 82
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for N1FS in metallocluster biosynthesis
    • Zheng, L., R. H. White, V. L. Cash, R. F. Jack, and D. R. Dean. 1993. Cysteine desulfurase activity indicates a role for N1FS in metallocluster biosynthesis. Proc. Natl. Acad. Sci. USA 90:2754-2758.
    • (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


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