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Volumn 41, Issue 47, 2002, Pages 13934-13945

An atomic-level mechanism for molybdenum nitrogenase. Part 1. Reduction of dinitrogen

Author keywords

[No Author keywords available]

Indexed keywords

DENSITY FUNCTIONAL THEORY (DFT);

EID: 0037180372     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi025623z     Document Type: Article
Times cited : (75)

References (60)
  • 1
    • 0001219252 scopus 로고    scopus 로고
    • Structure-function relationships of alternative nitrogenases
    • Eady, R. R. (1996) Structure-function relationships of alternative nitrogenases, Chem. Rev. 96, 3013-3030.
    • (1996) Chem. Rev. , vol.96 , pp. 3013-3030
    • Eady, R.R.1
  • 2
    • 7744224797 scopus 로고    scopus 로고
    • Structural basis of biological nitrogen fixation
    • Howard, J. B., and Rees, D. C. (1996) Structural basis of biological nitrogen fixation, Chem. Rev. 96, 2965-2982.
    • (1996) Chem. Rev. , vol.96 , pp. 2965-2982
    • Howard, J.B.1    Rees, D.C.2
  • 3
    • 0000703950 scopus 로고    scopus 로고
    • Mechanism of molybdenum nitrogenase
    • Burgess, B. K., and Lowe, D. J. (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
  • 8
    • 0034671711 scopus 로고    scopus 로고
    • Evidence for a two-electron transfer using the all-ferrous Fe protein during nitrogenase catalysis
    • Nyborg, A. C., Johnson, J. L., Gunn, A., and Watt, G. D. (2000) Evidence for a two-electron transfer using the all-ferrous Fe protein during nitrogenase catalysis, J. Biol. Chem. 275, 39307-39312.
    • (2000) J. Biol. Chem. , vol.275 , pp. 39307-39312
    • Nyborg, A.C.1    Johnson, J.L.2    Gunn, A.3    Watt, G.D.4
  • 9
    • 0021757851 scopus 로고
    • A nitrogen pressure of 50 atm does not prevent evolution of hydrogen by nitrogenase
    • Simpson, F. B., and Burris, R. H. (1984) A nitrogen pressure of 50 atm does not prevent evolution of hydrogen by nitrogenase, Science 224, 1095-1097.
    • (1984) Science , vol.224 , pp. 1095-1097
    • Simpson, F.B.1    Burris, R.H.2
  • 10
    • 3042990613 scopus 로고    scopus 로고
    • The Chatt cycle and the mechanism of enzymic reduction of molecular nitrogen
    • Pickett, C. J. (1996) The Chatt cycle and the mechanism of enzymic reduction of molecular nitrogen, J. Biol. Inorg. Chem. 1, 601-606.
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 601-606
    • Pickett, C.J.1
  • 11
    • 0031037279 scopus 로고    scopus 로고
    • Redox-dependent structural changes in the nitrogenase P-cluster
    • and references therein
    • Peters, J. W., Stowell, M. H. B., Soltis, S. M., Finnegan, M. G., Johnson, M. K., and Rees, D. C. (1997) Redox-dependent structural changes in the nitrogenase P-cluster, Biochemistry 36, 1181-1187 and references therein.
    • (1997) Biochemistry , vol.36 , pp. 1181-1187
    • Peters, J.W.1    Stowell, M.H.B.2    Soltis, S.M.3    Finnegan, M.G.4    Johnson, M.K.5    Rees, D.C.6
  • 13
    • 0033215327 scopus 로고    scopus 로고
    • New insights into structure-function relationships in nitrogenase: A 1.6 Å resolution X-ray crystallographic study of Klebsiella pneumoniae MoFe-protein
    • Mayer, S. M., Lawson, D. M., Gormal, C. A., Roe, S. M., and Smith, B. E. (1999) New insights into structure-function relationships in nitrogenase: A 1.6 Å 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
  • 15
    • 0035183071 scopus 로고    scopus 로고
    • A molybdenum-centred model for nitrogenase catalysis
    • Durrant, M. C. (2001) A molybdenum-centred model for nitrogenase catalysis, Inorg. Chem. Commun. 4, 60-62.
    • (2001) Inorg. Chem. Commun. , vol.4 , pp. 60-62
    • Durrant, M.C.1
  • 16
    • 0035847467 scopus 로고    scopus 로고
    • Theoretical studies of biological nitrogen fixation. I. Density functional modeling of the Mo-site of the FeMo-cofactor
    • Szilagyi, R. K., Musaev, D. G., and Morokuma, K. (2001) Theoretical studies of biological nitrogen fixation. I. Density functional modeling of the Mo-site of the FeMo-cofactor, Inorg. Chem. 40, 766-775.
    • (2001) Inorg. Chem. , vol.40 , pp. 766-775
    • Szilagyi, R.K.1    Musaev, D.G.2    Morokuma, K.3
  • 20
    • 0021764818 scopus 로고
    • 2-evolution rate on component-protein concentration and ratio and sodium dithionite concentration
    • 2-evolution rate on component-protein concentration and ratio and sodium dithionite concentration, Biochem. J. 224, 903-909.
    • (1984) Biochem. J. , vol.224 , pp. 903-909
    • Thorneley, R.N.F.1    Lowe, D.J.2
  • 21
    • 0028791920 scopus 로고
    • Nitrogenase structure and function: A biochemical-genetic perspective
    • Peters, J. W., Fisher, K., and Dean, D. R. (1995) Nitrogenase structure and function: A biochemical-genetic perspective, Annu. Rev. Microbiol. 49, 335-366.
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 335-366
    • Peters, J.W.1    Fisher, K.2    Dean, D.R.3
  • 22
    • 0000264798 scopus 로고    scopus 로고
    • 3 at the FeMo cluster of nitrogenase
    • 3 at the FeMo cluster of nitrogenase, Chem. Commun. 165-166.
    • (1997) Chem. Commun. , pp. 165-166
    • Dance, I.1
  • 24
    • 0034722944 scopus 로고    scopus 로고
    • Modeling the nitrogenase FeMo cofactor
    • Rod, T. H., and Nørskov, J. K. (2000) Modeling the nitrogenase FeMo cofactor, J. Am. Chem. Soc. 122, 12751-12763.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12751-12763
    • Rod, T.H.1    Nørskov, J.K.2
  • 25
    • 0025059442 scopus 로고
    • Diastereomer-dependent substrate reduction properties of a dinitrogenase containing 1-fluorohomocitrate in the iron-molybdenum cofactor
    • Madden, M. S., Kindon, N. D., Ludden, P. W., and Shah, V. K. (1990) Diastereomer-dependent substrate reduction properties of a dinitrogenase containing 1-fluorohomocitrate in the iron-molybdenum cofactor, Proc. Natl. Acad. Sci. U.S.A. 87, 6517-6521.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 6517-6521
    • Madden, M.S.1    Kindon, N.D.2    Ludden, P.W.3    Shah, V.K.4
  • 26
    • 0024290396 scopus 로고
    • Dinitrogenase with altered substrate specificity results from the use of homocitrate analogues for in vitro synthesis of the iron-molybdenum cofactor
    • Hoover, T. R., Imperial, J., Liang, J., Ludden, P. W., and Shah, V. K. (1988) Dinitrogenase with altered substrate specificity results from the use of homocitrate analogues for in vitro synthesis of the iron-molybdenum cofactor, Biochemistry 27, 3647-3652.
    • (1988) Biochemistry , vol.27 , pp. 3647-3652
    • Hoover, T.R.1    Imperial, J.2    Liang, J.3    Ludden, P.W.4    Shah, V.K.5
  • 27
    • 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, T. R., Madden, M. S., Ludden, P. W., and Shah, V. K. (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, 7796-7799.
    • (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
  • 28
    • 0035340589 scopus 로고    scopus 로고
    • Controlled protonation of iron-molybdenum cofactor by nitrogenase: A structural and theoretical analysis
    • Durrant, M. C. (2001) Controlled protonation of iron-molybdenum cofactor by nitrogenase: A structural and theoretical analysis, Biochem. J. 355, 569-576.
    • (2001) Biochem. J. , vol.355 , pp. 569-576
    • Durrant, M.C.1
  • 29
    • 0003996924 scopus 로고    scopus 로고
    • Oxford Molecular Ltd., Oxford
    • Chem-X. Version 1999.2 (1999) Oxford Molecular Ltd., Oxford.
    • (1999) Chem-X. Version 1999.2
  • 32
    • 0004294029 scopus 로고
    • Glaxo Research and Development, Greenford, U.K.
    • Sayle, R. (1993-1995) RasMol, Version 2.4, Glaxo Research and Development, Greenford, U.K.
    • (1993) RasMol, Version 2.4
    • Sayle, R.1
  • 33
    • 37049087710 scopus 로고
    • Bis[1,2-bis(dimethylphosphino)ethane]-dihydrogenhydridoiron(II) tetraphenylborate as a model for the function of nitrogenases
    • Hills, A., Hughes, D. L., Jimenez-Tenorio, M., Leigh, G. J., and Rowley, A. T. (1993) Bis[1,2-bis(dimethylphosphino)ethane]-dihydrogenhydridoiron(II) tetraphenylborate as a model for the function of nitrogenases, J. Chem. Soc., Dalton Trans. 3041-3049.
    • (1993) J. Chem. Soc., Dalton Trans. , pp. 3041-3049
    • Hills, A.1    Hughes, D.L.2    Jimenez-Tenorio, M.3    Leigh, G.J.4    Rowley, A.T.5
  • 35
    • 0028384694 scopus 로고
    • EXAFS studies of FeMo-cofactor and MoFe protein: Direct evidence for the long-range Mo-Fe-Fe interaction and cyanide binding to the Mo in FeMo-cofactor
    • Liu, H. I., Filipponi, A., Gavini, N., Burgess, B. K., Hedman, B., Di Cicco, A., Natoli, C. R., and Hodgson, K. O. (1994) EXAFS studies of FeMo-cofactor and MoFe protein: Direct evidence for the long-range Mo-Fe-Fe interaction and cyanide binding to the Mo in FeMo-cofactor, J. Am. Chem. Soc. 116, 2418-2423.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 2418-2423
    • Liu, H.I.1    Filipponi, A.2    Gavini, N.3    Burgess, B.K.4    Hedman, B.5    Di Cicco, A.6    Natoli, C.R.7    Hodgson, K.O.8
  • 37
    • 37049091512 scopus 로고
    • Molybdenum-(VI) complexes with malic acid: Their inter-relationships, and the crystal structure of dicaesium bis[(S)-malato(2-)cis-dioxomolybdate(VI)-water (1/1)
    • Knobler, C. B., Wilson, A. J., Hider, R. N., Jensen, I. W., Penfold, B. R., Robinson, W. T., and Wilkins, C. J. (1983) Molybdenum-(VI) complexes with malic acid: Their inter-relationships, and the crystal structure of dicaesium bis[(S)-malato(2-)cis-dioxomolybdate(VI)-water (1/1), J. Chem. Soc., Dalton Trans. 1299-1303.
    • (1983) J. Chem. Soc., Dalton Trans. , pp. 1299-1303
    • Knobler, C.B.1    Wilson, A.J.2    Hider, R.N.3    Jensen, I.W.4    Penfold, B.R.5    Robinson, W.T.6    Wilkins, C.J.7
  • 38
    • 0001518448 scopus 로고    scopus 로고
    • Reductive cleavage and related reactions leading to molybdenum-element multiple bonds: New pathways offered by three-coordinate molybdenum(III)
    • Cummins, C. C. (1998) Reductive cleavage and related reactions leading to molybdenum-element multiple bonds: New pathways offered by three-coordinate molybdenum(III), Chem. Commun. 1777-1786.
    • (1998) Chem. Commun. , pp. 1777-1786
    • Cummins, C.C.1
  • 42
    • 0000061312 scopus 로고
    • Diamagnetic (pentamethylcyclopentadienyl)tungsten complexes containing unsubstituted, monomethyl, or 1,1-dimethyl hydrazine or hydrazido ligands
    • Glassman, T. E., Vale, M. G., and Schrock, R. R. (1992) Diamagnetic (pentamethylcyclopentadienyl)tungsten complexes containing unsubstituted, monomethyl, or 1,1-dimethyl hydrazine or hydrazido ligands, J. Am. Chem. Soc. 114, 8098-8109.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 8098-8109
    • Glassman, T.E.1    Vale, M.G.2    Schrock, R.R.3
  • 44
    • 2242420463 scopus 로고    scopus 로고
    • unpublished work
    • Durrant, M. C., (2001) unpublished work.
    • (2001)
    • Durrant, M.C.1
  • 46
    • 0033532120 scopus 로고    scopus 로고
    • The isolated iron-molybdenum cofactor of nitrogenase catalyses hydrogen evolution at high potential
    • Le Gall, T., Ibrahim, S. K., Gormal, C. A., Smith, B. E., and Pickett, C. J. (1999) The isolated iron-molybdenum cofactor of nitrogenase catalyses hydrogen evolution at high potential, Chem. Commun. 773-774.
    • (1999) Chem. Commun. , pp. 773-774
    • Le Gall, T.1    Ibrahim, S.K.2    Gormal, C.A.3    Smith, B.E.4    Pickett, C.J.5
  • 49
    • 0033532683 scopus 로고    scopus 로고
    • The isolated iron-molybdenum cofactor of nitrogenase binds carbon monoxide upon electrochemically accessing reduced states
    • Ibrahim, S. K., Vincent, K., Gormal, C. A., Smith, B. E., Best, S. P., and Pickett, C. J. (1999) The isolated iron-molybdenum cofactor of nitrogenase binds carbon monoxide upon electrochemically accessing reduced states, Chem. Commun. 1019-1020.
    • (1999) Chem. Commun. , pp. 1019-1020
    • Ibrahim, S.K.1    Vincent, K.2    Gormal, C.A.3    Smith, B.E.4    Best, S.P.5    Pickett, C.J.6
  • 50
    • 0030809394 scopus 로고    scopus 로고
    • Time-resolved binding of carbon monoxide to nitrogenase monitored by stopped-flow infrared spectroscopy
    • George, S. J., Ashby, G. A., Wharton, C. W., and Thorneley, R. N. F. T. (1997) Time-resolved binding of carbon monoxide to nitrogenase monitored by stopped-flow infrared spectroscopy, J. Am. Chem. Soc. 6450-6451.
    • (1997) J. Am. Chem. Soc. , pp. 6450-6451
    • George, S.J.1    Ashby, G.A.2    Wharton, C.W.3    Thorneley, R.N.F.T.4
  • 52
    • 0030888054 scopus 로고    scopus 로고
    • Evidence for multiple substrate-reduction sites and distinct inhibitor-binding sites from an altered Azotobacter vinelandii nitrogenase MoFe protein
    • Shen, J., Dean, D. R., and Newton, W. E. (1997) Evidence for multiple substrate-reduction sites and distinct inhibitor-binding sites from an altered Azotobacter vinelandii nitrogenase MoFe protein, Biochemistry 36, 4884-4894.
    • (1997) Biochemistry , vol.36 , pp. 4884-4894
    • Shen, J.1    Dean, D.R.2    Newton, W.E.3
  • 53
    • 0028944336 scopus 로고
    • Role of the MoFe protein α-subunit histidine-195 residue in FeMo-cofactor binding and nitrogenase catalysis
    • Kim, C.-H., Newton, W. E., and Dean, D. R. (1995) Role of the MoFe protein α-subunit histidine-195 residue in FeMo-cofactor binding and nitrogenase catalysis, Biochemistry 34, 2798-2808.
    • (1995) Biochemistry , vol.34 , pp. 2798-2808
    • Kim, C.-H.1    Newton, W.E.2    Dean, D.R.3
  • 54
    • 0001268396 scopus 로고
    • Structure and spectroscopic properties of five-coordinate (2-methylimidazolato)- and six-coordinate (imidazole)(imidazolato)iron(II) "picket-fence" porphyrins
    • Mandon, D., Ott-Woelfel, F., Fischer, J., Weiss, R., Bill, E., and Trautwein, A. X. (1990) Structure and spectroscopic properties of five-coordinate (2-methylimidazolato)- and six-coordinate (imidazole)(imidazolato)iron(II) "picket-fence" porphyrins, Inorg. Chem. 29, 2442-2447.
    • (1990) Inorg. Chem. , vol.29 , pp. 2442-2447
    • Mandon, D.1    Ott-Woelfel, F.2    Fischer, J.3    Weiss, R.4    Bill, E.5    Trautwein, A.X.6
  • 55
    • 33847084940 scopus 로고
    • Imidazolate complexes of iron and manganese tetraphenylporphyrins
    • Landrum, J. T., Hatano, K., Scheidt, W. R., and Reed, C. A. (1980) Imidazolate complexes of iron and manganese tetraphenylporphyrins, J. Am. Chem. Soc. 102, 6729-6735.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 6729-6735
    • Landrum, J.T.1    Hatano, K.2    Scheidt, W.R.3    Reed, C.A.4
  • 56
    • 37049086377 scopus 로고
    • Crystal structures of low- and high-spin iron(III) complexes with quadridentate Schiff bases
    • Nishida, Y., Kino, K., and Kida, S. (1987) Crystal structures of low- and high-spin iron(III) complexes with quadridentate Schiff bases, J. Chem. Soc., Dalton Trans. 1157-1161.
    • (1987) J. Chem. Soc., Dalton Trans. , pp. 1157-1161
    • Nishida, Y.1    Kino, K.2    Kida, S.3
  • 57
    • 0000435474 scopus 로고
    • Influence of pentaamminechromium(III) on the acidity of coordinated imidazoles and pyrazole
    • and references therein
    • Winter, J. A., Caruso, D., and Shepherd, R. E. (1988) Influence of pentaamminechromium(III) on the acidity of coordinated imidazoles and pyrazole, Inorg. Chem. 27, 1086-1089 and references therein.
    • (1988) Inorg. Chem. , vol.27 , pp. 1086-1089
    • Winter, J.A.1    Caruso, D.2    Shepherd, R.E.3
  • 58
    • 0001261974 scopus 로고    scopus 로고
    • Electron paramagnetic resonance spectroscopy of the iron-molybdenum cofactor of Clostridium pasteurianum nitrogenase
    • George, G. N., Prince, R. C., and Bare, R. E. (1996) Electron paramagnetic resonance spectroscopy of the iron-molybdenum cofactor of Clostridium pasteurianum nitrogenase, Inorg. Chem. 35, 434-438.
    • (1996) Inorg. Chem. , vol.35 , pp. 434-438
    • George, G.N.1    Prince, R.C.2    Bare, R.E.3
  • 59
    • 0036570350 scopus 로고    scopus 로고
    • Binding modes for the first coupled electron and proton addition to FeMoco of nitrogenase
    • Lovell, T., Li, J., Case, D. A., and Noodleman, L. (2002) Binding modes for the first coupled electron and proton addition to FeMoco of nitrogenase, J. Am. Chem. Soc. 124, 4546-4547.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4546-4547
    • Lovell, T.1    Li, J.2    Case, D.A.3    Noodleman, L.4


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