메뉴 건너뛰기




Volumn 53, Issue 39, 2014, Pages 6151-6160

Another role for CO with nitrogenase? CO stimulates hydrogen evolution catalyzed by variant azotobacter vinelandii Mo-nitrogenases

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOLOGY; CATALYSIS; HYDROGEN; HYDROGEN BONDS; PROTONS;

EID: 84907855422     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500546k     Document Type: Article
Times cited : (8)

References (60)
  • 1
    • 0018130448 scopus 로고
    • Kinetic studies on electron transfer and interaction between nitrogenase components from Azotobacter vinelandii
    • Hageman, R. V. and Burris, R. H. (1978) Kinetic studies on electron transfer and interaction between nitrogenase components from Azotobacter vinelandii Biochemistry 17, 4117-4124
    • (1978) Biochemistry , vol.17 , pp. 4117-4124
    • Hageman, R.V.1    Burris, R.H.2
  • 2
    • 0021764941 scopus 로고
    • The mechanism of Klebsiella pneumoniae nitrogenase action
    • Lowe, D. J. and Thorneley, R. N. F. (1984) The mechanism of Klebsiella pneumoniae nitrogenase action Biochem. J. 224, 877-909
    • (1984) Biochem. J. , vol.224 , pp. 877-909
    • Lowe, D.J.1    Thorneley, R.N.F.2
  • 3
    • 0032535386 scopus 로고    scopus 로고
    • Nitrogenase of Azotobacter vinelandii: Kinetic analysis of the Fe protein redox cycle
    • Duyvis, M. G., Wassink, H., and Haaker, H. (1998) Nitrogenase of Azotobacter vinelandii: Kinetic analysis of the Fe protein redox cycle Biochemistry 37, 17345-17354
    • (1998) Biochemistry , vol.37 , pp. 17345-17354
    • Duyvis, M.G.1    Wassink, H.2    Haaker, H.3
  • 4
    • 0026734002 scopus 로고
    • Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii
    • Kim, J. and Rees, D. C. (1992) Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii Nature 360, 553-560
    • (1992) Nature , vol.360 , pp. 553-560
    • Kim, J.1    Rees, D.C.2
  • 6
    • 81555207920 scopus 로고    scopus 로고
    • X-ray emission spectroscopy evidences a central carbon in the nitrogenase iron-molybdenum cofactor
    • Lancaster, K. M., Roemelt, M., Ettenhuber, P., Hu, Y., Ribbe, M. W., Neese, F., Bergmann, U., and DeBeer, S. (2011) X-ray emission spectroscopy evidences a central carbon in the nitrogenase iron-molybdenum cofactor Science 334, 974-977
    • (2011) Science , vol.334 , pp. 974-977
    • Lancaster, K.M.1    Roemelt, M.2    Ettenhuber, P.3    Hu, Y.4    Ribbe, M.W.5    Neese, F.6    Bergmann, U.7    Debeer, S.8
  • 7
    • 84866749191 scopus 로고    scopus 로고
    • Radical SAM-dependent carbon insertion into the nitrogenase M-cluster
    • Wiig, J. A., Hu, Y., Lee, C. C., and Ribbe, M. W. (2012) Radical SAM-dependent carbon insertion into the nitrogenase M-cluster Science 337, 1672-1675
    • (2012) Science , vol.337 , pp. 1672-1675
    • Wiig, J.A.1    Hu, Y.2    Lee, C.C.3    Ribbe, M.W.4
  • 8
    • 0006156895 scopus 로고
    • Isolation of an iron-molybdenum cofactor from nitrogenase
    • Shah, V. K. and Brill, W. J. (1977) Isolation of an iron-molybdenum cofactor from nitrogenase Proc. Natl. Acad. Sci. U.S.A. 74, 3249-3253
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 3249-3253
    • Shah, V.K.1    Brill, W.J.2
  • 9
    • 0025191972 scopus 로고
    • Role for the nitrogenase MoFe protein α-subunit in FeMo-cofactor binding and catalysis
    • Scott, D. J., May, H. D., Newton, W. E., Brigle, K. E., and Dean, D. R. (1990) Role for the nitrogenase MoFe protein α-subunit in FeMo-cofactor binding and catalysis Nature 343, 188-190
    • (1990) Nature , vol.343 , pp. 188-190
    • Scott, D.J.1    May, H.D.2    Newton, W.E.3    Brigle, K.E.4    Dean, D.R.5
  • 10
    • 11144229617 scopus 로고    scopus 로고
    • Substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis
    • Barney, B. M., Igarashi, R. Y., Dos Santos, P. C., Dean, D. R., and Seefeldt, L. C. (2004) Substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis J. Biol. Chem. 279, 53621-53624
    • (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
  • 11
    • 80052936294 scopus 로고    scopus 로고
    • Assays of nitrogenase reaction products
    • In (Ribbe, M. W. Ed.) pp, Humana Press, New York. - 127
    • Newton, W. E. and Dilworth, M. J. (2011) Assays of Nitrogenase Reaction Products. In Nitrogen Fixation: Methods and Protocols (Ribbe, M. W., Ed.) pp 105-127, Humana Press, New York.
    • (2011) Nitrogen Fixation: Methods and Protocols , pp. 105
    • Newton, W.E.1    Dilworth, M.J.2
  • 12
    • 0015928874 scopus 로고
    • Inhibition of nitrogenase-catalyzed reductions
    • Hwang, J. C., Chen, C. H., and Burris, R. H. (1973) Inhibition of nitrogenase-catalyzed reductions Biochim. Biophys. Acta 292, 256-270
    • (1973) Biochim. Biophys. Acta , vol.292 , pp. 256-270
    • Hwang, J.C.1    Chen, C.H.2    Burris, R.H.3
  • 13
    • 0018805367 scopus 로고
    • Iron-sulfur clusters in the molybdenum-iron protein component of nitrogenase. Electron paramagnetic resonance of the CO-inhibited state
    • Davis, L. C., Henzl, M. T., Burris, R. H., and Orme-Johnson, W. H. (1979) Iron-sulfur clusters in the molybdenum-iron protein component of nitrogenase. Electron paramagnetic resonance of the CO-inhibited state Biochemistry 18, 4860-4869
    • (1979) Biochemistry , vol.18 , pp. 4860-4869
    • Davis, L.C.1    Henzl, M.T.2    Burris, R.H.3    Orme-Johnson, W.H.4
  • 14
    • 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
  • 15
    • 0034680937 scopus 로고    scopus 로고
    • Competitive substrate and inhibitor interactions at the physiologically relevant active site of nitrogenase
    • Christiansen, J., Seefeldt, L. C., and Dean, D. R. (2000) Competitive substrate and inhibitor interactions at the physiologically relevant active site of nitrogenase J. Biol. Chem. 275, 36104-36107
    • (2000) J. Biol. Chem. , vol.275 , pp. 36104-36107
    • Christiansen, J.1    Seefeldt, L.C.2    Dean, D.R.3
  • 16
    • 1542267776 scopus 로고    scopus 로고
    • Differentiation of acetylene-reduction sites by stereoselective proton addition during Azotobacter vinelandii nitrogenase-catalyzed C2D2 reduction
    • Han, J. and Newton, W. E. (2004) Differentiation of acetylene-reduction sites by stereoselective proton addition during Azotobacter vinelandii nitrogenase-catalyzed C2D2 reduction Biochemistry 43, 2947-2956
    • (2004) Biochemistry , vol.43 , pp. 2947-2956
    • Han, J.1    Newton, W.E.2
  • 17
    • 0030702105 scopus 로고    scopus 로고
    • CO binding to the FeMo cofactor of CO-inhibited nitrogenase: 13CO and 1H Q-band ENDOR investigation
    • Lee, H.-I., Cameron, L. M., Hales, B. J., and Hoffman, B. M. (1997) CO binding to the FeMo cofactor of CO-inhibited nitrogenase: 13CO and 1H Q-band ENDOR investigation J. Am. Chem. Soc. 119, 10121-10126
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 10121-10126
    • Lee, H.-I.1    Cameron, L.M.2    Hales, B.J.3    Hoffman, B.M.4
  • 18
    • 33947444303 scopus 로고
    • Mechanism of nitrogen fixation. VIII. Carbon monoxide as an inhibitor for nitrogen fixation by red clover
    • Lind, C. J. and Wilson, P. W. (1941) Mechanism of nitrogen fixation. VIII. Carbon monoxide as an inhibitor for nitrogen fixation by red clover J. Am. Chem. Soc. 63, 3511-3514
    • (1941) J. Am. Chem. Soc. , vol.63 , pp. 3511-3514
    • Lind, C.J.1    Wilson, P.W.2
  • 19
    • 0027738037 scopus 로고
    • Nitrogenase reactivity: Effects of pH on substrate reduction and CO inhibition
    • Pham, D. N. and Burgess, B. K. (1993) Nitrogenase reactivity: Effects of pH on substrate reduction and CO inhibition Biochemistry 32, 13725-13731
    • (1993) Biochemistry , vol.32 , pp. 13725-13731
    • Pham, D.N.1    Burgess, B.K.2
  • 20
    • 0026758053 scopus 로고
    • Nitrogenase-catalyzed ethane production and CO-sensitive hydrogen evolution from MoFe proteins having amino acid substitutions in an α-subunit FeMo cofactor-binding domain
    • Scott, D. J., Dean, D. R., and Newton, W. E. (1992) Nitrogenase-catalyzed ethane production and CO-sensitive hydrogen evolution from MoFe proteins having amino acid substitutions in an α-subunit FeMo cofactor-binding domain J. Biol. Chem. 267, 20002-20010
    • (1992) J. Biol. Chem. , vol.267 , pp. 20002-20010
    • Scott, D.J.1    Dean, D.R.2    Newton, W.E.3
  • 21
    • 21544470280 scopus 로고    scopus 로고
    • Variant MoFe proteins of Azotobacter vinelandii: Effects of carbon monoxide on electron paramagnetic resonance spectra generated during enzyme turnover
    • Maskos, Z., Fisher, K., Sørlie, M., Newton, W. E., and Hales, B. J. (2005) Variant MoFe proteins of Azotobacter vinelandii: Effects of carbon monoxide on electron paramagnetic resonance spectra generated during enzyme turnover JBIC, J. Biol. Inorg. Chem. 10, 394-406
    • (2005) JBIC, J. Biol. Inorg. Chem. , vol.10 , pp. 394-406
    • Maskos, Z.1    Fisher, K.2    Sørlie, M.3    Newton, W.E.4    Hales, B.J.5
  • 22
    • 0019441380 scopus 로고
    • Requirement of nifV gene for production of wild-type nitrogenase enzyme in Klebsiella pneumoniae
    • McLean, P. A. and Dixon, R. A. (1981) Requirement of nifV gene for production of wild-type nitrogenase enzyme in Klebsiella pneumoniae Nature 292, 655-656
    • (1981) Nature , vol.292 , pp. 655-656
    • McLean, P.A.1    Dixon, R.A.2
  • 23
    • 0024961083 scopus 로고
    • Homocitrate is a component of the iron-molybdenum cofactor of nitrogenase
    • Hoover, T. R., Imperial, J., Ludden, P. W., and Shah, V. K. (1989) Homocitrate is a component of the iron-molybdenum cofactor of nitrogenase Biochemistry 28, 2766-2771
    • (1989) Biochemistry , vol.28 , pp. 2766-2771
    • Hoover, T.R.1    Imperial, J.2    Ludden, P.W.3    Shah, V.K.4
  • 24
    • 77955301302 scopus 로고    scopus 로고
    • Vanadium nitrogenase reduces CO
    • Lee, C. C., Hu, Y., and Ribbe, M. W. (2010) Vanadium nitrogenase reduces CO Science 329, 642
    • (2010) Science , vol.329 , pp. 642
    • Lee, C.C.1    Hu, Y.2    Ribbe, M.W.3
  • 25
    • 0023953440 scopus 로고
    • The vanadium nitrogenase of Azotobacter vinelandii. Reduction of acetylene and ethylene to ethane
    • Dilworth, M. J., Eady, R. R., and Eldridge, M. E. (1988) The vanadium nitrogenase of Azotobacter vinelandii. Reduction of acetylene and ethylene to ethane Biochem. J. 249, 745-751
    • (1988) Biochem. J. , vol.249 , pp. 745-751
    • Dilworth, M.J.1    Eady, R.R.2    Eldridge, M.E.3
  • 26
    • 67249112766 scopus 로고    scopus 로고
    • Unique features of the nitrogenase VFe protein from Azotobacter vinelandii
    • Lee, C. C., Hu, Y., and Ribbe, M. W. (2009) Unique features of the nitrogenase VFe protein from Azotobacter vinelandii Proc. Natl. Acad. Sci. U.S.A. 106, 9209-9214
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 9209-9214
    • Lee, C.C.1    Hu, Y.2    Ribbe, M.W.3
  • 27
    • 79961225142 scopus 로고    scopus 로고
    • Extending the carbon chain: Hydrocarbon formation catalyzed by vanadium/molybdenum nitrogenases
    • Hu, Y., Lee, C. C., and Ribbe, M. W. (2011) Extending the carbon chain: Hydrocarbon formation catalyzed by vanadium/molybdenum nitrogenases Science 333, 753-755
    • (2011) Science , vol.333 , pp. 753-755
    • Hu, Y.1    Lee, C.C.2    Ribbe, M.W.3
  • 28
    • 79955577511 scopus 로고    scopus 로고
    • Molydenum nitrogenase catalyzes the reduction and coupling of CO to form hydrocarbons
    • Yang, Z. Y., Dean, D. R., and Seefeldt, L. C. (2011) Molydenum nitrogenase catalyzes the reduction and coupling of CO to form hydrocarbons J. Biol. Chem. 286, 19417-19421
    • (2011) J. Biol. Chem. , vol.286 , pp. 19417-19421
    • Yang, Z.Y.1    Dean, D.R.2    Seefeldt, L.C.3
  • 29
    • 0014036196 scopus 로고
    • Reduction of cyanide and isocyanide by nitrogenase of Azotobacter chroococcum
    • Kelly, M., Postgate, J. R., and Richards, R. L. (1967) Reduction of cyanide and isocyanide by nitrogenase of Azotobacter chroococcum Biochem. J. 102, 1c-3c
    • (1967) Biochem. J. , vol.102 , pp. 1c-3c
    • Kelly, M.1    Postgate, J.R.2    Richards, R.L.3
  • 30
    • 0030063724 scopus 로고    scopus 로고
    • Investigation of CO binding and release from Mo-nitrogenase during catalytic turnover
    • Cameron, L. M. and Hales, B. J. (1996) Investigation of CO binding and release from Mo-nitrogenase during catalytic turnover J. Am. Chem. Soc. 118, 279-280
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 279-280
    • Cameron, L.M.1    Hales, B.J.2
  • 31
    • 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. (1997) Time-resolved binding of carbon monoxide to nitrogenase monitored by stopped-flow infrared spectroscopy J. Am. Chem. Soc. 119, 6450-6451
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6450-6451
    • George, S.J.1    Ashby, G.A.2    Wharton, C.W.3    Thorneley, R.N.F.4
  • 32
    • 78650694527 scopus 로고    scopus 로고
    • Steric control of the hi-CO MoFe nitrogenase complex revealed by stopped-flow infrared spectroscopy
    • Yang, Z.-Y., Seefeldt, L. C., Dean, D. R., Cramer, S. P., and George, S. J. (2011) Steric control of the hi-CO MoFe nitrogenase complex revealed by stopped-flow infrared spectroscopy Angew. Chem., Int. Ed. 50, 272-275
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 272-275
    • Yang, Z.-Y.1    Seefeldt, L.C.2    Dean, D.R.3    Cramer, S.P.4    George, S.J.5
  • 33
    • 79955069648 scopus 로고    scopus 로고
    • Photolysis of hi-CO nitrogenase: Observation of a plethora of distinct CO species using infrared spectroscopy
    • Yan, L., Dapper, C. H., George, S. J., Wang, H.-X., Mitra, D., Dong, W.-B., Newton, W. E., and Cramer, S. P. (2011) Photolysis of hi-CO nitrogenase: Observation of a plethora of distinct CO species using infrared spectroscopy Eur. J. Inorg. Chem. 2011, 2064-2074
    • (2011) Eur. J. Inorg. Chem. , vol.2011 , pp. 2064-2074
    • Yan, L.1    Dapper, C.H.2    George, S.J.3    Wang, H.-X.4    Mitra, D.5    Dong, W.-B.6    Newton, W.E.7    Cramer, S.P.8
  • 34
    • 84870942505 scopus 로고    scopus 로고
    • IR-monitored photolysis of CO-inhibited nitrogenase: A major EPR-silent species with coupled terminal CO ligands
    • Yan, L., Pelmenschikov, V., Dapper, C. H., Scott, A. D., Newton, W. E., and Cramer, S. P. (2012) IR-monitored photolysis of CO-inhibited nitrogenase: A major EPR-silent species with coupled terminal CO ligands Chemistry 18, 16349-16357
    • (2012) Chemistry , vol.18 , pp. 16349-16357
    • Yan, L.1    Pelmenschikov, V.2    Dapper, C.H.3    Scott, A.D.4    Newton, W.E.5    Cramer, S.P.6
  • 36
    • 0026705527 scopus 로고
    • Structural models for the metal centers in the nitrogenase molybdenum-iron protein
    • Kim, J. and Rees, D. C. (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
  • 37
    • 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
  • 38
    • 0034687761 scopus 로고    scopus 로고
    • Differential effects on N2 binding and reduction, HD formation, and azide reduction with α-195His- and α-191Gln-substituted MoFe proteins of Azotobacter vinelandii nitrogenase
    • Fisher, K., Dilworth, M. J., and Newton, W. E. (2000) Differential effects on N2 binding and reduction, HD formation, and azide reduction with α-195His- and α-191Gln-substituted MoFe proteins of Azotobacter vinelandii nitrogenase Biochemistry 39, 15570-15577
    • (2000) Biochemistry , vol.39 , pp. 15570-15577
    • Fisher, K.1    Dilworth, M.J.2    Newton, W.E.3
  • 41
    • 0019321298 scopus 로고
    • Large-scale purification of high activity Azotobacter vinelandii nitrogenase
    • Burgess, B. K., Jacobs, D. B., and Stiefel, E. I. (1980) Large-scale purification of high activity Azotobacter vinelandii nitrogenase Biochim. Biophys. Acta 614, 196-209
    • (1980) Biochim. Biophys. Acta , vol.614 , pp. 196-209
    • Burgess, B.K.1    Jacobs, D.B.2    Stiefel, E.I.3
  • 42
    • 0023404187 scopus 로고
    • Nitrogenase of Klebsiella pneumoniae: Kinetic studies on the Fe protein involving reduction by sodium dithionite, the binding of MgADP and a conformational change that alters the reactivity of the 4Fe-4S centre
    • Ashby, G. A. and Thorneley, R. N. F. (1987) Nitrogenase of Klebsiella pneumoniae: Kinetic studies on the Fe protein involving reduction by sodium dithionite, the binding of MgADP and a conformational change that alters the reactivity of the 4Fe-4S centre Biochem. J. 246, 455-465
    • (1987) Biochem. J. , vol.246 , pp. 455-465
    • Ashby, G.A.1    Thorneley, R.N.F.2
  • 43
    • 0028879689 scopus 로고
    • Involvement of the P cluster in intramolecular electron transfer within the nitrogenase MoFe protein
    • Peters, J. W., Fisher, K., Newton, W. E., and Dean, D. R. (1995) Involvement of the P cluster in intramolecular electron transfer within the nitrogenase MoFe protein J. Biol. Chem. 270, 27007-27013
    • (1995) J. Biol. Chem. , vol.270 , pp. 27007-27013
    • Peters, J.W.1    Fisher, K.2    Newton, W.E.3    Dean, D.R.4
  • 44
    • 0020852333 scopus 로고
    • Nitrogenase of Klebsiella pneumoniae. Kinetics of the dissociation of oxidized iron protein from molybdenum-iron protein: Identification of the rate-limiting step for substrate reduction
    • Thorneley, R. N. F. and Lowe, D. J. (1983) Nitrogenase of Klebsiella pneumoniae. Kinetics of the dissociation of oxidized iron protein from molybdenum-iron protein: Identification of the rate-limiting step for substrate reduction Biochem. J. 215, 393-403
    • (1983) Biochem. J. , vol.215 , pp. 393-403
    • Thorneley, R.N.F.1    Lowe, D.J.2
  • 45
    • 0025833638 scopus 로고
    • Klebsiella pneumoniae nitrogenase. The pre-steady-state kinetics of MoFe-protein reduction and hydrogen evolution under conditions of limiting electron flux show that the rates of association with the Fe-protein and electron transfer are independent of the oxidation level of the MoFe protein
    • Fisher, K., Lowe, D. J., and Thorneley, R. N. F. (1991) Klebsiella pneumoniae nitrogenase. The pre-steady-state kinetics of MoFe-protein reduction and hydrogen evolution under conditions of limiting electron flux show that the rates of association with the Fe-protein and electron transfer are independent of the oxidation level of the MoFe protein Biochem. J. 279, 81-85
    • (1991) Biochem. J. , vol.279 , pp. 81-85
    • Fisher, K.1    Lowe, D.J.2    Thorneley, R.N.F.3
  • 46
    • 1542331318 scopus 로고    scopus 로고
    • Substrate reduction and CO susceptibility of the ΔnifV and α-Q191K MoFe proteins of Azotobacter vinelandii nitrogenase
    • In (Finan, T. O'Brian, M. Layzell, D. Vessey, K. and Newton, W. E. Eds.) p, CAB International, Wallingford, U.K.
    • Newton, W. E., Vichitphan, K., and Fisher, K. (2002) Substrate reduction and CO susceptibility of the ΔNifV and α-Q191K MoFe proteins of Azotobacter vinelandii nitrogenase. In Nitrogen Fixation: Global Prospects (Finan, T., O'Brian, M., Layzell, D., Vessey, K., and Newton, W. E., Eds.) p 370, CAB International, Wallingford, U.K.
    • (2002) Nitrogen Fixation: Global Prospects , pp. 370
    • Newton, W.E.1    Vichitphan, K.2    Fisher, K.3
  • 47
    • 0025601527 scopus 로고
    • Klebsiella pneumoniae nitrogenase. Mechanism of acetylene reduction and its inhibition by carbon monoxide
    • Lowe, D. J., Fisher, K., and Thorneley, R. N. F. (1990) Klebsiella pneumoniae nitrogenase. Mechanism of acetylene reduction and its inhibition by carbon monoxide Biochem. J. 272, 621-625
    • (1990) Biochem. J. , vol.272 , pp. 621-625
    • Lowe, D.J.1    Fisher, K.2    Thorneley, R.N.F.3
  • 48
    • 0023051604 scopus 로고
    • Characterization of three different flavodoxins from Azotobacter vinelandii
    • Klugkist, J., Voorberg, J., Haaker, H., and Veeger, C. (1986) Characterization of three different flavodoxins from Azotobacter vinelandii Eur. J. Biochem. 155, 33-40
    • (1986) Eur. J. Biochem. , vol.155 , pp. 33-40
    • Klugkist, J.1    Voorberg, J.2    Haaker, H.3    Veeger, C.4
  • 49
    • 0035916919 scopus 로고    scopus 로고
    • Electron paramagnetic resonance analysis of different Azotobacter vinelandii nitrogenase MoFe-protein conformations generated during enzyme turnover: Evidence for S = 3/2 spin states from reduced MoFe-protein intermediates
    • Fisher, K., Newton, W. E., and Lowe, D. J. (2001) Electron paramagnetic resonance analysis of different Azotobacter vinelandii nitrogenase MoFe-protein conformations generated during enzyme turnover: Evidence for S = 3/2 spin states from reduced MoFe-protein intermediates Biochemistry 40, 3333-3339
    • (2001) Biochemistry , vol.40 , pp. 3333-3339
    • Fisher, K.1    Newton, W.E.2    Lowe, D.J.3
  • 50
    • 35348832336 scopus 로고    scopus 로고
    • Conformations generated during turnover of the Azotobacter vinelandii MoFe protein and their relationship to physiological function
    • Fisher, K., Lowe, D. J., Tavares, P., Pereira, A. S., Huynh, B. H., Edmondson, D., and Newton, W. E. (2007) Conformations generated during turnover of the Azotobacter vinelandii MoFe protein and their relationship to physiological function J. Inorg. Biochem. 101, 1649-1656
    • (2007) J. Inorg. Biochem. , vol.101 , pp. 1649-1656
    • Fisher, K.1    Lowe, D.J.2    Tavares, P.3    Pereira, A.S.4    Huynh, B.H.5    Edmondson, D.6    Newton, W.E.7
  • 51
    • 0027174618 scopus 로고
    • Klebsiella pneumoniae nitrogenase. Pre-steady-state absorbance changes show redox changes occur in the MoFe protein that depend on substrate and component protein ratio; A role for P-centres in reducing dinitrogen?
    • Lowe, D. J., Fisher, K., and Thorneley, R. N. F. (1993) Klebsiella pneumoniae nitrogenase. Pre-steady-state absorbance changes show redox changes occur in the MoFe protein that depend on substrate and component protein ratio; a role for P-centres in reducing dinitrogen? Biochem. J. 292, 93-98
    • (1993) Biochem. J. , vol.292 , pp. 93-98
    • Lowe, D.J.1    Fisher, K.2    Thorneley, R.N.F.3
  • 52
    • 80054972869 scopus 로고    scopus 로고
    • Electron transfer within nitrogenase: Evidence for a deficit-spending mechanism
    • Danyal, K., Dean, D. R., Hoffman, B. M., and Seefeldt, L. C. (2011) Electron transfer within nitrogenase: Evidence for a deficit-spending mechanism Biochemistry 50, 9255-9263
    • (2011) Biochemistry , vol.50 , pp. 9255-9263
    • Danyal, K.1    Dean, D.R.2    Hoffman, B.M.3    Seefeldt, L.C.4
  • 53
    • 80055001439 scopus 로고    scopus 로고
    • Fe57 ENDOR spectroscopy and "electron inventory" analysis of the nitrogenase E4 intermediate suggest the metal-ion core of FeMo-cofactor cycles through only one redox couple
    • Doan, P. E., Telser, J., Barney, B. M., Igarashi, R. Y., Dean, D. R., Seefeldt, L. C., and Hoffman, B. M. (2011) 57Fe ENDOR spectroscopy and "electron inventory" analysis of the nitrogenase E4 intermediate suggest the metal-ion core of FeMo-cofactor cycles through only one redox couple J. Am. Chem. Soc. 133, 17329-17340
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 17329-17340
    • Doan, P.E.1    Telser, J.2    Barney, B.M.3    Igarashi, R.Y.4    Dean, D.R.5    Seefeldt, L.C.6    Hoffman, B.M.7
  • 54
    • 33646886579 scopus 로고    scopus 로고
    • Mechanistic significance of the preparatory migration of hydrogen atoms around the FeMo-co active site of nitrogenase
    • Dance, I. (2006) Mechanistic significance of the preparatory migration of hydrogen atoms around the FeMo-co active site of nitrogenase Biochemistry 45, 6328-6340
    • (2006) Biochemistry , vol.45 , pp. 6328-6340
    • Dance, I.1
  • 55
    • 84896940877 scopus 로고    scopus 로고
    • Mechanism of nitrogen fixation by nitrogenase: The next stage
    • references cited therein - 4062
    • Hoffman, B. M., Lukoyanov, D., Yang, Z.-Y., Dean, D. R., and Seefeldt, L. C. (2014) Mechanism of nitrogen fixation by nitrogenase: The next stage Chem. Rev. 114, 4041-4062 and references cited therein
    • (2014) Chem. Rev. , vol.114 , pp. 4041
    • Hoffman, B.M.1    Lukoyanov, D.2    Yang, Z.-Y.3    Dean, D.R.4    Seefeldt, L.C.5
  • 56
    • 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
  • 57
    • 79958862812 scopus 로고    scopus 로고
    • Calculated vibrational frequencies for FeMo-co, the active site of nitrogenase, bearing hydrogen atoms and carbon monoxide
    • Dance, I. (2011) Calculated vibrational frequencies for FeMo-co, the active site of nitrogenase, bearing hydrogen atoms and carbon monoxide Dalton Trans. 40, 6480-6489
    • (2011) Dalton Trans. , vol.40 , pp. 6480-6489
    • Dance, I.1
  • 58
    • 23644441586 scopus 로고    scopus 로고
    • The hydrogen chemistry of the FeMo-co active site of nitrogenase
    • Dance, I. (2005) The hydrogen chemistry of the FeMo-co active site of nitrogenase J. Am. Chem. Soc. 127, 10925-10942
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 10925-10942
    • Dance, I.1
  • 60
    • 84898866788 scopus 로고    scopus 로고
    • Substrate channel in nitrogenase revealed by a molecular dynamics approach
    • Smith, D., Danyal, K., Raugei, S., and Seefeldt, L. C. (2014) Substrate channel in nitrogenase revealed by a molecular dynamics approach Biochemistry 53, 2278-2285
    • (2014) Biochemistry , vol.53 , pp. 2278-2285
    • Smith, D.1    Danyal, K.2    Raugei, S.3    Seefeldt, L.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.