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Volumn 43, Issue 3, 2004, Pages 799-807

Voltammetric Studies of the Catalytic Mechanism of the Respiratory Nitrate Reductase from Escherichia coli: How Nitrate Reduction and Inhibition Depend on the Oxidation State of the Active Site

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ELECTRODES; ENZYME INHIBITION; ESCHERICHIA COLI; GRAPHITE; MOLYBDENUM; NITRATES; OXIDATION; PH EFFECTS; PYROLYSIS; REDOX REACTIONS; REDUCTION;

EID: 1642453844     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035869j     Document Type: Article
Times cited : (86)

References (36)
  • 1
    • 0034153610 scopus 로고    scopus 로고
    • Bacterial respiration: A flexible process for a changing environment
    • Richardson, D. J. (2000) Bacterial respiration: A flexible process for a changing environment, Microbiology 146, 551-571.
    • (2000) Microbiology , vol.146 , pp. 551-571
    • Richardson, D.J.1
  • 2
    • 0000273676 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • Hille, R. (1996) The mononuclear molybdenum enzymes, Chem. Rev. 96, 2757-2816.
    • (1996) Chem. Rev. , vol.96 , pp. 2757-2816
    • Hille, R.1
  • 3
    • 0025368948 scopus 로고
    • Nitrate reductases of Escherichia coli-sequence of the 2nd nitrate reductase and comparison with that encoded by the narGHJI operon
    • Blasco, F., lobbi, C., Ratouchniak, J., Bonnefoy, V., and Chippaux, M. (1990) Nitrate reductases of Escherichia coli-sequence of the 2nd nitrate reductase and comparison with that encoded by the narGHJI operon, Mol. Gen. Genet. 222, 104-111.
    • (1990) Mol. Gen. Genet. , vol.222 , pp. 104-111
    • Blasco, F.1    Lobbi, C.2    Ratouchniak, J.3    Bonnefoy, V.4    Chippaux, M.5
  • 4
    • 0023656328 scopus 로고
    • Biochemical and immunological evidence for a 2nd nitrate reductase in Escherichia coli K12
    • Iobbi, C., Santini, C. L., Bonnefoy, V., and Giordano, G. (1987) Biochemical and immunological evidence for a 2nd nitrate reductase in Escherichia coli K12, Eur. J. Biochem. 168, 451-459.
    • (1987) Eur. J. Biochem. , vol.168 , pp. 451-459
    • Iobbi, C.1    Santini, C.L.2    Bonnefoy, V.3    Giordano, G.4
  • 6
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
    • Jormakka, M., Tomroth, S., Byrne, B., and Iwata, S. (2002) Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N, Science 295, 1863-1868.
    • (2002) Science , vol.295 , pp. 1863-1868
    • Jormakka, M.1    Tomroth, S.2    Byrne, B.3    Iwata, S.4
  • 7
    • 0030006891 scopus 로고    scopus 로고
    • Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination
    • Schindelin, H., Kisker, C., Hilton, J., Rajagopalan, K. V., and Rees, D. C. (1996) Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination, Science 272, 1599-1600.
    • (1996) Science , vol.272 , pp. 1599-1600
    • Schindelin, H.1    Kisker, C.2    Hilton, J.3    Rajagopalan, K.V.4    Rees, D.C.5
  • 9
    • 0035095129 scopus 로고    scopus 로고
    • Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 Å and 2.03 Å
    • Ellis, P. J., Conrads, T., Hille, R., and Kuhn, P. (2001) Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 Å and 2.03 Å. Structure 9, 125-132.
    • (2001) Structure , vol.9 , pp. 125-132
    • Ellis, P.J.1    Conrads, T.2    Hille, R.3    Kuhn, P.4
  • 10
    • 0025328799 scopus 로고
    • The specific functions of menaquinone and demethylmenaquinone in anaerobic respiration with fumarate, dimethyl sulfoxide, trimethylamine N-oxide and nitrate by Escherichia coli
    • Wissenbach, U., Kroger, A., and Unden, G. (1990) The specific functions of menaquinone and demethylmenaquinone in anaerobic respiration with fumarate, dimethyl sulfoxide, trimethylamine N-oxide and nitrate by Escherichia coli, Arch. Microbiol. 154, 60-66.
    • (1990) Arch. Microbiol. , vol.154 , pp. 60-66
    • Wissenbach, U.1    Kroger, A.2    Unden, G.3
  • 11
    • 0032546574 scopus 로고    scopus 로고
    • Molybdenum cofactor properties and Fe-S cluster coordination in Escherichia coli nitrate reductase A: Investigation by site-directed mutagenesis of the conserved His-50 residue in the NarG subunit
    • Magalon, A., Asso, M., Guigliarelli, B., Rothery, R. A., Bertrand, P., Giordano, G., and Blasco, F. (1998) Molybdenum cofactor properties and Fe-S cluster coordination in Escherichia coli nitrate reductase A: Investigation by site-directed mutagenesis of the conserved His-50 residue in the NarG subunit, Biochemistry 37, 7363-7370.
    • (1998) Biochemistry , vol.37 , pp. 7363-7370
    • Magalon, A.1    Asso, M.2    Guigliarelli, B.3    Rothery, R.A.4    Bertrand, P.5    Giordano, G.6    Blasco, F.7
  • 12
    • 0030845184 scopus 로고    scopus 로고
    • Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A (NarGHI)
    • Magalon, A., Lemesle-Meunier, D., Rothery, R. A., Frixon, C., Weiner, J. H., and Blasco, F. (1997) Heme axial ligation by the highly conserved His residues in helix II of cytochrome b (NarI) of Escherichia coli nitrate reductase A (NarGHI), J. Biol. Chem. 272, 25652-25658.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25652-25658
    • Magalon, A.1    Lemesle-Meunier, D.2    Rothery, R.A.3    Frixon, C.4    Weiner, J.H.5    Blasco, F.6
  • 13
    • 0032571394 scopus 로고    scopus 로고
    • The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI)-effect of a MobAB mutation and interactions with Fe-S clusters
    • Rothery, R. A., Magalon, A., Giordano, G., Guigliarelli, B., Blasco, F., and Weiner, J. H. (1998) The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI)-effect of a MobAB mutation and interactions with Fe-S clusters, J. Biol. Chem. 273, 7462-7469.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7462-7469
    • Rothery, R.A.1    Magalon, A.2    Giordano, G.3    Guigliarelli, B.4    Blasco, F.5    Weiner, J.H.6
  • 14
    • 0029967413 scopus 로고    scopus 로고
    • Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential 4Fe-4S clusters
    • Guigliarelli, B., Magalon, A., Asso, M., Bertrand, P., Frixon, C., Giordano, G., and Blasco, F. (1996) Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential 4Fe-4S clusters, Biochemistry 35, 4828-4836.
    • (1996) Biochemistry , vol.35 , pp. 4828-4836
    • Guigliarelli, B.1    Magalon, A.2    Asso, M.3    Bertrand, P.4    Frixon, C.5    Giordano, G.6    Blasco, F.7
  • 15
    • 0020071963 scopus 로고
    • The association of two distinct b cytochromes with the respiratory nitrate reductase of Escherichia coli
    • Hackett, N. R., and Bragg, P. D. (1982) The association of two distinct b cytochromes with the respiratory nitrate reductase of Escherichia coli, FEMS Microbiol. Lett. 13, 213-217.
    • (1982) FEMS Microbiol. Lett. , vol.13 , pp. 213-217
    • Hackett, N.R.1    Bragg, P.D.2
  • 16
    • 0026741957 scopus 로고
    • EPR and redox characterization of iron-sulfur centers in nitrate reductases-A and reductases-Z from Escherichia coli-evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism
    • Guigliarelli, B., Asso, M., More, C., Augier, V., Blasco, F., Pommier, J., Giordano, G., and Bertrand, P. (1992) EPR and redox characterization of iron-sulfur centers in nitrate reductases-A and reductases-Z from Escherichia coli-evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism, Eur. J. Biochem. 207, 61-68.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 61-68
    • Guigliarelli, B.1    Asso, M.2    More, C.3    Augier, V.4    Blasco, F.5    Pommier, J.6    Giordano, G.7    Bertrand, P.8
  • 17
    • 18744432274 scopus 로고    scopus 로고
    • Enzyme electrokinetics: Using protein film voltammetry to investigate redox enzymes and their mechanisms
    • Léger, C., Elliott, S. J., Hoke, K. R., Jeuken, L. J. C., Jones, A. K., and Armstrong, F. A. (2003) Enzyme electrokinetics: Using protein film voltammetry to investigate redox enzymes and their mechanisms, Biochemistry 42, 8653-8662.
    • (2003) Biochemistry , vol.42 , pp. 8653-8662
    • Léger, C.1    Elliott, S.J.2    Hoke, K.R.3    Jeuken, L.J.C.4    Jones, A.K.5    Armstrong, F.A.6
  • 18
    • 0035949638 scopus 로고    scopus 로고
    • Catalytic protein film voltammetry from a respiratory nitrate reductase provides evidence for complex electrochemical modulation of enzyme activity
    • Anderson, L. J., Richardson, D. J., and Butt, J. N. (2001) Catalytic protein film voltammetry from a respiratory nitrate reductase provides evidence for complex electrochemical modulation of enzyme activity, Biochemistry 40, 11294-11307.
    • (2001) Biochemistry , vol.40 , pp. 11294-11307
    • Anderson, L.J.1    Richardson, D.J.2    Butt, J.N.3
  • 19
    • 0034566220 scopus 로고    scopus 로고
    • Using direct electrochemistry to probe rate-limiting events during nitrate reductase turnover
    • Anderson, L. J., Richardson, D. J., and Butt, J. N. (2000) Using direct electrochemistry to probe rate-limiting events during nitrate reductase turnover, Faraday Discuss., 155-169.
    • (2000) Faraday Discuss. , pp. 155-169
    • Anderson, L.J.1    Richardson, D.J.2    Butt, J.N.3
  • 20
    • 0035852958 scopus 로고    scopus 로고
    • Determination of an optimal potential window for catalysis by E. coli dimethyl sulfoxide reductase and hypothesis on the role of Mo(V) in the reaction pathway
    • Heffron, K., Leger, C., Rothery, R. A., Weiner, J. H., and Armstrong, F. A. (2001) Determination of an optimal potential window for catalysis by E. coli dimethyl sulfoxide reductase and hypothesis on the role of Mo(V) in the reaction pathway, Biochemistry 40, 3117-3126.
    • (2001) Biochemistry , vol.40 , pp. 3117-3126
    • Heffron, K.1    Leger, C.2    Rothery, R.A.3    Weiner, J.H.4    Armstrong, F.A.5
  • 21
    • 0033613194 scopus 로고    scopus 로고
    • The hemes of Escherichia coli nitrate reductase A (NarGHI): Potentiometric effects of inhibitor binding to NarI
    • Rothery, R. A., Blasco, F., Magalon, A., Asso, M., and Weiner, J. H. (1999) The hemes of Escherichia coli nitrate reductase A (NarGHI): Potentiometric effects of inhibitor binding to NarI, Biochemistry 38, 12747-12757.
    • (1999) Biochemistry , vol.38 , pp. 12747-12757
    • Rothery, R.A.1    Blasco, F.2    Magalon, A.3    Asso, M.4    Weiner, J.H.5
  • 22
    • 0027406134 scopus 로고
    • Site-directed mutagenesis of conserved cysteine residues within the beta-subunil of Escherichia coli nitrate reductase-physiological, biochemical, and EPR characterization of the mutated enzymes
    • Augier, V., Guigliarelli, B., Asso, M., Bertrand, P., Frixon, C., Giordano, G., Chippaux, M., and Blasco, F. (1993) Site-directed mutagenesis of conserved cysteine residues within the beta-subunil of Escherichia coli nitrate reductase-physiological, biochemical, and EPR characterization of the mutated enzymes, Biochemistry 32, 2013-2023.
    • (1993) Biochemistry , vol.32 , pp. 2013-2023
    • Augier, V.1    Guigliarelli, B.2    Asso, M.3    Bertrand, P.4    Frixon, C.5    Giordano, G.6    Chippaux, M.7    Blasco, F.8
  • 25
    • 0037137649 scopus 로고    scopus 로고
    • Effect of a dispersion of interfacial electron-transfer rates on steady state catalytic electron transport in NiFe-hydrogenase and other enzymes
    • Léger, C., Jones, A. K., Albracht, S. P. J., and Armstrong, F. A. (2002) Effect of a dispersion of interfacial electron-transfer rates on steady state catalytic electron transport in NiFe-hydrogenase and other enzymes, J. Phys. Chem. B 106, 13058-13063.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 13058-13063
    • Léger, C.1    Jones, A.K.2    Albracht, S.P.J.3    Armstrong, F.A.4
  • 26
    • 0001678195 scopus 로고    scopus 로고
    • Interpreting the catalytic voltammetry of electroactive enzymes adsorbed on electrodes
    • Heering, H. A., Hirst, J., and Armstrong, F. A. (1998) Interpreting the catalytic voltammetry of electroactive enzymes adsorbed on electrodes, J. Phys. Chem. B 102, 6889-6902.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 6889-6902
    • Heering, H.A.1    Hirst, J.2    Armstrong, F.A.3
  • 27
    • 0345651843 scopus 로고
    • Characterization of quasi-reversible surface processes by square-wave voltammetry
    • Odea, J. J., and Osteryoung, J. G. (1993) Characterization of quasi-reversible surface processes by square-wave voltammetry, Anal. Chem. 65, 3090-3097.
    • (1993) Anal. Chem. , vol.65 , pp. 3090-3097
    • Odea, J.J.1    Osteryoung, J.G.2
  • 28
    • 0037035167 scopus 로고    scopus 로고
    • Insights into gated electron-transfer kinetics at the electrode-protein interface: A square wave voltammetry study of the blue copper protein azurin
    • Jeuken, L. J. C., McEvoy, J. P., and Armstrong, F. A. (2002) Insights into gated electron-transfer kinetics at the electrode-protein interface: A square wave voltammetry study of the blue copper protein azurin, J. Phys. Chem. B 106, 2304-2313.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 2304-2313
    • Jeuken, L.J.C.1    McEvoy, J.P.2    Armstrong, F.A.3
  • 29
    • 0037157123 scopus 로고    scopus 로고
    • Electron-transfer mechanisms through biological redox chains in multicenter enzymes
    • Jeuken, L. J. C., Jones, A. K., Chapman, S. K., Cecchini, G., and Armstrong, F. A. (2002) Electron-transfer mechanisms through biological redox chains in multicenter enzymes, J. Am. Chem. Soc. 124, 5702-5713.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5702-5713
    • Jeuken, L.J.C.1    Jones, A.K.2    Chapman, S.K.3    Cecchini, G.4    Armstrong, F.A.5
  • 30
    • 0021810531 scopus 로고
    • Complexes with halide and other anions of the molybdenum center of nitrate reductase from Escherichia coli
    • George, G. N., Bray, R. C., Morpeth, F. F., and Boxer, D. H. (1985) Complexes with halide and other anions of the molybdenum center of nitrate reductase from Escherichia coli, Biochem. J. 227, 925-931.
    • (1985) Biochem. J. , vol.227 , pp. 925-931
    • George, G.N.1    Bray, R.C.2    Morpeth, F.F.3    Boxer, D.H.4
  • 32
    • 0034672324 scopus 로고    scopus 로고
    • Thiocyanate binding to the molybdenum centre of the periplasmic nitrate reductase from Paracoccus pantotrophus
    • Butler, C. S., Chamock, J. M., Garner, C. D., Thomson, A. J., Ferguson, S. J., Berks, B. C., and Richardson, D. J. (2000) Thiocyanate binding to the molybdenum centre of the periplasmic nitrate reductase from Paracoccus pantotrophus, Biochem. J. 352, 859-864.
    • (2000) Biochem. J. , vol.352 , pp. 859-864
    • Butler, C.S.1    Chamock, J.M.2    Garner, C.D.3    Thomson, A.J.4    Ferguson, S.J.5    Berks, B.C.6    Richardson, D.J.7
  • 34
    • 0031447054 scopus 로고    scopus 로고
    • The coordination chemistry and function of the molybdenum centres of the oxomolybdoenzymes
    • Enemark, J. H., and Garner, C. D. (1997) The coordination chemistry and function of the molybdenum centres of the oxomolybdoenzymes, J. Biol. Inorg. Chem. 2, 817-822.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 817-822
    • Enemark, J.H.1    Garner, C.D.2
  • 36
    • 0033619713 scopus 로고    scopus 로고
    • Formation of a pterin radical in the reaction of the heme domain of inducible nitric oxide synthase with oxygen
    • Hurshman, A. R., Krebs, C., Edmondson, D. E., Huynh, B. H., and Marletta, M. A. (1999) Formation of a pterin radical in the reaction of the heme domain of inducible nitric oxide synthase with oxygen, Biochemistry 38, 15689-15696.
    • (1999) Biochemistry , vol.38 , pp. 15689-15696
    • Hurshman, A.R.1    Krebs, C.2    Edmondson, D.E.3    Huynh, B.H.4    Marletta, M.A.5


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