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Volumn 48, Issue 10, 2009, Pages 2156-2163

Intramolecular electron transfer in sulfite-oxidizing enzymes: Elucidating the role of a conserved active site arginine

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITES; IDEAL SYSTEMS; INTER DOMAINS; INTRAMOLECULAR ELECTRON TRANSFERS; LASER FLASH PHOTOLYSIS; MECHANISTIC PATHWAYS; MOLYBDENUM-COFACTOR; OXYGEN LIGANDS; POSITIVE CHARGES; POSITIVELY CHARGED; RESIDUE FUNCTIONS; SULFITE OXIDASE; WILD TYPES;

EID: 64349119565     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801553q     Document Type: Article
Times cited : (35)

References (40)
  • 1
    • 33745933654 scopus 로고    scopus 로고
    • Molybdenum Cofactor Biosynthesis and Molybdenum Enzymes
    • Schwarz, G., and Mendel, R. R. (2006) Molybdenum Cofactor Biosynthesis and Molybdenum Enzymes. Annu. Rev. Plant Biol. 57, 623-647.
    • (2006) Annu. Rev. Plant Biol , vol.57 , pp. 623-647
    • Schwarz, G.1    Mendel, R.R.2
  • 2
    • 0036629252 scopus 로고    scopus 로고
    • Molybdenum and Tungsten in Biology
    • Hille, R. (2002) Molybdenum and Tungsten in Biology. Trends Biochem. Sci. 27, 360-367.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 360-367
    • Hille, R.1
  • 3
    • 0002646131 scopus 로고
    • Sulfite Oxidase (Sulfite: Ferricytochrome c Oxidoreductase)
    • Coughlan, M. P, Ed, Pergamon Press, Oxford, U.K
    • Rajagopalan, K. V. (1980) Sulfite Oxidase (Sulfite: Ferricytochrome c Oxidoreductase). in Molybdenum and Molybdenum-Containing Enzymes (Coughlan, M. P., Ed.) Pergamon Press, Oxford, U.K.
    • (1980) Molybdenum and Molybdenum-Containing Enzymes
    • Rajagopalan, K.V.1
  • 4
    • 0035093274 scopus 로고    scopus 로고
    • Kappler, U., Friedrich, C. G., Truper, H. G., and Dahl, C. (2001) Evidence for Two Pathways of Thiosulfate Oxidation in Starkeya Novella (Formerly Thiobacillus Novellus). Arch. Microbiol. 175, 102-111.
    • Kappler, U., Friedrich, C. G., Truper, H. G., and Dahl, C. (2001) Evidence for Two Pathways of Thiosulfate Oxidation in Starkeya Novella (Formerly Thiobacillus Novellus). Arch. Microbiol. 175, 102-111.
  • 5
    • 0033804108 scopus 로고    scopus 로고
    • Kelly, D. P., McDonald, I. R., and Wood, A. P. (2000) Proposal for the Reclassification of Thiobacillus Novellus as Starkeya Novella gen. Nov., Comb. Nov., in the α-Subclass of the Proteobacteria. Int. J. Syst. Evol. Microbiol. 50, 1797-1802.
    • Kelly, D. P., McDonald, I. R., and Wood, A. P. (2000) Proposal for the Reclassification of Thiobacillus Novellus as Starkeya Novella gen. Nov., Comb. Nov., in the α-Subclass of the Proteobacteria. Int. J. Syst. Evol. Microbiol. 50, 1797-1802.
  • 6
    • 33748781969 scopus 로고    scopus 로고
    • Structure of the Active Site of Sulfite Dehydrogenase from Starkeya Novella
    • Doonan, C. J., Kappler, U., and George, G. N. (2006) Structure of the Active Site of Sulfite Dehydrogenase from Starkeya Novella. Inorg. Chem. 45, 7488-7492.
    • (2006) Inorg. Chem , vol.45 , pp. 7488-7492
    • Doonan, C.J.1    Kappler, U.2    George, G.N.3
  • 7
    • 21644463020 scopus 로고    scopus 로고
    • Molecular Basis of Intramolecular Electron Transfer in Sulfite-Oxidizing Enzymes is Revealed by High Resolution Structure of a Heterodimeric Complex of the Catalytic Molybdopterin Subunit and a c-Type Cytochrome Subunit
    • Kappler, U., and Bailey, S. (2005) Molecular Basis of Intramolecular Electron Transfer in Sulfite-Oxidizing Enzymes is Revealed by High Resolution Structure of a Heterodimeric Complex of the Catalytic Molybdopterin Subunit and a c-Type Cytochrome Subunit. J. Biol. Chem. 280, 24999-25007.
    • (2005) J. Biol. Chem , vol.280 , pp. 24999-25007
    • Kappler, U.1    Bailey, S.2
  • 8
    • 21644466822 scopus 로고    scopus 로고
    • Crystallization and Preliminary X-Ray Analysis of Sulfite Dehydrogenase from Starkeya Novella
    • Kappler, U., and Bailey, S. (2004) Crystallization and Preliminary X-Ray Analysis of Sulfite Dehydrogenase from Starkeya Novella. Acta Crystallogr. D60, 2070-2072.
    • (2004) Acta Crystallogr , vol.D60 , pp. 2070-2072
    • Kappler, U.1    Bailey, S.2
  • 9
    • 38149049182 scopus 로고    scopus 로고
    • Magnetic Resonance Imaging and Magnetic Resonance Spectroscopy in Isolated Sulfite Oxidase Deficiency
    • Hoffmann, C., Ben-Zeev, B., Anikster, Y., Nissenkorn, A., Brand, N., Kuint, J., and Kushnir, T. (2007) Magnetic Resonance Imaging and Magnetic Resonance Spectroscopy in Isolated Sulfite Oxidase Deficiency. J. Child Neurol. 22, 1214-1221.
    • (2007) J. Child Neurol , vol.22 , pp. 1214-1221
    • Hoffmann, C.1    Ben-Zeev, B.2    Anikster, Y.3    Nissenkorn, A.4    Brand, N.5    Kuint, J.6    Kushnir, T.7
  • 11
    • 39149130401 scopus 로고    scopus 로고
    • Sulfite Increases Lipoperoxidation and Decreases the Activity of Catalase in Brain of Rats
    • Chiarani, F., Bavaresco, C. S., Dutra-Filho, C. S., Netto, C. A., and Wyse, A. T. (2008) Sulfite Increases Lipoperoxidation and Decreases the Activity of Catalase in Brain of Rats. Metab. Brain Dis. 23, 123-132.
    • (2008) Metab. Brain Dis , vol.23 , pp. 123-132
    • Chiarani, F.1    Bavaresco, C.S.2    Dutra-Filho, C.S.3    Netto, C.A.4    Wyse, A.T.5
  • 12
    • 5644288504 scopus 로고    scopus 로고
    • A Mechanism of Sulfite Neurotoxicity: Direct Inhibition of Glutamate Dehydrogenase
    • Zhang, X., Vincent, A. S., Halliwell, B., and Wong, K. P. (2004) A Mechanism of Sulfite Neurotoxicity: Direct Inhibition of Glutamate Dehydrogenase. J. Biol. Chem. 279, 43035-43045.
    • (2004) J. Biol. Chem , vol.279 , pp. 43035-43045
    • Zhang, X.1    Vincent, A.S.2    Halliwell, B.3    Wong, K.P.4
  • 14
    • 0035022115 scopus 로고    scopus 로고
    • Molybdenum Cofactor Deficiency: Report of Three Cases Presenting as Hypoxic-Ischemic Encephalopathy
    • Topcu, M., Coskun, T., Haliloglu, G., and Saatci, I. (2001) Molybdenum Cofactor Deficiency: Report of Three Cases Presenting as Hypoxic-Ischemic Encephalopathy. J. Child Neurol. 16, 264-270.
    • (2001) J. Child Neurol , vol.16 , pp. 264-270
    • Topcu, M.1    Coskun, T.2    Haliloglu, G.3    Saatci, I.4
  • 17
    • 0037035536 scopus 로고    scopus 로고
    • Effect of Solution Viscosity on Intramolecular Electron Transfer in Sulfite Oxidase
    • Feng, C., Kedia, R. V., Hazzard, J. T., Hurley, J. K., Tollin, G., and Enemark, J. H. (2002) Effect of Solution Viscosity on Intramolecular Electron Transfer in Sulfite Oxidase. Biochemistry 41, 5816-5821.
    • (2002) Biochemistry , vol.41 , pp. 5816-5821
    • Feng, C.1    Kedia, R.V.2    Hazzard, J.T.3    Hurley, J.K.4    Tollin, G.5    Enemark, J.H.6
  • 18
    • 0345724820 scopus 로고    scopus 로고
    • Intramolecular Electron Transfer in a Bacterial Sulfite Dehydrogenase
    • Feng, C., Kappler, U., Tollin, G., and Enemark, J. H. (2003) Intramolecular Electron Transfer in a Bacterial Sulfite Dehydrogenase. J. Am. Chem. Soc. 125, 14696-14697.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 14696-14697
    • Feng, C.1    Kappler, U.2    Tollin, G.3    Enemark, J.H.4
  • 20
    • 0033523919 scopus 로고    scopus 로고
    • Natural Engineering Principles of Electron Tunnelling in Biological Oxidation-Reduction
    • Page, C. C., Moser, C. C., Chen, X., and Dutton, P. L. (1999) Natural Engineering Principles of Electron Tunnelling in Biological Oxidation-Reduction. Nature 402, 47-52.
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 21
    • 1442328094 scopus 로고    scopus 로고
    • Electron Tunneling through Proteins
    • Gray, H. B., and Winkler, J. R. (2003) Electron Tunneling through Proteins. Q. Rev. Biophys. 36, 341-372.
    • (2003) Q. Rev. Biophys , vol.36 , pp. 341-372
    • Gray, H.B.1    Winkler, J.R.2
  • 22
    • 0142031492 scopus 로고    scopus 로고
    • Essential Role of Conserved Arginine 160 in Intramolecular Electron Transfer in Human Sulfite Oxidase
    • Feng, C., Wilson, H. L., Hurley, J. K., Hazzard, J. T., Tollin, G., Rajagopalan, K. V., and Enemark, J. H. (2003) Essential Role of Conserved Arginine 160 in Intramolecular Electron Transfer in Human Sulfite Oxidase. Biochemistry 42, 12235-12242.
    • (2003) Biochemistry , vol.42 , pp. 12235-12242
    • Feng, C.1    Wilson, H.L.2    Hurley, J.K.3    Hazzard, J.T.4    Tollin, G.5    Rajagopalan, K.V.6    Enemark, J.H.7
  • 23
    • 0032837245 scopus 로고    scopus 로고
    • The pH Dependence of Intramolecular Electron Transfer Rates in Sulfite Oxidase at High and Low Anion Concentrations
    • Pacheco, A., Hazzard, J. T., Tollin, G., and Enemark, J. H. (1999) The pH Dependence of Intramolecular Electron Transfer Rates in Sulfite Oxidase at High and Low Anion Concentrations. J. Biol. Inorg. Chem. 4, 390-401.
    • (1999) J. Biol. Inorg. Chem , vol.4 , pp. 390-401
    • Pacheco, A.1    Hazzard, J.T.2    Tollin, G.3    Enemark, J.H.4
  • 24
    • 0027490582 scopus 로고
    • Electron Transfer in Sulfite Oxidase: Effects of pH and Anions on Transient Kinetics
    • Sullivan, E. P., Jr., Hazzard, J. T., Tollin, G., and Enemark, J. H. (1993) Electron Transfer in Sulfite Oxidase: Effects of pH and Anions on Transient Kinetics. Biochemistry 32, 12465-12470.
    • (1993) Biochemistry , vol.32 , pp. 12465-12470
    • Sullivan Jr., E.P.1    Hazzard, J.T.2    Tollin, G.3    Enemark, J.H.4
  • 25
    • 0037921276 scopus 로고
    • Inhibition of Intramolecular Electron Transfer in Sulfite Oxidase by Anion Binding
    • Sullivan, E. P., Jr., Hazzard, J. T., Tollin, G., and Enemark, J. H. (1992) Inhibition of Intramolecular Electron Transfer in Sulfite Oxidase by Anion Binding. J. Am. Chem. Soc. 114, 9662-9663.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 9662-9663
    • Sullivan Jr., E.P.1    Hazzard, J.T.2    Tollin, G.3    Enemark, J.H.4
  • 26
    • 59049086460 scopus 로고    scopus 로고
    • Molecular Basis for Enzymatic Sulfite Oxidation: How Three Conserved Active Site Residues Shape Enzyme Activity
    • Bailey, S., Rapson, T., Johnson-Winters, K., Enemark, J. H., and Kappler, U. (2009) Molecular Basis for Enzymatic Sulfite Oxidation: How Three Conserved Active Site Residues Shape Enzyme Activity. J. Biol. Chem. 284, 2053-2063.
    • (2009) J. Biol. Chem , vol.284 , pp. 2053-2063
    • Bailey, S.1    Rapson, T.2    Johnson-Winters, K.3    Enemark, J.H.4    Kappler, U.5
  • 27
    • 33747485989 scopus 로고    scopus 로고
    • Kinetic and Structural Evidence for the Importance of Tyr236 for the Integrity of the Mo Active Site in a Bacterial Sulfite Dehydrogenase
    • Kappler, U., Bailey, S., Feng, C., Honeychurch, M. J., Hanson, G. R., Bernhardt, P. V., Tollin, G., and Enemark, J. H. (2006) Kinetic and Structural Evidence for the Importance of Tyr236 for the Integrity of the Mo Active Site in a Bacterial Sulfite Dehydrogenase. Biochemistry 45, 9696-9705.
    • (2006) Biochemistry , vol.45 , pp. 9696-9705
    • Kappler, U.1    Bailey, S.2    Feng, C.3    Honeychurch, M.J.4    Hanson, G.R.5    Bernhardt, P.V.6    Tollin, G.7    Enemark, J.H.8
  • 28
    • 0037048677 scopus 로고    scopus 로고
    • A System for the Heterologous Expression of Complex Redox Proteins in Rhodobacter capsulatus: Characterisation of Recombinant Sulphite: Cytochrome c Oxidoreductase from Starkeya novella
    • Kappler, U., and McEwan, A. G (2002) A System for the Heterologous Expression of Complex Redox Proteins in Rhodobacter capsulatus: Characterisation of Recombinant Sulphite: Cytochrome c Oxidoreductase from Starkeya novella. FEBS Lett. 529, 208-214.
    • (2002) FEBS Lett , vol.529 , pp. 208-214
    • Kappler, U.1    McEwan, A.G.2
  • 29
    • 1342325440 scopus 로고    scopus 로고
    • Cytochrome c551 from Starkeya Novella: Characterization, Spectroscopic Properties, and Phylogeny of a Diheme Protein of the SoxAX Family
    • Kappler, U., Aguey-Zinsou, K. F., Hanson, G R., Bernhardt, P. V., and McEwan, A. G. (2004) Cytochrome c551 from Starkeya Novella: Characterization, Spectroscopic Properties, and Phylogeny of a Diheme Protein of the SoxAX Family. J. Biol. Chem. 279, 6252-6260.
    • (2004) J. Biol. Chem , vol.279 , pp. 6252-6260
    • Kappler, U.1    Aguey-Zinsou, K.F.2    Hanson, G.R.3    Bernhardt, P.V.4    McEwan, A.G.5
  • 30
    • 28144438785 scopus 로고    scopus 로고
    • The Nature of Aqueous Tunneling Pathways between Electron-Transfer Proteins
    • Lin, J., Balabin, I. A., and Beratan, D. N. (2005) The Nature of Aqueous Tunneling Pathways between Electron-Transfer Proteins. Science 310, 1311-1313.
    • (2005) Science , vol.310 , pp. 1311-1313
    • Lin, J.1    Balabin, I.A.2    Beratan, D.N.3
  • 32
    • 0036026536 scopus 로고    scopus 로고
    • Insights from Protein Film Voltammetry into Mechanisms of Complex Biological Electron-Transfer Reactions
    • Armstrong, F. (2002) Insights from Protein Film Voltammetry into Mechanisms of Complex Biological Electron-Transfer Reactions. J. Chem. Soc., Dalton Trans., 661.
    • (2002) J. Chem. Soc., Dalton Trans , pp. 661
    • Armstrong, F.1
  • 33
    • 0037010013 scopus 로고    scopus 로고
    • A Voltammetric Study of Interdomain Electron Transfer within Sulfite Oxidase
    • Elliott, S. J., McElhaney, A. E., Feng, C., Enemark, J. H., and Armstrong, F. A. (2002) A Voltammetric Study of Interdomain Electron Transfer within Sulfite Oxidase. J. Am. Chem. Soc. 124, 11612-11613.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 11612-11613
    • Elliott, S.J.1    McElhaney, A.E.2    Feng, C.3    Enemark, J.H.4    Armstrong, F.A.5
  • 34
    • 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
  • 37
    • 24644468183 scopus 로고    scopus 로고
    • Interference, Fluctuation, and Alternation of Electron Tunneling in Protein Media. 2. Non-Condon Theory for the Energy Gap Dependence of Electron Transfer Rate
    • Nishioka, H., Kimura, A., Yamato, T., Kawatsu, T., and Kakitani, T. (2005) Interference, Fluctuation, and Alternation of Electron Tunneling in Protein Media. 2. Non-Condon Theory for the Energy Gap Dependence of Electron Transfer Rate. J. Phys. Chem. B 109, 15621-15635.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 15621-15635
    • Nishioka, H.1    Kimura, A.2    Yamato, T.3    Kawatsu, T.4    Kakitani, T.5
  • 38
    • 13544270860 scopus 로고    scopus 로고
    • Interference, Fluctuation, and Alternation of Electron Tunneling in Protein Media. 1. Two Tunneling Routes in Photo-synthetic Reaction Center Alternate due to Thermal Fluctuation of Protein Conformation
    • Nishioka, H., Kimura, A., Yamato, T., Kawatsu, T., and Kakitani, T. (2005) Interference, Fluctuation, and Alternation of Electron Tunneling in Protein Media. 1. Two Tunneling Routes in Photo-synthetic Reaction Center Alternate due to Thermal Fluctuation of Protein Conformation. J. Phys. Chem. B 109, 1978-1987.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 1978-1987
    • Nishioka, H.1    Kimura, A.2    Yamato, T.3    Kawatsu, T.4    Kakitani, T.5
  • 39
    • 50549083141 scopus 로고    scopus 로고
    • Average Electron Tunneling Route of the Electron Transfer in Protein Media
    • Nishioka, H., and Kakitani, T. (2008) Average Electron Tunneling Route of the Electron Transfer in Protein Media. J. Phys. Chem. B 112, 9948-9958.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9948-9958
    • Nishioka, H.1    Kakitani, T.2
  • 40
    • 54049095896 scopus 로고    scopus 로고
    • Persistence of Structure Over Fluctuations in Biological Electron-Transfer Reactions
    • Balabin, I. A., Beratan, D. N., and Skourtis, S. S. (2008) Persistence of Structure Over Fluctuations in Biological Electron-Transfer Reactions. Phys. Rev. Lett. 101, 158102.
    • (2008) Phys. Rev. Lett , vol.101 , pp. 158102
    • Balabin, I.A.1    Beratan, D.N.2    Skourtis, S.S.3


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