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Volumn 47, Issue 41, 2008, Pages 10852-10862

Electron transfer complex between nitrous oxide reductase and cytochrome c552 from Pseudomonas nautica: Kinetic, nuclear magnetic resonance, and docking studies

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[No Author keywords available]

Indexed keywords

ANESTHETICS;

EID: 53749097472     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801375q     Document Type: Article
Times cited : (43)

References (50)
  • 4
  • 5
    • 33747351535 scopus 로고    scopus 로고
    • Insight into catalysis of nitrous oxide reductase from high-resolution structures of resting and inhibitor-bound enzyme from Achromobacter cycloclastes
    • Paraskevopoulos, K., Antonyuk, S. V., Sawers, R. G., Eady, R. R., and Hasnain, S. S. (2006) Insight into catalysis of nitrous oxide reductase from high-resolution structures of resting and inhibitor-bound enzyme from Achromobacter cycloclastes. J. Mol. Biol. 362, 55-65.
    • (2006) J. Mol. Biol , vol.362 , pp. 55-65
    • Paraskevopoulos, K.1    Antonyuk, S.V.2    Sawers, R.G.3    Eady, R.R.4    Hasnain, S.S.5
  • 6
    • 0034026215 scopus 로고    scopus 로고
    • Electron tunneling pathways in proteins
    • Winkler, J. R. (2000) Electron tunneling pathways in proteins. Curr. Opin. Chem. Biol. 4, 192-198.
    • (2000) Curr. Opin. Chem. Biol , vol.4 , pp. 192-198
    • Winkler, J.R.1
  • 7
    • 0024964611 scopus 로고
    • The nature of the cupric site in nitrous oxide reductase and of CuA in cytochrome c oxidase
    • Kroneck, P. M., Antholine, W. A., Riester, J., and Zumft, W. G. (1989) The nature of the cupric site in nitrous oxide reductase and of CuA in cytochrome c oxidase. FEBS Lett. 248, 212-213.
    • (1989) FEBS Lett , vol.248 , pp. 212-213
    • Kroneck, P.M.1    Antholine, W.A.2    Riester, J.3    Zumft, W.G.4
  • 8
    • 0032543960 scopus 로고    scopus 로고
    • CuA and CuZ are variants of the electron transfer center in nitrous oxide reductase
    • Farrar, J. A., Zumft, W. G., and Thomson, A. J. (1998) CuA and CuZ are variants of the electron transfer center in nitrous oxide reductase. Proc. Natl. Acad. Sci. U.S.A. 95, 9891-9896.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 9891-9896
    • Farrar, J.A.1    Zumft, W.G.2    Thomson, A.J.3
  • 9
    • 0029102256 scopus 로고
    • Spectroscopic and mutagenesis studies on the CuA centre from the cytochrome-c oxidase complex of Paracoccus denitrificans
    • Farrar, J. A., Lappalainen, P., Zumft, W. G., Saraste, M., and Thomson, A. J. (1995) Spectroscopic and mutagenesis studies on the CuA centre from the cytochrome-c oxidase complex of Paracoccus denitrificans. Eur. J. Biochem. 232, 294-303.
    • (1995) Eur. J. Biochem , vol.232 , pp. 294-303
    • Farrar, J.A.1    Lappalainen, P.2    Zumft, W.G.3    Saraste, M.4    Thomson, A.J.5
  • 11
    • 0037096979 scopus 로고    scopus 로고
    • Multiple forms of the catalytic centre, CuZ, in the enzyme nitrous oxide reductase from Paracoccus pantotrophus
    • Rasmussen, T., Berks, B. C., Butt, J. N., and Thomson, A. J. (2002) Multiple forms of the catalytic centre, CuZ, in the enzyme nitrous oxide reductase from Paracoccus pantotrophus. Biochem. J. 364, 807-815.
    • (2002) Biochem. J , vol.364 , pp. 807-815
    • Rasmussen, T.1    Berks, B.C.2    Butt, J.N.3    Thomson, A.J.4
  • 16
    • 1642407786 scopus 로고    scopus 로고
    • Reductively activated nitrous oxide reductase reacts directly with substrate
    • Chan, J. M., Bollinger, J. A., Grewell, C. L., and Dooley, D. M. (2004) Reductively activated nitrous oxide reductase reacts directly with substrate. J. Am. Chem. Soc. 126, 3030-3031.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 3030-3031
    • Chan, J.M.1    Bollinger, J.A.2    Grewell, C.L.3    Dooley, D.M.4
  • 17
    • 35348827900 scopus 로고    scopus 로고
    • Anaerobic purification, characterization and preliminary mechanistic study of recombinant nitrous oxide reductase from Achromobacter cycloclastes
    • Fujita, K., Chan, J. M., Bollinger, J. A., Alvarez, M. L., and Dooley, D. M. (2007) Anaerobic purification, characterization and preliminary mechanistic study of recombinant nitrous oxide reductase from Achromobacter cycloclastes. J. Inorg. Biochem. 101, 1836-1844.
    • (2007) J. Inorg. Biochem , vol.101 , pp. 1836-1844
    • Fujita, K.1    Chan, J.M.2    Bollinger, J.A.3    Alvarez, M.L.4    Dooley, D.M.5
  • 18
    • 0027476458 scopus 로고
    • Purification and characterization of a nitrous oxide reductase from Thiosphaera pantotropha. Implications for the mechanism of aerobic nitrous oxide reduction
    • Berks, B. C., Baratta, D., Richardson, J., and Ferguson, S. J. (1993) Purification and characterization of a nitrous oxide reductase from Thiosphaera pantotropha. Implications for the mechanism of aerobic nitrous oxide reduction. Eur. J. Biochem. 212, 467-476.
    • (1993) Eur. J. Biochem , vol.212 , pp. 467-476
    • Berks, B.C.1    Baratta, D.2    Richardson, J.3    Ferguson, S.J.4
  • 19
    • 0025923259 scopus 로고
    • Cytochrome c2 is essential for electron transfer to nitrous oxide reductase from physiological substrates in Rhodobacter capsulatus and can act as an electron donor to the reductase in vitro. Correlation with photoinhibition studies
    • Richardson, D. J., Bell, L. C., McEwan, A. G., Jackson, J. B., and Ferguson, S. J. (1991) Cytochrome c2 is essential for electron transfer to nitrous oxide reductase from physiological substrates in Rhodobacter capsulatus and can act as an electron donor to the reductase in vitro. Correlation with photoinhibition studies. Eur. J. Biochem. 199, 677-683.
    • (1991) Eur. J. Biochem , vol.199 , pp. 677-683
    • Richardson, D.J.1    Bell, L.C.2    McEwan, A.G.3    Jackson, J.B.4    Ferguson, S.J.5
  • 20
    • 0027273523 scopus 로고
    • The reaction of reduced cytochromes c with nitrous oxide reductase ot Wolinella succinogenes
    • Zhang, C. S., and Hollocher, T. C. (1993) The reaction of reduced cytochromes c with nitrous oxide reductase ot Wolinella succinogenes. Biochim. Biophys. Acta 1142, 253-261.
    • (1993) Biochim. Biophys. Acta , vol.1142 , pp. 253-261
    • Zhang, C.S.1    Hollocher, T.C.2
  • 22
    • 0142183483 scopus 로고    scopus 로고
    • A Mutant of Paracoccus denitrificans with Disrupted Genes Coding for Cytochrome c550 and Pseudoazurin Establishes These Two Proteins as the In Vivo Electron Donors to Cytochrome cdl Nitrite Reductase
    • Pearson, I. V., Page, M. D., van Spanning, R. J. M., and Ferguson, S. J. (2003) A Mutant of Paracoccus denitrificans with Disrupted Genes Coding for Cytochrome c550 and Pseudoazurin Establishes These Two Proteins as the In Vivo Electron Donors to Cytochrome cdl Nitrite Reductase. J. Bacteriol. 185, 6308-6315.
    • (2003) J. Bacteriol , vol.185 , pp. 6308-6315
    • Pearson, I.V.1    Page, M.D.2    van Spanning, R.J.M.3    Ferguson, S.J.4
  • 23
    • 18844413338 scopus 로고    scopus 로고
    • How does nitrous oxide reductase interact with its electron donors? A docking study
    • Mattila, K., and Haltia, T. (2005) How does nitrous oxide reductase interact with its electron donors? A docking study. Proteins 59, 708-722.
    • (2005) Proteins , vol.59 , pp. 708-722
    • Mattila, K.1    Haltia, T.2
  • 25
    • 0000481224 scopus 로고
    • Caractérisation préliminaire du système cytochromique de la bactérie marine dénitricante Pseudomonas nautica 617.
    • Fauque, G M. J., Besson, S., Saraiva, L., and Moura, I. (1992) Caractérisation préliminaire du système cytochromique de la bactérie marine dénitricante Pseudomonas nautica 617. Oceanis 18, 211-216.
    • (1992) Oceanis , vol.18 , pp. 211-216
    • Fauque, G.M.J.1    Besson, S.2    Saraiva, L.3    Moura, I.4
  • 26
    • 0029088401 scopus 로고
    • Purification and preliminary characterization of three c-type cytochromes from Pseudomonas nautica strain 617
    • Saraiva, L. M., Besson, S., Moura, I., and Fauque, G. (1995) Purification and preliminary characterization of three c-type cytochromes from Pseudomonas nautica strain 617. Biochem. Biophys. Res. Commun. 212, 1088-1097.
    • (1995) Biochem. Biophys. Res. Commun , vol.212 , pp. 1088-1097
    • Saraiva, L.M.1    Besson, S.2    Moura, I.3    Fauque, G.4
  • 27
    • 0028050131 scopus 로고
    • Physico-chemical and spectroscopic properties of the monohemic cytochrome C552 from Pseudomonas nautica 617
    • Saraiva, L. M., Fauque, G., Besson, S., and Moura, I. (1994) Physico-chemical and spectroscopic properties of the monohemic cytochrome C552 from Pseudomonas nautica 617. Eur. J. Biochem. 224, 1011-1017.
    • (1994) Eur. J. Biochem , vol.224 , pp. 1011-1017
    • Saraiva, L.M.1    Fauque, G.2    Besson, S.3    Moura, I.4
  • 28
    • 0028291355 scopus 로고
    • Characterization of the dihemic cytochrome c549 from the marine denitrifying bacterium Pseudomonas nautica 617
    • Saraiva, L. M., Besson, S., Fauque, G., and Moura, I. (1994) Characterization of the dihemic cytochrome c549 from the marine denitrifying bacterium Pseudomonas nautica 617. Biochem. Biophys. Res. Commun. 199, 1289-1296.
    • (1994) Biochem. Biophys. Res. Commun , vol.199 , pp. 1289-1296
    • Saraiva, L.M.1    Besson, S.2    Fauque, G.3    Moura, I.4
  • 29
    • 23544450428 scopus 로고
    • The extinction coefficient of cytochrome c
    • Van Gelder, B. F., and Slater, E. C. (1962) The extinction coefficient of cytochrome c. Biochim. Biophys. Acta 58, 593-595.
    • (1962) Biochim. Biophys. Acta , vol.58 , pp. 593-595
    • Van Gelder, B.F.1    Slater, E.C.2
  • 30
    • 0019332115 scopus 로고
    • First practical assay for soluble nitrous oxide reductase of denitrifying bacteria and a partial kinetic characterization
    • Kristjansson, J. K., and Hollocher, T. C. (1980) First practical assay for soluble nitrous oxide reductase of denitrifying bacteria and a partial kinetic characterization. J. Biol. Chem. 255, 704-707.
    • (1980) J. Biol. Chem , vol.255 , pp. 704-707
    • Kristjansson, J.K.1    Hollocher, T.C.2
  • 32
    • 0034212826 scopus 로고    scopus 로고
    • BiGGER: A new (soft) docking algorithm for predicting protein interactions
    • Palma, P. N., Krippahl, L., Wampler, J. E., and Moura, J. J. (2000) BiGGER: A new (soft) docking algorithm for predicting protein interactions. Proteins 39, 372-384.
    • (2000) Proteins , vol.39 , pp. 372-384
    • Palma, P.N.1    Krippahl, L.2    Wampler, J.E.3    Moura, J.J.4
  • 33
  • 35
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte, L., Chothia, C., and Janin, J. (1999) The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285, 2177-2198.
    • (1999) J. Mol. Biol , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 36
    • 0034846778 scopus 로고    scopus 로고
    • Kinetics of inter- and intramolecular electron transfer of Pseudomonas nautica cytochrome cd1 nitrite reductase: Regulation of the NO-bound end product
    • Lopes, H., Besson, S., Moura, I., and Moura, J. J. (2001) Kinetics of inter- and intramolecular electron transfer of Pseudomonas nautica cytochrome cd1 nitrite reductase: Regulation of the NO-bound end product. J. Biol. Inorg. Chem. 6, 55-62.
    • (2001) J. Biol. Inorg. Chem , vol.6 , pp. 55-62
    • Lopes, H.1    Besson, S.2    Moura, I.3    Moura, J.J.4
  • 40
    • 1342304268 scopus 로고    scopus 로고
    • Characterization of Nitrous Oxide Reductase from a Methylotrophic Denitrifying Bacterium, Hyphomicrobium denitrificans A3151
    • Yamaguchi, K., Kawamura, A., Ogawa, H., and Suzuki, S. (2003) Characterization of Nitrous Oxide Reductase from a Methylotrophic Denitrifying Bacterium, Hyphomicrobium denitrificans A3151. J. Biochem. 134, 853-858.
    • (2003) J. Biochem , vol.134 , pp. 853-858
    • Yamaguchi, K.1    Kawamura, A.2    Ogawa, H.3    Suzuki, S.4
  • 41
    • 0346510924 scopus 로고    scopus 로고
    • Hyperfine shift and relaxation in the presence of chemical exchange
    • Bertini, I., and Luchinat, C. (1996) Hyperfine shift and relaxation in the presence of chemical exchange. Coord. Chem. Rev. 150, 111-130.
    • (1996) Coord. Chem. Rev , vol.150 , pp. 111-130
    • Bertini, I.1    Luchinat, C.2
  • 42
    • 2442610947 scopus 로고    scopus 로고
    • The architecture of the binding site in redox protein complexes: Implications for fast dissociation
    • Crowley, P. B., and Carrondo, M. A. (2004) The architecture of the binding site in redox protein complexes: Implications for fast dissociation. Proteins 55, 603-612.
    • (2004) Proteins , vol.55 , pp. 603-612
    • Crowley, P.B.1    Carrondo, M.A.2
  • 43
    • 0028799023 scopus 로고
    • Pseudospecific docking surfaces on electron transfer proteins as illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1 nitrite reductase
    • Williams, P. A., Fulop, V., Leung, Y. C., Chan, C., Moir, J. W., Howlett, G., Ferguson, S. J., Radford, S. E., and Hajdu, J. (1995) Pseudospecific docking surfaces on electron transfer proteins as illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1 nitrite reductase. Nat. Struct. Biol. 2, 975-982.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 975-982
    • Williams, P.A.1    Fulop, V.2    Leung, Y.C.3    Chan, C.4    Moir, J.W.5    Howlett, G.6    Ferguson, S.J.7    Radford, S.E.8    Hajdu, J.9
  • 44
    • 0032570589 scopus 로고    scopus 로고
    • Tryptophan 121 of Subunit II Is the Electron Entry Site to Cytochrome-c Oxidase in Paracoccus denitrificans. Involvement of a Hydrophobic Patch in the Docking Reaction
    • Witt, H., Malatesta, F., Nicoletti, F., Brunori, M., and Ludwig, B. (1998) Tryptophan 121 of Subunit II Is the Electron Entry Site to Cytochrome-c Oxidase in Paracoccus denitrificans. Involvement of a Hydrophobic Patch in the Docking Reaction. J. Biol. Chem. 273, 5132-5136.
    • (1998) J. Biol. Chem , vol.273 , pp. 5132-5136
    • Witt, H.1    Malatesta, F.2    Nicoletti, F.3    Brunori, M.4    Ludwig, B.5
  • 45
    • 0028958832 scopus 로고
    • Identification of interaction site of pseudoazurin with its redox partner, copper-containing nitrite reductase from Alcaligenes faecalis S-6
    • Kukimoto, M., Nishiyama, M., Ohnuki, T., Turley, S., Adman, E. T., Horinouchi, S., and Beppu, T. (1995) Identification of interaction site of pseudoazurin with its redox partner, copper-containing nitrite reductase from Alcaligenes faecalis S-6. Protein Eng. 8, 153-158.
    • (1995) Protein Eng , vol.8 , pp. 153-158
    • Kukimoto, M.1    Nishiyama, M.2    Ohnuki, T.3    Turley, S.4    Adman, E.T.5    Horinouchi, S.6    Beppu, T.7
  • 47
    • 8644248150 scopus 로고    scopus 로고
    • Mechanistic insight into the catechol oxidase activity by a biomimetic dinuclear copper complex
    • Granata, A., Monzani, E., and Casella, L. (2004) Mechanistic insight into the catechol oxidase activity by a biomimetic dinuclear copper complex. J. Biol. Inorg. Chem. 9, 903-913.
    • (2004) J. Biol. Inorg. Chem , vol.9 , pp. 903-913
    • Granata, A.1    Monzani, E.2    Casella, L.3
  • 48
    • 0000298228 scopus 로고
    • Hemocyanin and tyrosinase models. Synthesis, azide binding, and electrochemistry of dinuclear copper(II) complexes with poly(benzimidazole) ligands modeling the met forms of the proteins
    • Casella, L., Carugo, O., Gullotti, M., Garofani, S., and Zanello, P. (1993) Hemocyanin and tyrosinase models. Synthesis, azide binding, and electrochemistry of dinuclear copper(II) complexes with poly(benzimidazole) ligands modeling the met forms of the proteins. Inorg. Chem. 32, 2056-2067.
    • (1993) Inorg. Chem , vol.32 , pp. 2056-2067
    • Casella, L.1    Carugo, O.2    Gullotti, M.3    Garofani, S.4    Zanello, P.5
  • 49
    • 0034617617 scopus 로고    scopus 로고
    • pH-Controlled Change of the Metal Coordination in a Dicopper(II) Complex of the Ligand H-BPMP: Crystal Structures, Magnetic Properties, and Catecholase Activity
    • Torelli, S., Belle, C., Gautier-Luneau, I., Pierre, J. L., Saint-Aman, E., Latour, J. M., Le Pape, L., and Luneau, D. (2000) pH-Controlled Change of the Metal Coordination in a Dicopper(II) Complex of the Ligand H-BPMP: Crystal Structures, Magnetic Properties, and Catecholase Activity. Inorg. Chem. 39, 3526-3536.
    • (2000) Inorg. Chem , vol.39 , pp. 3526-3536
    • Torelli, S.1    Belle, C.2    Gautier-Luneau, I.3    Pierre, J.L.4    Saint-Aman, E.5    Latour, J.M.6    Le Pape, L.7    Luneau, D.8


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