메뉴 건너뛰기




Volumn 151, Issue 5, 2012, Pages 483-492

A new structural insight into differential interaction of cyanobacterial and plant ferredoxins with nitrite reductase as revealed by NMR and X-ray crystallographic studies

Author keywords

electron transfer; Ferredoxin; nitrite reductase; protein protein interaction

Indexed keywords

FERREDOXIN NITRITE REDUCTASE;

EID: 84860434830     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvs028     Document Type: Article
Times cited : (26)

References (37)
  • 1
    • 0842264043 scopus 로고    scopus 로고
    • A post genomic characterization of Arabidopsis ferredoxins
    • Hanke, G.T., Kimata-Ariga, Y., Taniguchi, I., and Hase, T. (2004) A post genomic characterization of Arabidopsis ferredoxins. Plant Physiol. 134, 255-264
    • (2004) Plant Physiol. , vol.134 , pp. 255-264
    • Hanke, G.T.1    Kimata-Ariga, Y.2    Taniguchi, I.3    Hase, T.4
  • 3
    • 4043169726 scopus 로고    scopus 로고
    • Structure and function of plant-type ferredoxins
    • Fukuyama, K. (2004) Structure and function of plant-type ferredoxins. Photosynth. Res. 81, 289-301
    • (2004) Photosynth. Res. , vol.81 , pp. 289-301
    • Fukuyama, K.1
  • 4
    • 0032213789 scopus 로고    scopus 로고
    • Structure of the mutant E92K of [2Fe-2S] ferredoxin i from Spinacia oleracea at 1.7 A resolution
    • Binda, C, Coda, A., Aliverti, A., Zanetti, G., and Mattevi, A. (1998) Structure of the mutant E92K of [2Fe-2S] ferredoxin I from Spinacia oleracea at 1.7 A resolution. Acta Crystallogr. D Biol. Crystallogr. 54, 1353-1358
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 1353-1358
    • Binda, C.1    Coda, A.2    Aliverti, A.3    Zanetti, G.4    Mattevi, A.5
  • 5
    • 34447120818 scopus 로고    scopus 로고
    • Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase
    • Dai, S., Friemann, R., Glauser, D.A., Bourquin, F., Manieri, W., Schurmann, P., and Eklund, H. (2007) Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase. Nature 448, 92-96
    • (2007) Nature , vol.448 , pp. 92-96
    • Dai, S.1    Friemann, R.2    Glauser, D.A.3    Bourquin, F.4    Manieri, W.5    Schurmann, P.6    Eklund, H.7
  • 6
    • 0037156873 scopus 로고    scopus 로고
    • Structure-function relationships in Anabaena fer-redoxin/ferredoxin: NADP(+) reductase electron transfer: Insights from site-directed mutagenesis, transient absorption spectroscopy and X-ray crystallography
    • Hurley, J.K., Morales, R., Martinez-Julvez, M., Brodie, T.B., Medina, M., Gomez-Moreno, C, and Tollin, G (2002) Structure-function relationships in Anabaena fer-redoxin/ferredoxin: NADP(+) reductase electron transfer: insights from site-directed mutagenesis, transient absorption spectroscopy and X-ray crystallography. Biochim. Biophys. Acta 1554, 5-21
    • (2002) Biochim. Biophys. Acta , vol.1554 , pp. 5-21
    • Hurley, J.K.1    Morales, R.2    Martinez-Julvez, M.3    Brodie, T.B.4    Medina, M.5    Gomez-Moreno, C.6    Tollin, G.7
  • 8
    • 0033731168 scopus 로고    scopus 로고
    • Crystallographic studies of the interaction between the ferredoxin-NADP+ reductase and ferredoxin from the cyanobacterium Anabaena: Looking for the elusive ferredoxin molecule
    • Morales, R., Kachalova, G, Vellieux, F., Charon, M.-H, and Frey, M. (2000) Crystallographic studies of the interaction between the ferredoxin-NADP+ reductase and ferredoxin from the cyanobacterium Anabaena: looking for the elusive ferredoxin molecule. Acta Crystallogr D Biol Crystallogr. 56, 1408-1412
    • (2000) Acta Crystallogr D Biol Crystallogr. , vol.56 , pp. 1408-1412
    • Morales, R.1    Kachalova, G.2    Vellieux, F.3    Charon, M.-H.4    Frey, M.5
  • 9
    • 33744515908 scopus 로고    scopus 로고
    • NMR study of the electron transfer complex of plant ferredoxin and sulfite reductase: Mapping the interaction sites of ferredoxin
    • Saitoh, T., Ikegami, T., Nakayama, M., Teshima, K., Akutsu, H., and Hase, T. (2006) NMR study of the electron transfer complex of plant ferredoxin and sulfite reductase: mapping the interaction sites of ferredoxin. J. Biol. Chem. 281, 10482-10488
    • (2006) J. Biol. Chem. , vol.281 , pp. 10482-10488
    • Saitoh, T.1    Ikegami, T.2    Nakayama, M.3    Teshima, K.4    Akutsu, H.5    Hase, T.6
  • 10
    • 34447127145 scopus 로고    scopus 로고
    • Ferredoxin/ferredoxin-thioredoxin reductase complex: Complete NMR mapping of the interaction site on ferredoxin by gallium substitution
    • Xu, X., Kim, S.K., Schurmann, P., Hirasawa, M., Tripathy, J.N., Smith, J., Knaff, D.B., and Ubbink, M. (2006) Ferredoxin/ferredoxin-thioredoxin reductase complex: complete NMR mapping of the interaction site on ferredoxin by gallium substitution. FEBS Lett. 580, 6714-6720
    • (2006) FEBS Lett. , vol.580 , pp. 6714-6720
    • Xu, X.1    Kim, S.K.2    Schurmann, P.3    Hirasawa, M.4    Tripathy, J.N.5    Smith, J.6    Knaff, D.B.7    Ubbink, M.8
  • 11
    • 0033911508 scopus 로고    scopus 로고
    • Differential interaction of maize root ferredoxin: NADP(+) oxidoreductase with photosynthetic and non-photosynthetic ferredoxin isoproteins
    • Onda, Y., Matsumura, T., Kimata-Ariga, Y., Sakakibara, H, Sugiyama, T., and Hase, T. (2000) Differential interaction of maize root ferredoxin: NADP(+) oxidoreductase with photosynthetic and non-photosynthetic ferredoxin isoproteins. Plant Physiol. 123, 1037-1045
    • (2000) Plant Physiol. , vol.123 , pp. 1037-1045
    • Onda, Y.1    Matsumura, T.2    Kimata-Ariga, Y.3    Sakakibara, H.4    Sugiyama, T.5    Hase, T.6
  • 12
    • 0032829695 scopus 로고    scopus 로고
    • Comparison of the electrostatic binding sites on the surface of ferredoxin for two ferredoxin-dependent enzymes, ferredoxin-NADP(+) reductase and sulfite reductase
    • Akashi, T., Matsumura, T., Ideguchi, T., Iwakiri, K, Kawakatsu, T., Taniguchi, I., and Hase, T. (1999) Comparison of the electrostatic binding sites on the surface of ferredoxin for two ferredoxin-dependent enzymes, ferredoxin-NADP(+) reductase and sulfite reductase. J. Biol. Chem. 274, 29399-29405
    • (1999) J. Biol. Chem. , vol.274 , pp. 29399-29405
    • Akashi, T.1    Matsumura, T.2    Ideguchi, T.3    Iwakiri, K.4    Kawakatsu, T.5    Taniguchi, I.6    Hase, T.7
  • 13
    • 0024553524 scopus 로고
    • Spinach ferredoxin-nitrite reductase: Characterization of catalytic activity and interaction of the enzyme with substrates
    • Mikami, B. and Ida, S. (1989) Spinach ferredoxin-nitrite reductase: characterization of catalytic activity and interaction of the enzyme with substrates. J. Biochem. 105, 47-50
    • (1989) J. Biochem. , vol.105 , pp. 47-50
    • Mikami, B.1    Ida, S.2
  • 14
    • 0346463125 scopus 로고    scopus 로고
    • Mechanism of spinach chloro-plast ferredoxin-dependent nitrite reductase: Spectro-scopic evidence for intermediate states
    • Kuznetsova, S., Knaff, D.B., Hirasawa, M., Lagoutte, B., and Setif, P. (2004) Mechanism of spinach chloro-plast ferredoxin-dependent nitrite reductase: spectro-scopic evidence for intermediate states. Biochemistry 43, 510-517
    • (2004) Biochemistry , vol.43 , pp. 510-517
    • Kuznetsova, S.1    Knaff, D.B.2    Hirasawa, M.3    Lagoutte, B.4    Setif, P.5
  • 15
    • 4143146335 scopus 로고    scopus 로고
    • Reactions of spinach nitrite reductase with its substrate, nitrite, and a putative intermediate, hydroxylamine
    • Kuznetsova, S., Knaff, D.B., Hirasawa, M., Setif, P., and Mattioli, T.A. (2004) Reactions of spinach nitrite reductase with its substrate, nitrite, and a putative intermediate, hydroxylamine. Biochemistry 43, 10765-10774
    • (2004) Biochemistry , vol.43 , pp. 10765-10774
    • Kuznetsova, S.1    Knaff, D.B.2    Hirasawa, M.3    Setif, P.4    Mattioli, T.A.5
  • 16
    • 1042290466 scopus 로고    scopus 로고
    • Oxidation-reduction properties of maize ferredoxin: Sulfite oxidoreductase
    • Hirasawa, M., Nakayama, M., Hase, T., and Knaff, D.B. (2004) Oxidation-reduction properties of maize ferredoxin: sulfite oxidoreductase. Biochim. Biophys. Acta 1608, 140-148
    • (2004) Biochim. Biophys. Acta , vol.1608 , pp. 140-148
    • Hirasawa, M.1    Nakayama, M.2    Hase, T.3    Knaff, D.B.4
  • 17
    • 28944439659 scopus 로고    scopus 로고
    • Structure of spinach nitrite reductase: Implications for multi-electron reactions by the iron-sulfur:siroheme co-factor
    • Swamy, U., Wang, M., Tripathy, J.N., Kim, S.K., Hirasawa, M., Knaff, D.B., and Allen, J.P. (2005) Structure of spinach nitrite reductase: implications for multi-electron reactions by the iron-sulfur:siroheme co-factor. Biochemistry 44, 16054-16063
    • (2005) Biochemistry , vol.44 , pp. 16054-16063
    • Swamy, U.1    Wang, M.2    Tripathy, J.N.3    Kim, S.K.4    Hirasawa, M.5    Knaff, D.B.6    Allen, J.P.7
  • 18
    • 70349768785 scopus 로고    scopus 로고
    • A novel variant of ferredoxin-dependent sulfite reductase having preferred substrate specificity for nitrite in the unicellular red alga Cyanidioschyzon merolae
    • Sekine, K, Sakakibara, Y., Hase, T., and Sato, N. (2009) A novel variant of ferredoxin-dependent sulfite reductase having preferred substrate specificity for nitrite in the unicellular red alga Cyanidioschyzon merolae. Biochem. J. 423, 91-98
    • (2009) Biochem. J. , vol.423 , pp. 91-98
    • Sekine, K.1    Sakakibara, Y.2    Hase, T.3    Sato, N.4
  • 20
    • 0034596917 scopus 로고    scopus 로고
    • Differential electron flow around photosystem i by two C-4-photosynthetic-cell-specific ferredoxins
    • Kimata-Ariga, Y., Matsumura, T., Kada, S., Fujimoto, H., Fujita, Y., Endo, T., Mano, J., Sato, F., and Hase, T. (2000) Differential electron flow around photosystem I by two C-4-photosynthetic-cell-specific ferredoxins. EMBO J. 19, 5041-5050
    • (2000) EMBO J. , vol.19 , pp. 5041-5050
    • Kimata-Ariga, Y.1    Matsumura, T.2    Kada, S.3    Fujimoto, H.4    Fujita, Y.5    Endo, T.6    Mano, J.7    Sato, F.8    Hase, T.9
  • 21
    • 0003022798 scopus 로고
    • Molecular-cloning and differential expression of the maize ferredoxin gene family
    • Hase, T., Kimata, Y., Yonekura, K, Matsumura, T., and Sakakibara, H. (1991) Molecular-cloning and differential expression of the maize ferredoxin gene family. Plant Physiol. 96, 77-83
    • (1991) Plant Physiol. , vol.96 , pp. 77-83
    • Hase, T.1    Kimata, Y.2    Yonekura, K.3    Matsumura, T.4    Sakakibara, H.5
  • 23
    • 0025082839 scopus 로고
    • Purification and some properties of the nitrite reductase from the cyanobacterium Phormidium laminosum
    • Arizmendi, J.M. and Serra, J.L. (1990) Purification and some properties of the nitrite reductase from the cyanobacterium Phormidium laminosum. Biochim. Biophys. Acta 1040, 237-244
    • (1990) Biochim. Biophys. Acta , vol.1040 , pp. 237-244
    • Arizmendi, J.M.1    Serra, J.L.2
  • 24
    • 0033777345 scopus 로고    scopus 로고
    • Analysis of reductant supply system for ferredoxin-dependent sulfite reductase in photosynthetic and non-photosynthetic organs of maize
    • Yonekura-Sakakibara, K., Onda, Y., Ashikari, T., Tanaka, Y., Kusumi, T., and Hase, T. (2000) Analysis of reductant supply system for ferredoxin-dependent sulfite reductase in photosynthetic and non-photosynthetic organs of maize. Plant Physiol. 122, 887-894
    • (2000) Plant Physiol. , vol.122 , pp. 887-894
    • Yonekura-Sakakibara, K.1    Onda, Y.2    Ashikari, T.3    Tanaka, Y.4    Kusumi, T.5    Hase, T.6
  • 25
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A. and Teplyakov, A. (1997) MOLREP: an automated program for molecular replacement. J. Appl. Cryst. 30, 1022-1025
    • (1997) J. Appl. Cryst. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 27
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 28
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 29
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • Dolinsky, T.J., Nielsen, J.E., McCammon, J.A., and Baker, N.A. (2004) PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res. 32, W665-W667
    • (2004) Nucleic Acids Res. , vol.32
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 30
    • 0002381679 scopus 로고
    • Enzyme-activities in an artificial stroma medium-an experimental-model for studying effects of dehydration on photosynthesis
    • Kaiser, W.M., Schroppelmeier, G, and Wirth, E. (1986) Enzyme-activities in an artificial stroma medium-an experimental-model for studying effects of dehydration on photosynthesis. Planta 167, 292-299
    • (1986) Planta , vol.167 , pp. 292-299
    • Kaiser, W.M.1    Schroppelmeier, G.2    Wirth, E.3
  • 31
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR Spectroscopy
    • Zuiderweg, E.R.P. (2002) Mapping protein-protein interactions in solution by NMR Spectroscopy. Biochemistry 41, 1-7
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.P.1
  • 32
    • 0029400480 scopus 로고
    • Nmrpipe - A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G, Pfeifer, J., and Bax, A. (1995) Nmrpipe-a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 33
    • 0004040543 scopus 로고    scopus 로고
    • University of California, San Francisco
    • Goddard, T.D. and Kneller, D.G (1999) SPARKY 3, University of California, San Francisco
    • (1999) SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 34
    • 0028103275 scopus 로고
    • The ccp4 suite-programs for protein crystallography
    • Bailey, S. (1994) The ccp4 suite-programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
    • Bailey, S.1
  • 36
    • 0027942020 scopus 로고
    • + reductase and the role of water at the complex interface
    • + reductase and the role of water at the complex interface. Biochemistry 33, 13321-13328
    • (1994) Biochemistry , vol.33 , pp. 13321-13328
    • Jelesarov, I.1    Bosshard, H.R.2
  • 37
    • 79960098090 scopus 로고    scopus 로고
    • Mapping of protein-protein interaction sites in the plant-type [2Fe-2S] ferredoxin
    • Kameda, H., Hirabayashi, K., Wada, K., and Fukuyama, K. (2011) Mapping of protein-protein interaction sites in the plant-type [2Fe-2S] ferredoxin. PLos One 6, e21947
    • (2011) PLos One , vol.6
    • Kameda, H.1    Hirabayashi, K.2    Wada, K.3    Fukuyama, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.