메뉴 건너뛰기




Volumn 2, Issue 3, 2009, Pages 407-415

The interaction of spinach nitrite reductase with ferredoxin: A site-directed mutation study

Author keywords

Electron transport; Enzymology; Molecular biology; Nitrogen metabolism

Indexed keywords

SPINACIA OLERACEA;

EID: 76149113995     PISSN: 16742052     EISSN: 17529867     Source Type: Journal    
DOI: 10.1093/mp/ssn098     Document Type: Article
Times cited : (20)

References (31)
  • 1
    • 0029051294 scopus 로고
    • Direct electrochemistry and EPR spectroscopy of spinach ferredoxin mutants with modified electron transfer activities
    • Aliverti, A., Hagen, W. R., and Zanetti, G. (1995). Direct electrochemistry and EPR spectroscopy of spinach ferredoxin mutants with modified electron transfer activities. FEBS Lett. 168, 220-224.
    • (1995) FEBS Lett. , vol.168 , pp. 220-224
    • Aliverti, A.1    Hagen, W.R.2    Zanetti, G.3
  • 2
  • 3
    • 0016686529 scopus 로고
    • The role of an iron-sulfur center and siroheme in spinach nitrite reductase
    • Aparicio, P. J., Knaff, D. B., and Malkin, R. (1975). The role of an iron-sulfur center and siroheme in spinach nitrite reductase. Arch. Biochem. Biophys. 169, 45-50.
    • (1975) Arch. Biochem. Biophys. , vol.169 , pp. 45-50
    • Aparicio, P.J.1    Knaff, D.B.2    Malkin, R.3
  • 4
    • 0032213789 scopus 로고    scopus 로고
    • Structure of the mutant E92K of [2Fe-2S] ferredoxin 1 from Spinacea oleracea at 1. 7 Å resolution
    • Binda, C., Coda, A., Aliverti, A., Zanetti, G., and Mattevi, A. (1998). Structure of the mutant E92K of [2Fe-2S] ferredoxin 1 from Spinacea oleracea at 1. 7 Å resolution. Acta Cryst. D54, 1353-1358.
    • (1998) Acta Cryst. , vol.D54 , pp. 1353-1358
    • Binda, C.1    Coda, A.2    Aliverti, A.3    Zanetti, G.4    Mattevi, A.5
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0034736295 scopus 로고    scopus 로고
    • Identification of amino acid residues from Anabaena sp. PCC 7120 involved in ferredoxin binding
    • Curdt, I., Singh, B. B., Jakoby, M., Hachtel, W., and Böhme, H. (2000). Identification of amino acid residues from Anabaena sp. PCC 7120 involved in ferredoxin binding. Biochem. Biophys. Acta. 1543, 60-68.
    • (2000) Biochem. Biophys. Acta. , vol.1543 , pp. 60-68
    • Curdt, I.1    Singh, B.B.2    Jakoby, M.3    Hachtel, W.4    Böhme, H.5
  • 8
    • 0033749797 scopus 로고    scopus 로고
    • Homology predicted structure and functional interaction of ferredoxin from the eukaryotic alga Chlamydomonas reinhardtii with nitrite reductase and glutamate synthase
    • Garcia-Sánchez, M. I., Diaz-Quintana, A., Gotor, C., Jacquot, J.-P., de la Rosa, M. A., and Vega, J. M. (2000). Homology predicted structure and functional interaction of ferredoxin from the eukaryotic alga Chlamydomonas reinhardtii with nitrite reductase and glutamate synthase. J. Biol. Inorg. Chem. 5, 713-719.
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 713-719
    • Garcia-Sánchez, M.I.1    Diaz-Quintana, A.2    Gotor, C.3    Jacquot, J.-P.4    De La Rosa, M.A.5    Vega, J.M.6
  • 9
    • 0031437209 scopus 로고    scopus 로고
    • Critical residues of Chlamydomonas reinhardtii ferredoxin for interaction with nitrite reductase and glutamate synthase by site-directed mutagenesis
    • Garcia-Sánchez, M. I., Gotor, C., Jacquot, J.-P., Stein, M., Suzuki, A., and Vega, J. M. (1997). Critical residues of Chlamydomonas reinhardtii ferredoxin for interaction with nitrite reductase and glutamate synthase by site-directed mutagenesis. Eur. J. Biochem. 250, 364-368.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 364-368
    • Garcia-Sánchez, M.I.1    Gotor, C.2    Jacquot, J.-P.3    Stein, M.4    Suzuki, A.5    Vega, J.M.6
  • 10
    • 33746918945 scopus 로고    scopus 로고
    • The interaction of ferredoxin with ferredoxin-dependent enzymes
    • Golbeck J., ed. (Dordrecht, The Netherlands: Springer)
    • Hase, T., Schürmann, P., and Knaff, D. B. (2006). The interaction of ferredoxin with ferredoxin-dependent enzymes. In Photosystem 1, Golbeck J., ed. (Dordrecht, The Netherlands: Springer), pp. 477-498.
    • (2006) Photosystem , vol.1 , pp. 477-498
    • Hase, T.1    Schürmann, P.2    Knaff, D.B.3
  • 11
    • 0021984634 scopus 로고
    • Interaction of ferredoxin with ferredoxin-linked nitrite reductase with ferredoxin
    • Hirasawa, M., and Knaff, D. B. (1985). Interaction of ferredoxin with ferredoxin-linked nitrite reductase with ferredoxin. Biochem. Biophys. Acta. 830, 171-180.
    • (1985) Biochem. Biophys. Acta. , vol.830 , pp. 171-180
    • Hirasawa, M.1    Knaff, D.B.2
  • 13
    • 0027506040 scopus 로고
    • The effect of lysine and arginine modifying reagents on spinach ferredoxin: Nitrite oxidoreductase
    • Hirasawa, M., de Best, J. H., and Knaff, D. B. (1985). The effect of lysine and arginine modifying reagents on spinach ferredoxin: nitrite oxidoreductase. Biochim. Biophys. Acta. 1140, 304-312.
    • (1985) Biochim. Biophys. Acta. , vol.1140 , pp. 304-312
    • Hirasawa, M.1    De Best, J.H.2    Knaff, D.B.3
  • 14
    • 0032564821 scopus 로고    scopus 로고
    • The role of aromatic and acidic amino acids in the electron transfer reaction catalyzed by spinach ferredoxin-dependent glutamate synthase
    • Hirasawa, M., Hurley, J. K., Salamon, Z., Tollin, G., Markley, J. L., Chen, H., Xia, B., and Knaff, D. B. (1998). The role of aromatic and acidic amino acids in the electron transfer reaction catalyzed by spinach ferredoxin-dependent glutamate synthase. Biochim. Biophys. Acta. 1363, 134-146.
    • (1998) Biochim. Biophys. Acta. , vol.1363 , pp. 134-146
    • Hirasawa, M.1    Hurley, J.K.2    Salamon, Z.3    Tollin, G.4    Markley, J.L.5    Chen, H.6    Xia, B.7    Knaff, D.B.8
  • 15
    • 0023656101 scopus 로고
    • Prosthetic group content and ligand-binding properties of spinach nitrite reductase
    • Hirasawa, M., Shaw, R. W., Palmer, G., and Knaff, D. B. (1987). Prosthetic group content and ligand-binding properties of spinach nitrite reductase. J. Biol. Chem. 262, 12428-12433.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12428-12433
    • Hirasawa, M.1    Shaw, R.W.2    Palmer, G.3    Knaff, D.B.4
  • 16
    • 0028246411 scopus 로고
    • Transient kinetic and oxidation-reduction studies of spinach ferredoxin: Nitrite oxidoreductase
    • Hirasawa, M., Tollin, G., Salamon, Z., and Knaff, D. B. (1994). Transient kinetic and oxidation-reduction studies of spinach ferredoxin: nitrite oxidoreductase. Biochim. Biophys. Acta. 1185, 336-345.
    • (1994) Biochim. Biophys. Acta. , vol.1185 , pp. 336-345
    • Hirasawa, M.1    Tollin, G.2    Salamon, Z.3    Knaff, D.B.4
  • 17
    • 0027142648 scopus 로고
    • An aromatic amino acid is required at position 65 in Anabaena ferredoxin for rapid electron transfer to ferredoxin:NADP+ oxidoreductase
    • Hurley, J. K., Cheng, H., Xia, B., Markley, J. L., Medina, M., Gómez-Moreno, C., and Tollin, G. (1993a). An aromatic amino acid is required at position 65 in Anabaena ferredoxin for rapid electron transfer to ferredoxin:NADP+ oxidoreductase. J. Am. Chem. Soc. 116, 11698-11701.
    • (1993) J. Am. Chem. Soc. , vol.116 , pp. 11698-11701
    • Hurley, J.K.1    Cheng, H.2    Xia, B.3    Markley, J.L.4    Medina, M.5    Gómez-Moreno, C.6    Tollin, G.7
  • 18
    • 0027384925 scopus 로고
    • Amino acid residues in Anabaena ferredoxin crucial to interaction with ferredoxin-NADP+ oxidoreductase: Site-directed mutagenesis and laser flash photolysis
    • Hurley, J. K., et al. (1993b). Amino acid residues in Anabaena ferredoxin crucial to interaction with ferredoxin-NADP+ oxidoreductase: site-directed mutagenesis and laser flash photolysis. Biochemistry. 32, 9346-9354.
    • (1993) Biochemistry. , vol.32 , pp. 9346-9354
    • Hurley, J.K.1
  • 19
    • 0030885192 scopus 로고    scopus 로고
    • Structure-function relationships in Anabaena ferredoxin: Correlations between x-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+-reductase for site-specific ferredoxin mutants
    • Hurley, J. K., et al. (1997). Structure-function relationships in Anabaena ferredoxin: correlations between x-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+- reductase for site-specific ferredoxin mutants. Biochemistry. 36, 11100-11117.
    • (1997) Biochemistry. , vol.36 , pp. 11100-11117
    • Hurley, J.K.1
  • 20
    • 0031031952 scopus 로고    scopus 로고
    • Residue Glu91 of Chlamydomonas reinhardtii ferredoxin is essential for electron transfer to ferredoxin-thioredoxin reductase
    • Jacquot, J.-P., Stein, M., Suzuki, A., Liottet, S., Sandoz, G., and Miginiac-Maslow, M. (1997). Residue Glu91 of Chlamydomonas reinhardtii ferredoxin is essential for electron transfer to ferredoxin-thioredoxin reductase. FEBS Lett. 400, 293-296.
    • (1997) FEBS Lett. , vol.400 , pp. 293-296
    • Jacquot, J.-P.1    Stein, M.2    Suzuki, A.3    Liottet, S.4    Sandoz, G.5    Miginiac-Maslow, M.6
  • 21
    • 0020477481 scopus 로고
    • Evidence for siroheme-FeS interaction in spinach ferredoxin-sulfite reductase
    • Krueger, R. J., and Siegel, L. M. (1982a). Evidence for siroheme-FeS interaction in spinach ferredoxin-sulfite reductase. Biochemistry. 21, 2905-2909.
    • (1982) Biochemistry. , vol.21 , pp. 2905-2909
    • Krueger, R.J.1    Siegel, L.M.2
  • 22
    • 0020477453 scopus 로고
    • Spinach siroheme enzymes: Isolation and characterization of ferredoxin-sulfite reductase and comparison of properties with ferredoxin-nitrite reductase
    • Krueger, R. J., and Siegel, L. M. (1982b). Spinach siroheme enzymes: isolation and characterization of ferredoxin-sulfite reductase and comparison of properties with ferredoxin-nitrite reductase. Biochemistry. 21, 2892-2904.
    • (1982) Biochemistry. , vol.21 , pp. 2892-2904
    • Krueger, R.J.1    Siegel, L.M.2
  • 23
    • 0346463125 scopus 로고    scopus 로고
    • The mechanism of spinach chloroplast ferredoxindependent nitrite reductase: Spectroscopic evidence for intermediate states
    • Kuznetsova, S., Knaff, D. B., Hirasawa, M., Lagoutte, B., and Sétif, P. (2004a). The mechanism of spinach chloroplast ferredoxindependent nitrite reductase: spectroscopic 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    Sétif, P.5
  • 24
    • 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., Sétif, P., and Mattioli, T. A. (2004b). 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    Sétif, P.4    Mattioli, T.A.5
  • 25
    • 0008185046 scopus 로고
    • Dihydroorotic dehydrogenase. I. Some properties of the enzyme
    • Miller, R. W., and Massey, V. (1965). Dihydroorotic dehydrogenase. I. Some properties of the enzyme. J. Biol. Chem. 240, 1453-1465.
    • (1965) J. Biol. Chem. , vol.240 , pp. 1453-1465
    • Miller, R.W.1    Massey, V.2
  • 26
    • 0033619724 scopus 로고    scopus 로고
    • Refined x-ray structures of the oxidized, at 1. 3Å , andreduced, at 1. 17Å , [2Fe-2S] ferredoxinfrom the cyanobacterium Anabaena PCC 7119 show redox-linked conformational changes
    • Morales, R., Chron, M.-H., Hudry-Clergeon, G., Pétillot, Y., Norager, S., Medina, M., and Frey, M. (1999). Refined x-ray structures of the oxidized, at 1. 3Å , andreduced, at 1. 17Å , [2Fe-2S] ferredoxinfrom the cyanobacterium Anabaena PCC 7119 show redox-linked conformational changes. Biochemistry. 38, 15764-15773.
    • (1999) Biochemistry. , vol.38 , pp. 15764-15773
    • Morales, R.1    Chron, M.-H.2    Hudry-Clergeon, G.3    Pétillot, Y.4    Norager, S.5    Medina, M.6    Frey, M.7
  • 27
    • 0029874052 scopus 로고    scopus 로고
    • Mutations of Glu92 in ferreddoxin i from spinach leaves produces proteins fully functional in electron transfer but less efficient in supporting NADP+ photoreduction
    • Piubelli, L., Aliverti, A., Bellintani, F., and Zanetti, G. (1996). Mutations of Glu92 in ferreddoxin I from spinach leaves produces proteins fully functional in electron transfer but less efficient in supporting NADP+ photoreduction. Eur. J. Biochem. 236, 465-489.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 465-489
    • Piubelli, L.1    Aliverti, A.2    Bellintani, F.3    Zanetti, G.4
  • 28
    • 0025907697 scopus 로고
    • Crystallization and structure determination to 2. 5 Å resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120
    • Rypniewski, W. R., Breiter, D. R., Benning, M. M., Wesenberg, G., Oh, B.-H., Markley, J. L., Rayment, I., and Holden, H. M. (1991). Crystallization and structure determination to 2. 5 Å resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120. Biochemistry. 30, 4126-4131.
    • (1991) Biochemistry. , vol.30 , pp. 4126-4131
    • Rypniewski, W.R.1    Breiter, D.R.2    Benning, M.M.3    Wesenberg, G.4    Oh, B.-H.5    Markley, J.L.6    Rayment, I.7    Holden, H.M.8
  • 29
    • 0015918806 scopus 로고
    • Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein: Molecular parameters and prosthetic groups
    • Siegel, L. M., Murphy, M. J., and Kamin, H. (1973). Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein: molecular parameters and prosthetic groups. J. Biol. Chem. 248, 251-264.
    • (1973) J. Biol. Chem. , vol.248 , pp. 251-264
    • Siegel, L.M.1    Murphy, M.J.2    Kamin, H.3
  • 30
    • 28944439659 scopus 로고    scopus 로고
    • Structure of spinach nitrite reductase: Implications for multi-electron reactions by the iron-sulfur:siroheme cofactor
    • 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 cofactor. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.