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Volumn 45, Issue 8, 2012, Pages 476-481

Biochemical characterization of ferredoxin-NADP+reductase interaction with flavodoxin in Pseudomonas putida

Author keywords

Ferredoxin NADP+ reductase; Flavodoxin; Isothermal titration calorimetry; Protein protein interaction; Pseudomonas putida KT2440

Indexed keywords

FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; FLAVODOXIN; RECOMBINANT PROTEIN;

EID: 84866611505     PISSN: 19766696     EISSN: 1976670X     Source Type: Journal    
DOI: 10.5483/BMBRep.2012.45.8.071     Document Type: Article
Times cited : (9)

References (21)
  • 1
    • 2342565785 scopus 로고    scopus 로고
    • Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases
    • Ceccarelli, E. A., Arakaki, A. K., Cortez, N. and Carrillo, N. (2004) Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases. Biochim. Biophys. Acta. 1698, 155-165.
    • (2004) Biochim. Biophys. Acta. , vol.1698 , pp. 155-165
    • Ceccarelli, E.A.1    Arakaki, A.K.2    Cortez, N.3    Carrillo, N.4
  • 2
    • 33646052947 scopus 로고    scopus 로고
    • Flavodoxins: sequence, folding, binding, function and beyond
    • Sancho, J. (2006) Flavodoxins: sequence, folding, binding, function and beyond. Cell Mol. Life Sci. 63, 855-864.
    • (2006) Cell Mol. Life Sci. , vol.63 , pp. 855-864
    • Sancho, J.1
  • 3
    • 0035147528 scopus 로고    scopus 로고
    • Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase
    • Kurisu, G., Kusunoki, M., Katoh, E., Yamazaki, T. and Teshima, K. (2001) Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase. Nat. Struct. Biol. 8, 117-121.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 117-121
    • Kurisu, G.1    Kusunoki, M.2    Katoh, E.3    Yamazaki, T.4    Teshima, K.5
  • 4
  • 5
    • 0242523330 scopus 로고    scopus 로고
    • Ferredoxin-NADP(+) reductase uses the same site for the interaction with ferredoxin and flavodoxin
    • Martinez-Julvez, M., Medina, M. and Gomez-Moreno, C. (1999) Ferredoxin-NADP(+) reductase uses the same site for the interaction with ferredoxin and flavodoxin. J. Biol. Inorg. Chem. 4, 568-578.
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 568-578
    • Martinez-Julvez, M.1    Medina, M.2    Gomez-Moreno, C.3
  • 7
    • 35348831225 scopus 로고    scopus 로고
    • Molecular characterization of fprB (ferredoxin-NADP+ reductase) in Pseudomonas putida KT2440
    • Lee, Y., Yeom, J., Kang, Y. S., Kim, J., Sung, J. S., Jeon, C. O. and Park, W. (2007) Molecular characterization of fprB (ferredoxin-NADP+ reductase) in Pseudomonas putida KT2440. J. Microbiol. Biotechnol. 17, 1504-1512.
    • (2007) J. Microbiol. Biotechnol. , vol.17 , pp. 1504-1512
    • Lee, Y.1    Yeom, J.2    Kang, Y.S.3    Kim, J.4    Sung, J.S.5    Jeon, C.O.6    Park, W.7
  • 8
    • 0034644695 scopus 로고    scopus 로고
    • MioC is an FMN-binding protein that is essential for Escherichia coli biotin synthase activity in vitro
    • Birch, O. M., Hewitson, K. S., Fuhrmann, M., Burgdorf, K., Baldwin, J.E., Roach, P.L. and Shaw, N. M. (2000) MioC is an FMN-binding protein that is essential for Escherichia coli biotin synthase activity in vitro. J. Biol. Chem. 275, 32277-32280.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32277-32280
    • Birch, O.M.1    Hewitson, K.S.2    Fuhrmann, M.3    Burgdorf, K.4    Baldwin, J.E.5    Roach, P.L.6    Shaw, N.M.7
  • 9
    • 33845921565 scopus 로고    scopus 로고
    • Solution structures and backbone dynamics of a flavodoxin MioC from Escherichia coli in both Apo- and Holo-forms: implications for cofactor binding and electron transfer
    • Hu, Y., Li, Y., Zhang, X., Guo, X., Xia, B. and Jin, C. (2006) Solution structures and backbone dynamics of a flavodoxin MioC from Escherichia coli in both Apo- and Holo-forms: implications for cofactor binding and electron transfer. J. Biol. Chem. 281, 35454-35466.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35454-35466
    • Hu, Y.1    Li, Y.2    Zhang, X.3    Guo, X.4    Xia, B.5    Jin, C.6
  • 11
    • 0033614010 scopus 로고    scopus 로고
    • Complex formation between Azotobacter vinelandii ferredoxin I and its physiological electron donor NADPH-ferredoxin reductase
    • Jung, Y.S., Roberts, V. A., Stout, C. D. and Burgess, B. K. (1999) Complex formation between Azotobacter vinelandii ferredoxin I and its physiological electron donor NADPH-ferredoxin reductase. J. Biol. Chem. 274, 2978-2987.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2978-2987
    • Jung, Y.S.1    Roberts, V.A.2    Stout, C.D.3    Burgess, B.K.4
  • 12
    • 80051795712 scopus 로고    scopus 로고
    • Physiochemical properties and kinetics of glucoamylase produced from deoxy-D-glucose resistant mutant of Aspergillus niger for soluble starch hydrolysis
    • Riaz, M., Rashid, M. H., Sawyer, L., Akhtar, S., Javed, M. R., Nadeem, H. and Wear, M. (2012) Physiochemical properties and kinetics of glucoamylase produced from deoxy-D-glucose resistant mutant of Aspergillus niger for soluble starch hydrolysis. Food Chem. 130, 24-30.
    • (2012) Food Chem , vol.130 , pp. 24-30
    • Riaz, M.1    Rashid, M.H.2    Sawyer, L.3    Akhtar, S.4    Javed, M.R.5    Nadeem, H.6    Wear, M.7
  • 13
    • 0036310647 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis FprA, a novel bacterial NADPH-ferredoxin reductase
    • Fischer, F., Raimondi, D., Aliverti, A. and Zanetti, G. (2002) Mycobacterium tuberculosis FprA, a novel bacterial NADPH-ferredoxin reductase. Eur. J. Biochem. 269, 3005-3013.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3005-3013
    • Fischer, F.1    Raimondi, D.2    Aliverti, A.3    Zanetti, G.4
  • 14
    • 0035147528 scopus 로고    scopus 로고
    • Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase
    • Kurisu, G., Kusunoki, M., Katoh, E., Yamazaki, T. and Teshima, K. (2001) Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase. Nat. Struct. Biol. 8, 117-121.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 117-121
    • Kurisu, G.1    Kusunoki, M.2    Katoh, E.3    Yamazaki, T.4    Teshima, K.5
  • 15
    • 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
  • 16
    • 0032560020 scopus 로고    scopus 로고
    • Isothermal titration calorimetric studies on the associations of putidaredoxin to NADH-putidaredoxin reductase and P450cam
    • Aoki, M., Ishimori, K., Fukada, H., Takahashi, K. and Morishima, I. (1998) Isothermal titration calorimetric studies on the associations of putidaredoxin to NADH-putidaredoxin reductase and P450cam. Biochim. Biophys. Acta. 1384, 180-188.
    • (1998) Biochim. Biophys. Acta. , vol.1384 , pp. 180-188
    • Aoki, M.1    Ishimori, K.2    Fukada, H.3    Takahashi, K.4    Morishima, I.5
  • 18
    • 0014216230 scopus 로고
    • Studies on crystalline D-amino acid oxidase V. Characterization of borohydride-reduced enzyme-substrate intermediate. Synthesis of epsilon-N-(1-carboxyethyl)-L-lysine
    • Hellerman, L. and Coffey, D. S. (1967) Studies on crystalline D-amino acid oxidase. V. Characterization of borohydride-reduced enzyme-substrate intermediate. Synthesis of epsilon-N-(1-carboxyethyl)-L-lysine. J. Biol. Chem. 242, 582-589.
    • (1967) J. Biol. Chem. , vol.242 , pp. 582-589
    • Hellerman, L.1    Coffey, D.S.2
  • 19
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K. and Pease, L.R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 20
    • 84857711687 scopus 로고    scopus 로고
    • Temperature, organic solvent and pH stabil: zation of the neutral protease from saling vibrio nrotedyticus: significance of the strutural calcium
    • Asghari, S. M., Khageh, K., Dalfard, A. B., Pazhang, M. and Karbalaei-Heidari, H. R. (2011) Temperature, organic solvent and pH stabil: zation of the neutral protease from saling vibrio nrotedyticus: significance of the strutural calcium. BMB Rep. 44, 665-668.
    • (2011) BMB Rep , vol.44 , pp. 665-668
    • Asghari, S.M.1    Khageh, K.2    Dalfard, A.B.3    Pazhang, M.4    Karbalaei-Heidari, H.R.5
  • 21
    • 78650713798 scopus 로고    scopus 로고
    • Soluble expression, purtication and the role of C-terminal glycine residues in scorpion toxin BmK AGP-SYPU2
    • Zhang, R., Cui, Y., Zhang, X., Yang, Z., Zhao, Y., Song, Y., Wu, C. and Zhang, J. (2010) Soluble expression, purtication and the role of C-terminal glycine residues in scorpion toxin BmK AGP-SYPU2. BMB Rep. 43, 801-806.
    • (2010) BMB Rep , vol.43 , pp. 801-806
    • Zhang, R.1    Cui, Y.2    Zhang, X.3    Yang, Z.4    Zhao, Y.5    Song, Y.6    Wu, C.7    Zhang, J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.