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Volumn 1764, Issue 9, 2006, Pages 1462-1469

Characterization of DitA3, the [Fe3S4] ferredoxin of an aromatic ring-hydroxylating dioxygenase from a diterpenoid-degrading microorganism

Author keywords

Fe3S4 ferredoxin; Dioxygenase; Electrochemistry; Redox potential

Indexed keywords

DIMER; DIOXYGENASE; DITA3 PROTEIN; DITERPENOID; GRAPHITE; POTASSIUM CHLORIDE; PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; DITA PROTEIN, PSEUDOMONAS ABIETANIPHILA; DITERPENE; FERREDOXIN;

EID: 33748453563     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.06.011     Document Type: Article
Times cited : (4)

References (54)
  • 1
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert H., Holm R., and Münck E. Iron-sulfur clusters: Nature's modular, multipurpose structures. Science 277 (1997) 653-659
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.2    Münck, E.3
  • 2
    • 0001531848 scopus 로고    scopus 로고
    • Protein control of redox potentials of iron-sulfur proteins
    • Stephens P.J., Jollie D.R., and Warshel A. Protein control of redox potentials of iron-sulfur proteins. Chem. Rev. 96 (1996) 2491-2513
    • (1996) Chem. Rev. , vol.96 , pp. 2491-2513
    • Stephens, P.J.1    Jollie, D.R.2    Warshel, A.3
  • 3
    • 0018829763 scopus 로고
    • On the nature of the iron-sulfur centers in a ferredoxin from Azotobacter vinelandii. Mössbauer studies and cluster displacement experiments
    • Emptage M.H., Kent T.A., Huynh B.H., Rawlings J., Orme-Johnson W.H., and Münck E. On the nature of the iron-sulfur centers in a ferredoxin from Azotobacter vinelandii. Mössbauer studies and cluster displacement experiments. J. Biol. Chem. 255 (1980) 1793-1796
    • (1980) J. Biol. Chem. , vol.255 , pp. 1793-1796
    • Emptage, M.H.1    Kent, T.A.2    Huynh, B.H.3    Rawlings, J.4    Orme-Johnson, W.H.5    Münck, E.6
  • 4
    • 0018829764 scopus 로고
    • Iron-sulfur clusters in Azotobacter ferredoxin at 2.5 Å resolution
    • Stout C.D., Ghosh D., Pattabhi V., and Robbins A.H. Iron-sulfur clusters in Azotobacter ferredoxin at 2.5 Å resolution. J. Biol. Chem. 255 (1980) 1797-1800
    • (1980) J. Biol. Chem. , vol.255 , pp. 1797-1800
    • Stout, C.D.1    Ghosh, D.2    Pattabhi, V.3    Robbins, A.H.4
  • 5
    • 0009746605 scopus 로고
    • Trinuclear cuboidal and heterometallic cubane-type iron-sulfur clusters: new structural and reactivity themes in chemistry and biology
    • Holm R.H. Trinuclear cuboidal and heterometallic cubane-type iron-sulfur clusters: new structural and reactivity themes in chemistry and biology. Adv. Inorg. Chem. 38 (1992) 1-73
    • (1992) Adv. Inorg. Chem. , vol.38 , pp. 1-73
    • Holm, R.H.1
  • 6
    • 0035826560 scopus 로고    scopus 로고
    • Determination of the midpoint potential of the FAD and FMN flavin cofactors and of the 3Fe-4S cluster of glutamate synthase
    • Ravasio S., Curti B., and Vanoni M.A. Determination of the midpoint potential of the FAD and FMN flavin cofactors and of the 3Fe-4S cluster of glutamate synthase. Biochemistry 40 (2001) 5533-5541
    • (2001) Biochemistry , vol.40 , pp. 5533-5541
    • Ravasio, S.1    Curti, B.2    Vanoni, M.A.3
  • 9
    • 0000170823 scopus 로고
    • Structure of the 3Fe-4S cluster in Desulfovibrio gigas ferredoxin II
    • Kissinger C.R., Adman E.T., Sieker L.C., and Jensen L.H. Structure of the 3Fe-4S cluster in Desulfovibrio gigas ferredoxin II. J. Am. Chem. Soc. 110 (1988) 8721-8723
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 8721-8723
    • Kissinger, C.R.1    Adman, E.T.2    Sieker, L.C.3    Jensen, L.H.4
  • 11
    • 0021103853 scopus 로고
    • Three-iron clusters in iron-sulfur proteins
    • Beinert H., and Thomson A.J. Three-iron clusters in iron-sulfur proteins. Arch. Biochem. Biophys. 222 (1983) 333-361
    • (1983) Arch. Biochem. Biophys. , vol.222 , pp. 333-361
    • Beinert, H.1    Thomson, A.J.2
  • 12
    • 0019332456 scopus 로고
    • Evidence for a three-iron center in a ferredoxin from Desulfovibrio gigas. Mössbauer and EPR studies
    • Huynh B.H., Moura J.J.G., Moura I., Kent T.A., LeGall J., Xavier A.V., and Münck E. Evidence for a three-iron center in a ferredoxin from Desulfovibrio gigas. Mössbauer and EPR studies. J. Biol. Chem. 255 (1980) 3242-3244
    • (1980) J. Biol. Chem. , vol.255 , pp. 3242-3244
    • Huynh, B.H.1    Moura, J.J.G.2    Moura, I.3    Kent, T.A.4    LeGall, J.5    Xavier, A.V.6    Münck, E.7
  • 14
    • 0002004201 scopus 로고
    • Reactivities and biological functions of iron-sulfur clusters
    • Lindahl P.A., and Kovacs J.A. Reactivities and biological functions of iron-sulfur clusters. J. Clust. Sci. 1 (1990) 29-73
    • (1990) J. Clust. Sci. , vol.1 , pp. 29-73
    • Lindahl, P.A.1    Kovacs, J.A.2
  • 15
    • 0025360449 scopus 로고
    • Recent developments in the field of iron-sulfur proteins
    • Beinert H. Recent developments in the field of iron-sulfur proteins. FASEB J. 4 (1990) 2483-2491
    • (1990) FASEB J. , vol.4 , pp. 2483-2491
    • Beinert, H.1
  • 16
    • 0011509370 scopus 로고    scopus 로고
    • Structural and functional aspects of metal sites in biology
    • Holm R.H., Kennepohl P., and Solomon E.I. Structural and functional aspects of metal sites in biology. Chem. Rev. 96 (1996) 2239-2314
    • (1996) Chem. Rev. , vol.96 , pp. 2239-2314
    • Holm, R.H.1    Kennepohl, P.2    Solomon, E.I.3
  • 17
    • 0026409862 scopus 로고
    • Perspectives on non-heme iron protein chemistry
    • Howard J.B., and Rees D.C. Perspectives on non-heme iron protein chemistry. Adv. Protein Chem. 42 (1991) 199-280
    • (1991) Adv. Protein Chem. , vol.42 , pp. 199-280
    • Howard, J.B.1    Rees, D.C.2
  • 18
    • 0344834199 scopus 로고
    • Iron-sulfur cluster enzymes: themes and variations
    • Cammack R. Iron-sulfur cluster enzymes: themes and variations. Adv. Inorg. Chem. 38 (1992) 281-322
    • (1992) Adv. Inorg. Chem. , vol.38 , pp. 281-322
    • Cammack, R.1
  • 19
    • 0034029015 scopus 로고    scopus 로고
    • Aromatic hydrocarbon dioxygenases in environmental biotechnology
    • Gibson D.T., and Parales R.E. Aromatic hydrocarbon dioxygenases in environmental biotechnology. Curr. Opin. Biotechnol. 11 (2000) 236-243
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 236-243
    • Gibson, D.T.1    Parales, R.E.2
  • 22
    • 0021378817 scopus 로고
    • An investigation of the iron-sulphur proteins of benzene dioxygenase from Pseudomonas putida by electron-spin-resonance spectroscopy
    • Geary P.J., Saboowalla F., Patil D., and Cammack R. An investigation of the iron-sulphur proteins of benzene dioxygenase from Pseudomonas putida by electron-spin-resonance spectroscopy. Biochem. J. 217 (1984) 667-673
    • (1984) Biochem. J. , vol.217 , pp. 667-673
    • Geary, P.J.1    Saboowalla, F.2    Patil, D.3    Cammack, R.4
  • 23
    • 0031060718 scopus 로고    scopus 로고
    • Structure-function analysis of the bacterial aromatic ring-hydroxylating dioxygenases
    • Butler C.S., and Mason J.R. Structure-function analysis of the bacterial aromatic ring-hydroxylating dioxygenases. Adv. Microbiol. Physiol. 38 (1997) 47-84
    • (1997) Adv. Microbiol. Physiol. , vol.38 , pp. 47-84
    • Butler, C.S.1    Mason, J.R.2
  • 24
    • 0029997109 scopus 로고    scopus 로고
    • Comparison of the Rieske [2Fe-2S] centre in the bc1 complex and in bacterial dioxygenases by circular-dichroism spectroscopy and cyclic voltammetry
    • Link T.A., Hatzfeld O.M., Unalkat P., Shergill J.K., Cammack R., and Mason J.R. Comparison of the Rieske [2Fe-2S] centre in the bc1 complex and in bacterial dioxygenases by circular-dichroism spectroscopy and cyclic voltammetry. Biochemistry 35 (1996) 7546-7552
    • (1996) Biochemistry , vol.35 , pp. 7546-7552
    • Link, T.A.1    Hatzfeld, O.M.2    Unalkat, P.3    Shergill, J.K.4    Cammack, R.5    Mason, J.R.6
  • 26
    • 23844520705 scopus 로고    scopus 로고
    • Characterization of [3Fe-4S] ferredoxin DbfA3, which functions in the angular dioxygenase system of Terrabacter sp. Strain DBF63
    • Takagi T., Habe H., Yoshida T., Yamane H., Omori T., and Nojiri H. Characterization of [3Fe-4S] ferredoxin DbfA3, which functions in the angular dioxygenase system of Terrabacter sp. Strain DBF63. App. Microbiol. Biotech. 68 (2005) 336-345
    • (2005) App. Microbiol. Biotech. , vol.68 , pp. 336-345
    • Takagi, T.1    Habe, H.2    Yoshida, T.3    Yamane, H.4    Omori, T.5    Nojiri, H.6
  • 27
    • 0032929306 scopus 로고    scopus 로고
    • A novel aromatic-ring-hydroxylating dioxygenase from the diterpenoid-degrading bacterium Pseudomonas abietaniphila BKME-9
    • Martin V.J.J., and Mohn W.W. A novel aromatic-ring-hydroxylating dioxygenase from the diterpenoid-degrading bacterium Pseudomonas abietaniphila BKME-9. J. Bacteriol. 181 (1999) 2675-2682
    • (1999) J. Bacteriol. , vol.181 , pp. 2675-2682
    • Martin, V.J.J.1    Mohn, W.W.2
  • 29
    • 0027954042 scopus 로고
    • Hyperexpression of a synthetic gene encoding a high potential iron-sulfur protein
    • Eltis L.D., Iwagami S.G., and Smith M. Hyperexpression of a synthetic gene encoding a high potential iron-sulfur protein. Protein Eng. 7 (1994) 1145-1150
    • (1994) Protein Eng. , vol.7 , pp. 1145-1150
    • Eltis, L.D.1    Iwagami, S.G.2    Smith, M.3
  • 30
    • 0029962741 scopus 로고    scopus 로고
    • The solution structure refinement of the paramagnetic reduced high-potential iron-surfur protein I from Ectothiorhodospira halophila by using stable isotope labelling and nuclear relaxation
    • Bertini I., Couture M.M.-J., Donaire A., Eltis L.D., Felli I.C., and Luchinat C. The solution structure refinement of the paramagnetic reduced high-potential iron-surfur protein I from Ectothiorhodospira halophila by using stable isotope labelling and nuclear relaxation. Eur. J. Biochem. 241 (1996) 440-452
    • (1996) Eur. J. Biochem. , vol.241 , pp. 440-452
    • Bertini, I.1    Couture, M.M.-J.2    Donaire, A.3    Eltis, L.D.4    Felli, I.C.5    Luchinat, C.6
  • 31
    • 0000404096 scopus 로고
    • The growth of mirco-organisms in relation to their energy supply
    • Bauchop T., and Elsden R. The growth of mirco-organisms in relation to their energy supply. J. Gen. Microbiol. 23 (1960) 457-469
    • (1960) J. Gen. Microbiol. , vol.23 , pp. 457-469
    • Bauchop, T.1    Elsden, R.2
  • 32
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schäger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schäger, H.1    von Jagow, G.2
  • 34
    • 0024411870 scopus 로고
    • Protein measurement using bicinchoninic acid: elimination of interfering substances
    • Brown R.E., Jarvis K.L., and Hyland K.J. Protein measurement using bicinchoninic acid: elimination of interfering substances. Anal. Biochem. 180 (1989) 136-139
    • (1989) Anal. Biochem. , vol.180 , pp. 136-139
    • Brown, R.E.1    Jarvis, K.L.2    Hyland, K.J.3
  • 35
    • 0025055440 scopus 로고
    • Purification and properties of NADH-ferredoxin NAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816
    • Haigler B.E., and Gibson D.T. Purification and properties of NADH-ferredoxin NAP reductase, a component of naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816. J. Bacteriol. 172 (1990) 457-464
    • (1990) J. Bacteriol. , vol.172 , pp. 457-464
    • Haigler, B.E.1    Gibson, D.T.2
  • 36
    • 0017413173 scopus 로고
    • Inhibition of methylene blue formation during determination of the acid-labile sulfide of iron-sulfur protein samples containing dithionite
    • Chen J.-S., and Morenson L.E. Inhibition of methylene blue formation during determination of the acid-labile sulfide of iron-sulfur protein samples containing dithionite. Anal. Biochem. 79 (1977) 157-165
    • (1977) Anal. Biochem. , vol.79 , pp. 157-165
    • Chen, J.-S.1    Morenson, L.E.2
  • 37
    • 0024320468 scopus 로고
    • Direct electron transfer of redox proteins at the bare glassy carbon electrode
    • Hagen W.R. Direct electron transfer of redox proteins at the bare glassy carbon electrode. Eur. J. Biochem. 182 (1989) 523-530
    • (1989) Eur. J. Biochem. , vol.182 , pp. 523-530
    • Hagen, W.R.1
  • 38
    • 33947483336 scopus 로고
    • Theory and application of cyclic voltammetry for measurement of electrode reaction kinetics
    • Nicholson R.S. Theory and application of cyclic voltammetry for measurement of electrode reaction kinetics. Anal. Chem. 37 (1965) 1351-1355
    • (1965) Anal. Chem. , vol.37 , pp. 1351-1355
    • Nicholson, R.S.1
  • 39
    • 0032546580 scopus 로고    scopus 로고
    • Effect of iron-sulfur cluster environment in modulating the thermodynamic properties and biological function of ferredoxin from Pyrococcus furiosus
    • Brereton P.S., Verhagen M.F., Zhou Z.H., and Adams M.W.W. Effect of iron-sulfur cluster environment in modulating the thermodynamic properties and biological function of ferredoxin from Pyrococcus furiosus. Biochemistry 37 (1998) 7351-7362
    • (1998) Biochemistry , vol.37 , pp. 7351-7362
    • Brereton, P.S.1    Verhagen, M.F.2    Zhou, Z.H.3    Adams, M.W.W.4
  • 40
    • 0001479540 scopus 로고    scopus 로고
    • Site-directed mutations of the 4Fe-ferredoxin for the hyperthermophilic archaeon Pyrococcus furiosus: role of the cluster-coordinating aspartate in physiological electron transfer reactions
    • Zhou Z.H., and Adams M.W.W. Site-directed mutations of the 4Fe-ferredoxin for the hyperthermophilic archaeon Pyrococcus furiosus: role of the cluster-coordinating aspartate in physiological electron transfer reactions. Biochemistry 36 (1997) 10892-10900
    • (1997) Biochemistry , vol.36 , pp. 10892-10900
    • Zhou, Z.H.1    Adams, M.W.W.2
  • 41
    • 0032532605 scopus 로고    scopus 로고
    • Voltametric studies of the reaction of iron-sulphur clusters ([3Fe4S] or [M3Fe-4S]) formed in Pyrococcus furiosus ferredoxin
    • Fawcett S.E.J., Davis D., Breton J.L., Thomson A.J., and Armstrong F.A. Voltametric studies of the reaction of iron-sulphur clusters ([3Fe4S] or [M3Fe-4S]) formed in Pyrococcus furiosus ferredoxin. Biochem. J. 335 (1998) 357-368
    • (1998) Biochem. J. , vol.335 , pp. 357-368
    • Fawcett, S.E.J.1    Davis, D.2    Breton, J.L.3    Thomson, A.J.4    Armstrong, F.A.5
  • 42
    • 0022420478 scopus 로고
    • Circular dichroism and redox properties of high redox potential ferredoxins
    • Przysiecki C.T., Meyer T.E., and Cusanovich M.A. Circular dichroism and redox properties of high redox potential ferredoxins. Biochemistry 24 (1985) 2542-2549
    • (1985) Biochemistry , vol.24 , pp. 2542-2549
    • Przysiecki, C.T.1    Meyer, T.E.2    Cusanovich, M.A.3
  • 43
    • 77956772373 scopus 로고
    • Structural and functional diversity of ferredoxins and related proteins
    • Matsubara H., and Saeki K. Structural and functional diversity of ferredoxins and related proteins. Adv. Inorg. Chem. 38 (1992) 223-280
    • (1992) Adv. Inorg. Chem. , vol.38 , pp. 223-280
    • Matsubara, H.1    Saeki, K.2
  • 47
    • 0023119695 scopus 로고
    • Spectroscopic studies of the seven-iron-containing ferredoxins from Azotobacter vinelandii and Thermus thermophilus
    • Johnson M.K., Bennett D.E., Fee J.A., and Sweeney W.V. Spectroscopic studies of the seven-iron-containing ferredoxins from Azotobacter vinelandii and Thermus thermophilus. Biochim. Biophys. Acta 911 (1987) 81-94
    • (1987) Biochim. Biophys. Acta , vol.911 , pp. 81-94
    • Johnson, M.K.1    Bennett, D.E.2    Fee, J.A.3    Sweeney, W.V.4
  • 48
    • 0028670507 scopus 로고
    • Mössbauer and EPR studies of Azotobacter vinelandii ferredoxin I
    • Hu Z., Jollie D., Burgess B.K., Stephens P.J., and Münck E. Mössbauer and EPR studies of Azotobacter vinelandii ferredoxin I. Biochemistry 33 (1994) 14475-14485
    • (1994) Biochemistry , vol.33 , pp. 14475-14485
    • Hu, Z.1    Jollie, D.2    Burgess, B.K.3    Stephens, P.J.4    Münck, E.5
  • 49
    • 0021764689 scopus 로고
    • Azotobacter chroococcum 7Fe ferredoxin. Two pH-dependent forms of the reduced 3Fe clusters and its conversion to a 4Fe cluster
    • George S.J., Richards A.J., Thomson A.J., and Yates M.G. Azotobacter chroococcum 7Fe ferredoxin. Two pH-dependent forms of the reduced 3Fe clusters and its conversion to a 4Fe cluster. Biochem. J. 224 (1984) 247-251
    • (1984) Biochem. J. , vol.224 , pp. 247-251
    • George, S.J.1    Richards, A.J.2    Thomson, A.J.3    Yates, M.G.4
  • 50
    • 0028793620 scopus 로고
    • Identification of the iron-sulfur clusters in a ferredoxin from the archaeon Sulfolobus acidocaldarius. Evidence for a reduced [3Fe-4S] cluster with pH-dependent electronic properties
    • Breton J.L., Duff J.L., Butt J.N., Armstrong F.A., George S.J., Petillot Y., Forest E., Schafer G., and Thomson A.J. Identification of the iron-sulfur clusters in a ferredoxin from the archaeon Sulfolobus acidocaldarius. Evidence for a reduced [3Fe-4S] cluster with pH-dependent electronic properties. Eur. J. Biochem. 233 (1995) 937-946
    • (1995) Eur. J. Biochem. , vol.233 , pp. 937-946
    • Breton, J.L.1    Duff, J.L.2    Butt, J.N.3    Armstrong, F.A.4    George, S.J.5    Petillot, Y.6    Forest, E.7    Schafer, G.8    Thomson, A.J.9
  • 53
    • 0023985949 scopus 로고
    • Structure, function and evolution of bacterial ferredoxins
    • Bruschi M., and Guerlesquin F. Structure, function and evolution of bacterial ferredoxins. FEMS Microbiol. Rev. 4 (1988) 155-175
    • (1988) FEMS Microbiol. Rev. , vol.4 , pp. 155-175
    • Bruschi, M.1    Guerlesquin, F.2
  • 54
    • 0025323166 scopus 로고
    • Spectroscopic characterization of the novel iron-sulfur cluster in Pyrococcus furiosus ferredoxin
    • Conover R.C., Kowal A.T., Fu W., Park J.-B., Aono S., and Adams M.W.W. Spectroscopic characterization of the novel iron-sulfur cluster in Pyrococcus furiosus ferredoxin. J. Biol. Chem. 265 (1990) 8533-8541
    • (1990) J. Biol. Chem. , vol.265 , pp. 8533-8541
    • Conover, R.C.1    Kowal, A.T.2    Fu, W.3    Park, J.-B.4    Aono, S.5    Adams, M.W.W.6


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