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Volumn 11, Issue 12, 2002, Pages 2969-2973

Redox-dependent structural changes in archaeal and bacterial Rieske-type [2Fe-2S] clusters

Author keywords

Anthranilate dioxygenase (AntDO); Archaeal Rieske ferredoxin (ARF); Iron sulfur cluster; Reduction potential; Rieske type ferredoxin; X ray absorption fine structure; X ray absorption spectroscopy

Indexed keywords

ANTHRANILIC ACID; FERREDOXIN; ARCHAEAL PROTEIN; BACTERIAL PROTEIN; IRON SULFUR PROTEIN; RIESKE IRON-SULFUR PROTEIN; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 0036891683     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0222402     Document Type: Article
Times cited : (31)

References (31)
  • 2
    • 0033546142 scopus 로고    scopus 로고
    • Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. II. The Rieske protein of phylogenetically distant acidophilic organisms
    • Brugna, M., Nitschke, W., Asso, M., Guigliarelli, B., Lemesle-Meunier, D., and Schmidt, C. 1999. Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. II. The Rieske protein of phylogenetically distant acidophilic organisms. J. Biol. Chem. 274: 16766-16772.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16766-16772
    • Brugna, M.1    Nitschke, W.2    Asso, M.3    Guigliarelli, B.4    Lemesle-Meunier, D.5    Schmidt, C.6
  • 3
    • 0031574021 scopus 로고    scopus 로고
    • Biological identity and diversity in photosynthesis and respiration: Structure of the lumen-side domain of the chloroplast Rieske protein
    • Carrell, C.J., Zhang, H., Cramer, W.A., and Smith, J.L. 1997. Biological identity and diversity in photosynthesis and respiration: Structure of the lumen-side domain of the chloroplast Rieske protein. Structure 5: 1613-1625.
    • (1997) Structure , vol.5 , pp. 1613-1625
    • Carrell, C.J.1    Zhang, H.2    Cramer, W.A.3    Smith, J.L.4
  • 4
    • 0021959501 scopus 로고
    • Evidence for N coordination to Fe in the [2Fe-2S] clusters of Thermus Rieske protein and phthalate dioxygenase from Pseudomonas
    • Cline, J.F., Hoffman, B.M., Mims, W.B., LaHaie, E., Ballou, D.P., and Fee, J.A. 1985. Evidence for N coordination to Fe in the [2Fe-2S] clusters of Thermus Rieske protein and phthalate dioxygenase from Pseudomonas. J. Biol. Chem. 260: 3251-3254.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3251-3254
    • Cline, J.F.1    Hoffman, B.M.2    Mims, W.B.3    LaHaie, E.4    Ballou, D.P.5    Fee, J.A.6
  • 5
    • 0034480510 scopus 로고    scopus 로고
    • A cluster exposed: Structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins
    • Colbert, C.L., Couture, M.M.-J., Eltis, L.D., and Bolin, J. 2000. A cluster exposed: Structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins. Structure 8: 1267-1278.
    • (2000) Structure , vol.8 , pp. 1267-1278
    • Colbert, C.L.1    Couture, M.M.-J.2    Eltis, L.D.3    Bolin, J.4
  • 6
    • 0027093793 scopus 로고
    • Phthalate dioxygenase reductase: A modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]
    • Correll, C.C., Batie, C.J., Ballou, D.P., and Ludwig, M.L. 1992. Phthalate dioxygenase reductase: A modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]. Science 258: 1604-1610.
    • (1992) Science , vol.258 , pp. 1604-1610
    • Correll, C.C.1    Batie, C.J.2    Ballou, D.P.3    Ludwig, M.L.4
  • 7
    • 2442728899 scopus 로고    scopus 로고
    • X-ray absorption spectroscopic analysis of Fe(II) and Cu(II) forms of a herbicide-degrading α-ketoglutarate dioxygenase
    • Cosper, N.J., Stålhandske, C.M.V., Saari, R.E., Hausinger, R.P., and Scott, R.A. 1999. X-ray absorption spectroscopic analysis of Fe(II) and Cu(II) forms of a herbicide-degrading α-ketoglutarate dioxygenase. J. Biol. Inorg. Chem. 4: 122-129.
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 122-129
    • Cosper, N.J.1    Stålhandske, C.M.V.2    Saari, R.E.3    Hausinger, R.P.4    Scott, R.A.5
  • 8
    • 0033600552 scopus 로고    scopus 로고
    • Electron paramagnetic resonance measurements of the ferrous mononuclear site of phthalate dioxygenase substituted with alternate divalent metal ions: Direct evidence for ligation of two histidines in the copper(II)-reconstituted protein
    • Coulter, E.D., Moon, N., Batie, C.J., Dunham, W.R., and Ballou, D.P. 1999. Electron paramagnetic resonance measurements of the ferrous mononuclear site of phthalate dioxygenase substituted with alternate divalent metal ions: Direct evidence for ligation of two histidines in the copper(II)-reconstituted protein. Biochemistry 38: 11062-11072.
    • (1999) Biochemistry , vol.38 , pp. 11062-11072
    • Coulter, E.D.1    Moon, N.2    Batie, C.J.3    Dunham, W.R.4    Ballou, D.P.5
  • 9
    • 0032502711 scopus 로고    scopus 로고
    • Alteration of the midpoint potential and catalytic activity of the Rieske iron-sulfur protein by changes of amino acids forming hydrogen bonds to the iron-sulfur cluster
    • Denke, E., Merbitz-Zahradnik, T., Hatzfeld, O.M., Snyder, C.H., Link, T.A., and Trumpower, B.L. 1998. Alteration of the midpoint potential and catalytic activity of the Rieske iron-sulfur protein by changes of amino acids forming hydrogen bonds to the iron-sulfur cluster. J. Biol. Chem. 273: 9085-9093.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9085-9093
    • Denke, E.1    Merbitz-Zahradnik, T.2    Hatzfeld, O.M.3    Snyder, C.H.4    Link, T.A.5    Trumpower, B.L.6
  • 10
    • 0035190139 scopus 로고    scopus 로고
    • Characterization and evolution of anthranilate 1,2-dioxygenase from Acinetobacter sp. strain ADP1
    • Eby, D.M., Beharry, Z.M., Coulter, E.D., Kurtz, D.M., and Neidle, E.L. 2001. Characterization and evolution of anthranilate 1,2-dioxygenase from Acinetobacter sp. strain ADP1. J. Bacteriol. 183: 109-118.
    • (2001) J. Bacteriol. , vol.183 , pp. 109-118
    • Eby, D.M.1    Beharry, Z.M.2    Coulter, E.D.3    Kurtz, D.M.4    Neidle, E.L.5
  • 11
    • 0021759095 scopus 로고
    • Purification and characterization of the Rieske iron-sulfur protein from Thermus thermophilus. Evidence for a [2Fe-2S] cluster having non-cysteine ligands
    • Fee, J.A., Findling, K.L., Yoshida, T., Hille, R., Tarr, G.E., Hearshen, D.O., Dunham, W.R., Day, E.P., Kent, T.A., and Münck, E. 1984. Purification and characterization of the Rieske iron-sulfur protein from Thermus thermophilus. Evidence for a [2Fe-2S] cluster having non-cysteine ligands. J. Biol. Chem. 259: 124-133.
    • (1984) J. Biol. Chem. , vol.259 , pp. 124-133
    • Fee, J.A.1    Findling, K.L.2    Yoshida, T.3    Hille, R.4    Tarr, G.E.5    Hearshen, D.O.6    Dunham, W.R.7    Day, E.P.8    Kent, T.A.9    Münck, E.10
  • 12
    • 0034720770 scopus 로고    scopus 로고
    • Specific mutagenesis of the Rieske iron-sulfur protein in Rhodobacter sphaeroides shows that both the thermodynamic gradient and the pK of the oxidized form determine the rate of quinol oxidation by the bc(1) complex
    • Guergova-Kuras, M., Kuras, R., Ugulava, N., Hadad, I., and Crofts, A.R. 2000. Specific mutagenesis of the Rieske iron-sulfur protein in Rhodobacter sphaeroides shows that both the thermodynamic gradient and the pK of the oxidized form determine the rate of quinol oxidation by the bc(1) complex. Biochemistry 39: 7436-7444.
    • (2000) Biochemistry , vol.39 , pp. 7436-7444
    • Guergova-Kuras, M.1    Kuras, R.2    Ugulava, N.3    Hadad, I.4    Crofts, A.R.5
  • 13
    • 0029999657 scopus 로고    scopus 로고
    • Active site structure of Rieske-type proteins: Electron nuclear double resonance studies of isotopically labeled phthalate dioxygenase from Pseudomonas cepacia and Rieske protein from Rhodobacter capsulatus and molecular modeling studies of a Rieske center
    • Gurbiel, R.J., Doan, P.E., Gassner, G.T., Macke, T.J., Case, D.A., Ohnishi, T., Fee, J.A., Ballou, D.P., and Hoffman, B.M. 1996. Active site structure of Rieske-type proteins: Electron nuclear double resonance studies of isotopically labeled phthalate dioxygenase from Pseudomonas cepacia and Rieske protein from Rhodobacter capsulatus and molecular modeling studies of a Rieske center. Biochemistry 35: 7834-7845.
    • (1996) Biochemistry , vol.35 , pp. 7834-7845
    • Gurbiel, R.J.1    Doan, P.E.2    Gassner, G.T.3    Macke, T.J.4    Case, D.A.5    Ohnishi, T.6    Fee, J.A.7    Ballou, D.P.8    Hoffman, B.M.9
  • 15
    • 0030585240 scopus 로고    scopus 로고
    • Structure of a water soluble fragment of the "Rieske" iron sulfur protein of the bovine heart mitochondrial cytochrome bc(1) complex determined by MAD phasing at 1.5 angstrom resolution
    • Iwata, S., Saynovits, M., Link, T.A., and Michel, H. 1996. Structure of a water soluble fragment of the "Rieske" iron sulfur protein of the bovine heart mitochondrial cytochrome bc(1) complex determined by MAD phasing at 1.5 angstrom resolution. Structure 4: 567-579.
    • (1996) Structure , vol.4 , pp. 567-579
    • Iwata, S.1    Saynovits, M.2    Link, T.A.3    Michel, H.4
  • 18
    • 0023002388 scopus 로고
    • Evidence for a redox-linked ionizable group associated with the [2Fe-2S] cluster of Thermus Rieske protein
    • Kuila, D. and Fee, J.A. 1986. Evidence for a redox-linked ionizable group associated with the [2Fe-2S] cluster of Thermus Rieske protein. J. Biol. Chem. 261: 2768-2771.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2768-2771
    • Kuila, D.1    Fee, J.A.2
  • 19
    • 0442331120 scopus 로고    scopus 로고
    • Iron sulfur proteins
    • Link, T.A. 1999. Iron sulfur proteins. Adv. Inorg. Chem. 47: 83-157.
    • (1999) Adv. Inorg. Chem. , vol.47 , pp. 83-157
    • Link, T.A.1
  • 22
    • 0026743341 scopus 로고
    • The electron-transport proteins of hydroxylating bacterial dioxygenases
    • Mason, J.R. and Cammack, R. 1992. The electron-transport proteins of hydroxylating bacterial dioxygenases. Annu. Rev. Microbiol. 46: 277-305.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 277-305
    • Mason, J.R.1    Cammack, R.2
  • 23
    • 0033619724 scopus 로고    scopus 로고
    • Refined X-ray structures of the oxidized, at 1.3 Å, and reduced, at 1.17 Å, [2Fe-2S] ferredoxin from the cyanobacterium Anabaena PCC7119 show redox-linked conformational changes
    • Morales, R., Charon, M.-H., Hudry-Clergeon, G., Peillot, Y., Norager, S., Medina, M., and Frey, M. 1999. Refined X-ray structures of the oxidized, at 1.3 Å, and reduced, at 1.17 Å, [2Fe-2S] ferredoxin from the cyanobacterium Anabaena PCC7119 show redox-linked conformational changes. Biochemistry 38: 15764-15773.
    • (1999) Biochemistry , vol.38 , pp. 15764-15773
    • Morales, R.1    Charon, M.-H.2    Hudry-Clergeon, G.3    Peillot, Y.4    Norager, S.5    Medina, M.6    Frey, M.7
  • 25
    • 0029590773 scopus 로고
    • EPR, electron spin echo envelope modulation, and electron nuclear double resonance studies of the 2Fe2S centers of the 2-halobenzoate 1,2-dioxygenase from Burkholderia (Pseudomonas) cepacia 2CBS
    • Riedel, A., Fetzner, S., Rampp, M., Lingens, F., Liebl, U., Zimmermann, J.-L., and Nitschke, W. 1995. EPR, electron spin echo envelope modulation, and electron nuclear double resonance studies of the 2Fe2S centers of the 2-halobenzoate 1,2-dioxygenase from Burkholderia (Pseudomonas) cepacia 2CBS. J. Biol. Chem. 270: 30869-30873.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30869-30873
    • Riedel, A.1    Fetzner, S.2    Rampp, M.3    Lingens, F.4    Liebl, U.5    Zimmermann, J.-L.6    Nitschke, W.7
  • 27
    • 0001617255 scopus 로고
    • Measurement of metal-ligand distances by EXAFS
    • Scott, R.A. 1985. Measurement of metal-ligand distances by EXAFS. Methods Enzymol. 117: 414-459.
    • (1985) Methods Enzymol. , vol.117 , pp. 414-459
    • Scott, R.A.1
  • 28
    • 0028290824 scopus 로고
    • Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: The enzymology of coupling electron transfer reactions to transmembrane proton translocation
    • Trumpower, B.L. and Gennis, R.B. 1994. Energy transduction by cytochrome complexes in mitochondrial and bacterial respiration: The enzymology of coupling electron transfer reactions to transmembrane proton translocation. Annu. Rev. Biochem. 63: 675-716.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 675-716
    • Trumpower, B.L.1    Gennis, R.B.2
  • 29
    • 0024962349 scopus 로고
    • X-ray absorption spectroscopy of the [2Fe-2S] Rieske cluster in Pseudomonas cepacia phthalate dioxygenase. Determination of core dimensions and iron ligation
    • Tsang, H.-T., Bade, C.J., Ballou, D.P., and Penner-Hahn, J.E. 1989. X-ray absorption spectroscopy of the [2Fe-2S] Rieske cluster in Pseudomonas cepacia phthalate dioxygenase. Determination of core dimensions and iron ligation. Biochemistry 28: 7233-7240.
    • (1989) Biochemistry , vol.28 , pp. 7233-7240
    • Tsang, H.-T.1    Bade, C.J.2    Ballou, D.P.3    Penner-Hahn, J.E.4
  • 31
    • 0032539991 scopus 로고    scopus 로고
    • Evidence for oxidation-state-dependent conformational changes in human ferredoxin from multinuclear, multidimensional NMR spectroscopy
    • Xia, B., Volkman, B.F., and Markley, J.L. 1998. Evidence for oxidation-state-dependent conformational changes in human ferredoxin from multinuclear, multidimensional NMR spectroscopy. Biochemistry 37: 3965-3973.
    • (1998) Biochemistry , vol.37 , pp. 3965-3973
    • Xia, B.1    Volkman, B.F.2    Markley, J.L.3


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