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Volumn 294, Issue 2, 1999, Pages 501-513

Vertebrate-type and plant-type ferredoxins: Crystal structure comparison and electron transfer pathway modelling

Author keywords

Adrenodoxin; Crystal structure; Electron transfer pathway; Ferredoxin; 2Fe 2S cluster

Indexed keywords

ADRENODOXIN; CYSTEINE; CYTOCHROME P450; FERREDOXIN; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; OXIDOREDUCTASE; SOLVENT;

EID: 0038687057     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3253     Document Type: Article
Times cited : (38)

References (54)
  • 1
  • 2
    • 0031053908 scopus 로고    scopus 로고
    • Specific aspects of electron transfer from adrenodoxin to cytochromes p450scc and p45011beta
    • Beckert V., Bernhardt R. Specific aspects of electron transfer from adrenodoxin to cytochromes p450scc and p45011beta. J. Biol. Chem. 272:1997;4883-4888.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4883-4888
    • Beckert, V.1    Bernhardt, R.2
  • 3
    • 0027980825 scopus 로고
    • Mutations of tyrosine 82 in bovine adrenodoxin that affect binding to cytochromes P45011A1 and P45011B1 but not electron transfer
    • Beckert V., Dettmer R., Bernhardt R. Mutations of tyrosine 82 in bovine adrenodoxin that affect binding to cytochromes P45011A1 and P45011B1 but not electron transfer. J. Biol. Chem. 269:1994;2568-2573.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2568-2573
    • Beckert, V.1    Dettmer, R.2    Bernhardt, R.3
  • 4
    • 0029073959 scopus 로고
    • Mutational effects on the spectroscopic properties and biological activities of oxidized bovine adrenodoxin, and their structural implications
    • Beckert V., Schrauber H., Bernhardt R., Van Dijk A. A., Kakoschke C., Wray V. Mutational effects on the spectroscopic properties and biological activities of oxidized bovine adrenodoxin, and their structural implications. Eur. J. Biochem. 231:1995;226-235.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 226-235
    • Beckert, V.1    Schrauber, H.2    Bernhardt, R.3    Van Dijk, A.A.4    Kakoschke, C.5    Wray, V.6
  • 5
    • 0026434593 scopus 로고
    • Protein electron transfer rates set by the bridging secondary and tertiary structure
    • Beratan D. N., Betts J. N., Onuchic J. N. Protein electron transfer rates set by the bridging secondary and tertiary structure. Science. 252:1991;1285-1288.
    • (1991) Science , vol.252 , pp. 1285-1288
    • Beratan, D.N.1    Betts, J.N.2    Onuchic, J.N.3
  • 6
    • 0028794689 scopus 로고    scopus 로고
    • Cytochrome P450: Structure, function, and generation of reactive oxygen species
    • Bernhardt R. Cytochrome P450: structure, function, and generation of reactive oxygen species. Rev. Physiol. Biochem. Pharmacol. 127:1996;137-221.
    • (1996) Rev. Physiol. Biochem. Pharmacol. , vol.127 , pp. 137-221
    • Bernhardt, R.1
  • 7
    • 0033570020 scopus 로고    scopus 로고
    • Crystal structure determination at 1. 4 Å resolution of ferredoxin from the green algae Chlorella fusca
    • Bes M. T., Parisini E., Inda L. A., Saraiva L., Peleato M. L., Sheldrick G. M. Crystal structure determination at 1. 4 Å resolution of ferredoxin from the green algae Chlorella fusca. Structure. 7:1999;1201-1211.
    • (1999) Structure , vol.7 , pp. 1201-1211
    • Bes, M.T.1    Parisini, E.2    Inda, L.A.3    Saraiva, L.4    Peleato, M.L.5    Sheldrick, G.M.6
  • 8
    • 0023985949 scopus 로고
    • Structure, function and evolution of bacterial ferredoxins
    • Bruschi M., Guerlesquin F. Structure, function and evolution of bacterial ferredoxins. FEMS Microbiol. Rev. 54:1988;155-176.
    • (1988) FEMS Microbiol. Rev. , vol.54 , pp. 155-176
    • Bruschi, M.1    Guerlesquin, F.2
  • 9
    • 0024576740 scopus 로고
    • Adrenodoxin with a COOH-terminal deletion (des 116-128) exhibits enhanced activity
    • Cupp J. R., Vickery L. E. Adrenodoxin with a COOH-terminal deletion (des 116-128) exhibits enhanced activity. J. Biol. Chem. 264:1989;1602-1607.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1602-1607
    • Cupp, J.R.1    Vickery, L.E.2
  • 11
    • 0025234580 scopus 로고
    • Identification of localized redox states in plant-type two-iron ferredoxins using the nuclear Overhauser effect
    • Dugad L. B., La Mar G. N., Banci L., Bertini I. Identification of localized redox states in plant-type two-iron ferredoxins using the nuclear Overhauser effect. Biochemistry. 29:1990;2263-2271.
    • (1990) Biochemistry , vol.29 , pp. 2263-2271
    • Dugad, L.B.1    La Mar, G.N.2    Banci, L.3    Bertini, I.4
  • 12
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf R. M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. 15:1997;133-138.
    • (1997) J. Mol. Graph. , vol.15 , pp. 133-138
    • Esnouf, R.M.1
  • 13
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans S. V. SETOR: hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11:1993;134-138.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 14
    • 0030010138 scopus 로고    scopus 로고
    • Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin
    • Frolow F., Harel M., Sussman J. L., Mevarech M., Shoham M. Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin. Nature Struct. Biol. 3:1996;452-458.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 452-458
    • Frolow, F.1    Harel, M.2    Sussman, J.L.3    Mevarech, M.4    Shoham, M.5
  • 15
    • 0029055861 scopus 로고
    • Tertiary structure of [2Fe-2S] ferredoxin from Spirulina platensis refined at 2.5 Å resolution: Structural comparisons of plant-type ferredoxins and an electrostatic potential analysis
    • Fukuyama K., Ueki N., Nakamura H., Tsukihara T., Matsubara H. Tertiary structure of [2Fe-2S] ferredoxin from Spirulina platensis refined at 2.5 Å resolution: structural comparisons of plant-type ferredoxins and an electrostatic potential analysis. J. Biochem. 117:1995;1017-1023.
    • (1995) J. Biochem. , vol.117 , pp. 1017-1023
    • Fukuyama, K.1    Ueki, N.2    Nakamura, H.3    Tsukihara, T.4    Matsubara, H.5
  • 16
    • 0032575490 scopus 로고    scopus 로고
    • Structural and functional consequences of substitutions at the Pro108-Arg14 hydrogen bond in bovine adrenodoxin
    • Grinberg A., Bernhardt R. Structural and functional consequences of substitutions at the Pro108-Arg14 hydrogen bond in bovine adrenodoxin. Biochem. Biophys. Res. Commun. 249:1998;933-937.
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 933-937
    • Grinberg, A.1    Bernhardt, R.2
  • 18
    • 0003742069 scopus 로고
    • Department of Chemistry and Molecular Biology,University College London
    • Hubbard S. J., Thornton J. M. NACCESS, computer program. 1993;Department of Chemistry and Molecular Biology,University College London.
    • (1993) NACCESS, Computer Program
    • Hubbard, S.J.1    Thornton, J.M.2
  • 20
    • 0025119856 scopus 로고
    • HERA - A program to draw schematic diagrams of protein secondary structures
    • Hutchinson E. G., Thornton J. M. HERA - a program to draw schematic diagrams of protein secondary structures. Proteins: Struct. Funct. Genet. 8:1990;203-212.
    • (1990) Proteins: Struct. Funct. Genet. , vol.8 , pp. 203-212
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 22
    • 0027301957 scopus 로고
    • Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena
    • Jacobson B. L., Chae Y. K., Markley J. L., Rayment I., Holden H. M. Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena. Biochemistry. 32:1993;6788-6793.
    • (1993) Biochemistry , vol.32 , pp. 6788-6793
    • Jacobson, B.L.1    Chae, Y.K.2    Markley, J.L.3    Rayment, I.4    Holden, H.M.5
  • 23
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T. A., Zou J.-Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 24
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 25
    • 0030841589 scopus 로고    scopus 로고
    • Detecting folding motifs and similarities in protein structures
    • Kleywegt G. J., Jones T. A. Detecting folding motifs and similarities in protein structures. Methods Enzymol. 277:1997;525-545.
    • (1997) Methods Enzymol. , vol.277 , pp. 525-545
    • Kleywegt, G.J.1    Jones, T.A.2
  • 26
    • 0026097297 scopus 로고
    • Ferredoxin-dependent chloroplast enzymes
    • Knaff D. B., Hirasawa M. Ferredoxin-dependent chloroplast enzymes. Biochim. Biophys. Acta. 1056:1991;93-125.
    • (1991) Biochim. Biophys. Acta , vol.1056 , pp. 93-125
    • Knaff, D.B.1    Hirasawa, M.2
  • 27
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis J. P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, J.P.1
  • 28
    • 0002108871 scopus 로고
    • Enzymology of mitochondrial side-chain cleavage by cytochrome P-450scc
    • K. Ruckpaul, & H. Rein. Berlin: Akademie-Verlag
    • Lambeth J. D. Enzymology of mitochondrial side-chain cleavage by cytochrome P-450scc. Ruckpaul K., Rein H. Frontiers in Biotransformation. 1990;58-100 Akademie-Verlag, Berlin.
    • (1990) Frontiers in Biotransformation , pp. 58-100
    • Lambeth, J.D.1
  • 29
    • 0343052039 scopus 로고    scopus 로고
    • Preparation and crystallization of a cross-linked complex of bovine adrenodoxin and adrenodoxin reductase
    • Lapko A., Müller A., Heese O., Ruckpaul K., Heinemann U. Preparation and crystallization of a cross-linked complex of bovine adrenodoxin and adrenodoxin reductase. Proteins: Struct. Funct. Genet. 28:1997;289-292.
    • (1997) Proteins: Struct. Funct. Genet. , vol.28 , pp. 289-292
    • Lapko, A.1    Müller, A.2    Heese, O.3    Ruckpaul, K.4    Heinemann, U.5
  • 30
    • 0028881975 scopus 로고
    • SURFNET: A program for visualizing molecular surfaces, cavities and intermolecular interactions
    • Laskowski R. A. SURFNET: a program for visualizing molecular surfaces, cavities and intermolecular interactions. J. Mol. Graph. 13:1995;323-330.
    • (1995) J. Mol. Graph. , vol.13 , pp. 323-330
    • Laskowski, R.A.1
  • 31
    • 0025852624 scopus 로고
    • Proton nuclear magnetic resonance of adrenodoxin
    • Miura S., Ichikawa Y. Proton nuclear magnetic resonance of adrenodoxin. Eur. J. Biochem. 197:1991a;747-757.
    • (1991) Eur. J. Biochem. , vol.197 , pp. 747-757
    • Miura, S.1    Ichikawa, Y.2
  • 32
    • 0025809263 scopus 로고
    • Conformational change of adrenodoxin induced by reduction of iron-sulfur cluster
    • Miura S., Ichikawa Y. Conformational change of adrenodoxin induced by reduction of iron-sulfur cluster. J. Biol. Chem. 266:1991b;6252-6258.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6252-6258
    • Miura, S.1    Ichikawa, Y.2
  • 33
    • 0032520951 scopus 로고    scopus 로고
    • New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108)
    • Müller A., Müller J. J., Muller Y. A., Uhlmann H., Bernhardt R., Heinemann U. New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108). Structure. 6:1998;269-280.
    • (1998) Structure , vol.6 , pp. 269-280
    • Müller, A.1    Müller, J.J.2    Muller, Y.A.3    Uhlmann, H.4    Bernhardt, R.5    Heinemann, U.6
  • 34
    • 0025854571 scopus 로고
    • X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa
    • Nar H., Messerschmidt A., Huber R., van de Kamp M., Canters G. W. X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa. J. Mol. Biol. 218:1991;427-447.
    • (1991) J. Mol. Biol. , vol.218 , pp. 427-447
    • Nar, H.1    Messerschmidt, A.2    Huber, R.3    Van De Kamp, M.4    Canters, G.W.5
  • 35
    • 0029107760 scopus 로고
    • The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue
    • Nassar N., Horn G., Herrmann Ch., Scherer A., McCormick F., Wittinghofer A. The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature. 375:1995;554-560.
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, Ch.3    Scherer, A.4    McCormick, F.5    Wittinghofer, A.6
  • 36
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K. A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 37
    • 0001011321 scopus 로고
    • Comparison of three-dimensional structures of homologous proteins
    • Overington J. P. Comparison of three-dimensional structures of homologous proteins. Curr. Opin. Struct. Biol. 2:1992;394-401.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 394-401
    • Overington, J.P.1
  • 38
    • 0028307538 scopus 로고
    • An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas
    • Pochapsky T. C., Ye X. M., Ratnaswamy G., Lyons T. A. An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas. Biochemistry. 33:1994;6424-6432.
    • (1994) Biochemistry , vol.33 , pp. 6424-6432
    • Pochapsky, T.C.1    Ye, X.M.2    Ratnaswamy, G.3    Lyons, T.A.4
  • 40
  • 41
    • 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., Holden H. M. Crystallization and structure determination to 2.5-Å resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120. Biochemistry. 30:1991;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
  • 42
    • 0029824469 scopus 로고    scopus 로고
    • Different effects of carboxy-terminal deletion in the adrenodoxin molecule on cytochrome c and acetylated cytochrome c reductions
    • Sagara Y., Hara T., Ariyasu Y., Kajiyama A., Yasukochi T., Horiuchi T. Different effects of carboxy-terminal deletion in the adrenodoxin molecule on cytochrome c and acetylated cytochrome c reductions. Biol. Pharm. Bull. 19:1996;1401-1406.
    • (1996) Biol. Pharm. Bull. , vol.19 , pp. 1401-1406
    • Sagara, Y.1    Hara, T.2    Ariyasu, Y.3    Kajiyama, A.4    Yasukochi, T.5    Horiuchi, T.6
  • 44
    • 0001531848 scopus 로고    scopus 로고
    • Protein control of redox potentials of iron-sulfur proteins
    • -2513
    • Stephens P. J., Jollie D. R., Warshel A. Protein control of redox potentials of iron-sulfur proteins. Chem. Rev. 96:1996;2491-2513.
    • (1996) Chem. Rev. , vol.96 , pp. 2491
    • Stephens, P.J.1    Jollie, D.R.2    Warshel, A.3
  • 45
    • 0024528790 scopus 로고
    • Protein adaptation to extreme salinity: The crystal structure of 2Fe-2S ferredoxin from Halobacterium marismortui
    • Sussman J. L., Shoham M., Harel M. Protein adaptation to extreme salinity: the crystal structure of 2Fe-2S ferredoxin from Halobacterium marismortui. Prog. Clin. Biol. Res. 289:1989;171-187.
    • (1989) Prog. Clin. Biol. Res. , vol.289 , pp. 171-187
    • Sussman, J.L.1    Shoham, M.2    Harel, M.3
  • 46
    • 0000133490 scopus 로고
    • Ferredoxins as electron carriers in photosynthesis and in the biological production and consumption of hydrogen gas
    • Tagawa K., Arnon D. I. Ferredoxins as electron carriers in photosynthesis and in the biological production and consumption of hydrogen gas. Nature. 195:1962;537-543.
    • (1962) Nature , vol.195 , pp. 537-543
    • Tagawa, K.1    Arnon, D.I.2
  • 47
    • 0019739089 scopus 로고
    • X-ray analysis of a [2Fe-2S] ferredoxin from Spirulina platensis. Main chain fold and location of side-chains at 2.5 Å resolution
    • Tsukihara T., Fukuyama K., Nakamura M., Katsube Y., Tanaka N., Kakudo M., Wada K., Hase T., Matsubara H. X-ray analysis of a [2Fe-2S] ferredoxin from Spirulina platensis. Main chain fold and location of side-chains at 2.5 Å resolution. J. Biochem. 90:1981;1763-1773.
    • (1981) J. Biochem. , vol.90 , pp. 1763-1773
    • Tsukihara, T.1    Fukuyama, K.2    Nakamura, M.3    Katsube, Y.4    Tanaka, N.5    Kakudo, M.6    Wada, K.7    Hase, T.8    Matsubara, H.9
  • 49
    • 0023664641 scopus 로고
    • The use of a specific fluorescence probe to study the interaction of adrenodoxin with adrenodoxin reductase and cytochrome P-450scc
    • Tuls J., Geren L. M., Lambeth J. D., Millett F. The use of a specific fluorescence probe to study the interaction of adrenodoxin with adrenodoxin reductase and cytochrome P-450scc. J. Biol. Chem. 262:1987;10020-10025.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10020-10025
    • Tuls, J.1    Geren, L.M.2    Lambeth, J.D.3    Millett, F.4
  • 50
    • 0029560248 scopus 로고
    • The role of threonine 54 in adrenodoxin for the properties of its iron-sulfur cluster and its electron transfer function
    • Uhlmann H., Bernhardt R. The role of threonine 54 in adrenodoxin for the properties of its iron-sulfur cluster and its electron transfer function. J. Biol. Chem. 270:1995;29959-29966.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29959-29966
    • Uhlmann, H.1    Bernhardt, R.2
  • 51
    • 0027979002 scopus 로고
    • C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450
    • Uhlmann H., Kraft R., Bernhardt R. C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450. J. Biol. Chem. 269:1994;22557-22564.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22557-22564
    • Uhlmann, H.1    Kraft, R.2    Bernhardt, R.3
  • 52
    • 0030864409 scopus 로고    scopus 로고
    • Pro108 is important for folding and stabilization of adrenal ferredoxin, but does not influence the functional properties of the protein
    • Uhlmann H., Iametti S., Vecchio G., Bonomi F., Bernhardt R. Pro108 is important for folding and stabilization of adrenal ferredoxin, but does not influence the functional properties of the protein. Eur. J. Biochem. 248:1997;897-902.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 897-902
    • Uhlmann, H.1    Iametti, S.2    Vecchio, G.3    Bonomi, F.4    Bernhardt, R.5
  • 53
    • 0031022337 scopus 로고    scopus 로고
    • Molecular recognition and electron transfer in mitochondrial steroid hydroxylase systems
    • Vickery L. E. Molecular recognition and electron transfer in mitochondrial steroid hydroxylase systems. Steroids. 62:1997;124-127.
    • (1997) Steroids , vol.62 , pp. 124-127
    • Vickery, L.E.1
  • 54
    • 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., Markley J. L. Evidence for oxidation-state dependent conformational changes in human ferredoxin from multinuclear, multidimensional NMR spectroscopy. Biochemistry. 37:1998;3965-3973.
    • (1998) Biochemistry , vol.37 , pp. 3965-3973
    • Xia, B.1    Volkman, B.F.2    Markley, J.L.3


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