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Volumn 71, Issue 6, 1996, Pages 2958-2969

Structural origins of redox potentials in fe-s proteins: Electrostatic potentials of crystal structures

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; IRON SULFUR PROTEIN; RUBREDOXIN; SOLVENT; VALINE;

EID: 0029753015     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79533-4     Document Type: Article
Times cited : (70)

References (46)
  • 1
    • 2742516196 scopus 로고
    • Novel iron-sulfur centers in metalloenzymes and redox proteins from extremely thermophilic bacteria
    • Adams, M. 1992. Novel iron-sulfur centers in metalloenzymes and redox proteins from extremely thermophilic bacteria. Adv. Inorg. Chem. 38: 341-396.
    • (1992) Adv. Inorg. Chem. , vol.38 , pp. 341-396
    • Adams, M.1
  • 2
    • 0026035308 scopus 로고
    • Structure of rubredoxin from Desulfovibrio vulgaris at 1.5 Å resolution
    • Adman, E., L. C. Sieker, and L. Jensen. 1991. Structure of rubredoxin from Desulfovibrio vulgaris at 1.5 Å resolution. J Mol. Biol. 217:337-352.
    • (1991) J Mol. Biol. , vol.217 , pp. 337-352
    • Adman, E.1    Sieker, L.C.2    Jensen, L.3
  • 3
    • 0001282755 scopus 로고
    • The H-S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin and Chromatium vinosum high potential iron protein
    • Adman, E., K. D. Watenpaugh, and L. H. Jensen. 1975. The H-S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin and Chromatium vinosum high potential iron protein. Proc. Natl. Acad. Sci. USA. 72:4854-4858.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 4854-4858
    • Adman, E.1    Watenpaugh, K.D.2    Jensen, L.H.3
  • 4
    • 9544223014 scopus 로고
    • Oxidation-reduction and substitution reactions of iron-sulphur centers
    • Academic Press, London
    • Armstrong, F. 1982. Oxidation-reduction and substitution reactions of iron-sulphur centers. In Advances in Inorganic and Bioinorganic Mechanisms. Academic Press, London. 65-120.
    • (1982) Advances in Inorganic and Bioinorganic Mechanisms , pp. 65-120
    • Armstrong, F.1
  • 6
    • 0028355401 scopus 로고
    • Molecular structure of the oxidized high-potential iron-sulfur protein isolated from Ectothiorhodospira vacuolata
    • Benning, M. M., T. E. Meyer, I. Rayment, and H. M. Holden. 1994. Molecular structure of the oxidized high-potential iron-sulfur protein isolated from Ectothiorhodospira vacuolata. Biochemistry. 33: 2476-2483.
    • (1994) Biochemistry , vol.33 , pp. 2476-2483
    • Benning, M.M.1    Meyer, T.E.2    Rayment, I.3    Holden, H.M.4
  • 7
    • 0025990490 scopus 로고
    • The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5 Å resolution
    • Breiter, D. R., T. E. Meyer, I. Rayment, and H. Holden. 1991. The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5 Å resolution. J. Biol. Chem. 226:18660-18667.
    • (1991) J. Biol. Chem. , vol.226 , pp. 18660-18667
    • Breiter, D.R.1    Meyer, T.E.2    Rayment, I.3    Holden, H.4
  • 9
    • 0344834199 scopus 로고
    • Iron-sulfur cluster in enzymes: Themes and variations
    • Academic Press, Inc., San Diego
    • Cammack, R. 1992. Iron-sulfur cluster in enzymes: themes and variations. In Iron-Sulfur Proteins. Academic Press, Inc., San Diego. 281-322.
    • (1992) Iron-Sulfur Proteins , pp. 281-322
    • Cammack, R.1
  • 10
    • 0016160014 scopus 로고
    • Two-angstrom crystal structure of oxidized Chromatium high potential iron protein
    • Carter, C. W., J. Kraut, S. T. Freer, N.-H. Xuong, R. A. Alden, and R. G. Bartsch. 1974. Two-angstrom crystal structure of oxidized Chromatium high potential iron protein. J. Biol. Chem. 249:4212-4225.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4212-4225
    • Carter, C.W.1    Kraut, J.2    Freer, S.T.3    Xuong, N.-H.4    Alden, R.A.5    Bartsch, R.G.6
  • 11
    • 0023044641 scopus 로고
    • Control of the redox potential of cytochrome c and microscopic dielectric effects in proteins
    • Churg, A. K., and A. Warshel. 1986. Control of the redox potential of cytochrome c and microscopic dielectric effects in proteins. Biochemistry. 25:1675-1681.
    • (1986) Biochemistry , vol.25 , pp. 1675-1681
    • Churg, A.K.1    Warshel, A.2
  • 12
    • 0027051883 scopus 로고
    • X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archebacterium Pyrococcus furiosus
    • Day, M. W., B. T. Hsu, L. Joshua-Tor, J.-B. Park, Z. H. Zhou, M. W. W. Adams, and D. C. Rees. 1992. X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archebacterium Pyrococcus furiosus. Protein Sci. 1:1494-1507.
    • (1992) Protein Sci. , vol.1 , pp. 1494-1507
    • Day, M.W.1    Hsu, B.T.2    Joshua-Tor, L.3    Park, J.-B.4    Zhou, Z.H.5    Adams, M.W.W.6    Rees, D.C.7
  • 13
    • 0023645585 scopus 로고
    • Rubredoxin from Desulfovibrio gigas. A molecular model of the oxidized form at 1.4 Å resolution
    • Frey, M. W., L. Sieker, F. Payan, R. Haser, M. Bruschi, G. Pepe, and J. LeGall. 1987. Rubredoxin from Desulfovibrio gigas. A molecular model of the oxidized form at 1.4 Å resolution. J. Mol. Biol. 197:525-541.
    • (1987) J. Mol. Biol. , vol.197 , pp. 525-541
    • Frey, M.W.1    Sieker, L.2    Payan, F.3    Haser, R.4    Bruschi, M.5    Pepe, G.6    LeGall, J.7
  • 14
    • 0003648101 scopus 로고
    • 575 Science Drive, Madison, Wisconsin, USA 53711
    • Genetics Computer Group. 1994. Program Manual for the Wisconsin Package, 575 Science Drive, Madison, Wisconsin, USA 53711.
    • (1994) Program Manual for the Wisconsin Package
  • 15
    • 0023779259 scopus 로고
    • Calculation of the total electrostatic energy of a macromolecular system: Solution energies, binding energies, and conformational analysis
    • Gilson, M. K., and B. H. Honig. 1988. Calculation of the total electrostatic energy of a macromolecular system: solution energies, binding energies, and conformational analysis. Proteins. 4:7-18.
    • (1988) Proteins , vol.4 , pp. 7-18
    • Gilson, M.K.1    Honig, B.H.2
  • 16
    • 0027054423 scopus 로고
    • Mutation of conserved residues in Escherichia coli thioredoxin: Effects on stability and function
    • Gleason, F. K. 1992. Mutation of conserved residues in Escherichia coli thioredoxin: effects on stability and function. Protein Sci. 1:609-616.
    • (1992) Protein Sci. , vol.1 , pp. 609-616
    • Gleason, F.K.1
  • 17
    • 0025944990 scopus 로고
    • Electrostatic control of midpoint potentials in the cytochrome subunit of the Rhodopseudomonas viridis reaction center
    • Gunner, M. R., and B. Honig. 1991. Electrostatic control of midpoint potentials in the cytochrome subunit of the Rhodopseudomonas viridis reaction center. Proc. Natl. Acad Sci. USA. 88:9151-9155.
    • (1991) Proc. Natl. Acad Sci. USA , vol.88 , pp. 9151-9155
    • Gunner, M.R.1    Honig, B.2
  • 18
    • 0000742502 scopus 로고
    • Apparent local dielectric response around ions in water: A method for its determination and its applications
    • Hyun, J. K., C. S. Babu, and T. Ichiye. 1995. Apparent local dielectric response around ions in water: a method for its determination and its applications. J. Phys. Chem. 99:5187-5195.
    • (1995) J. Phys. Chem. , vol.99 , pp. 5187-5195
    • Hyun, J.K.1    Babu, C.S.2    Ichiye, T.3
  • 19
    • 0028023334 scopus 로고
    • 4] clusters in Peptococcus Aerogenes ferredoxin, Azotobacter vinelandii ferredoxin I, and Chromatium vinosum high-potential iron protein
    • 4] clusters in Peptococcus Aerogenes ferredoxin, Azotobacter vinelandii ferredoxin I, and Chromatium vinosum high-potential iron protein. Biochemistry. 33:10911-10924.
    • (1994) Biochemistry , vol.33 , pp. 10911-10924
    • Jensen, G.M.1    Warshel, A.2    Stephens, P.J.3
  • 20
    • 33645858780 scopus 로고
    • Transferable intermolecular potential functions for water, alcohols, and ethers. Application to liquid water
    • Jorgensen, W. L. 1981. Transferable intermolecular potential functions for water, alcohols, and ethers. Application to liquid water. J. Am. Chem. Soc. 103:335-340.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 335-340
    • Jorgensen, W.L.1
  • 21
    • 33845376931 scopus 로고
    • Optimized intermolecular potential functions for amides and peptides. Structure and properties of liquids amides
    • Jorgensen, W. L., and C. J. Swenson. 1985. Optimized intermolecular potential functions for amides and peptides. Structure and properties of liquids amides. J. Am. Chem. Soc. 107:569-578.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 569-578
    • Jorgensen, W.L.1    Swenson, C.J.2
  • 22
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24:946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0026611315 scopus 로고
    • Effect of the Asn52-IIe mutation on the redox potential of yeast cytochrome c. Theory and experiment
    • Langen, R., G. D. Brayer, A. M. Berghuis, G. McLendon, F. Sherman, and A. Warshel. 1992a. Effect of the Asn52-IIe mutation on the redox potential of yeast cytochrome c. Theory and experiment. J. Mol. Biol. 224:589-600.
    • (1992) J. Mol. Biol. , vol.224 , pp. 589-600
    • Langen, R.1    Brayer, G.D.2    Berghuis, A.M.3    McLendon, G.4    Sherman, F.5    Warshel, A.6
  • 25
    • 0028956795 scopus 로고
    • Isolation, characterization, and primary structure of rubredoxin from the photosynthetic bacterium, Heliobacillus mobilis
    • Lee, W. Y., D. C. Brune, R. LoBrutto, and R. E. Blankenship. 1995. Isolation, characterization, and primary structure of rubredoxin from the photosynthetic bacterium, Heliobacillus mobilis. Arch. Biochem. Biophys. 318:80-88.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 80-88
    • Lee, W.Y.1    Brune, D.C.2    LoBrutto, R.3    Blankenship, R.E.4
  • 26
    • 0024281294 scopus 로고
    • Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-binuclear iron cluster
    • LeGall, J., B. C. Prickril, I. Moura, A. V. Xavier, J. J. Moura, and B. H. Huynh. 1988. Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-binuclear iron cluster. Biochemistry. 27:1636-1642.
    • (1988) Biochemistry , vol.27 , pp. 1636-1642
    • LeGall, J.1    Prickril, B.C.2    Moura, I.3    Xavier, A.V.4    Moura, J.J.5    Huynh, B.H.6
  • 27
    • 0000024186 scopus 로고
    • An integral equation theory for the structure of water around globular solutes
    • Liu, Y., and T. Ichiye. 1994. An integral equation theory for the structure of water around globular solutes. Chem. Phys. Lett. 231:380-386.
    • (1994) Chem. Phys. Lett. , vol.231 , pp. 380-386
    • Liu, Y.1    Ichiye, T.2
  • 28
    • 0013788501 scopus 로고
    • Rubredoxin: A new electron transfer protein from Clostridium pasteurianum
    • Lovenberg, W., and B. Sobel. 1965. Rubredoxin: a new electron transfer protein from Clostridium pasteurianum. Proc. Natl. Acad. Sci. USA. 54:193-199.
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 193-199
    • Lovenberg, W.1    Sobel, B.2
  • 29
    • 0001099937 scopus 로고
    • Traitement 'stastique des erreurs dans la determination des structures cristallines
    • Luzzati, V. 1952. Traitement 'stastique des erreurs dans la determination des structures cristallines. Acta Cryst. 5:802-810.
    • (1952) Acta Cryst. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 30
    • 77956772373 scopus 로고
    • Structural and functional diversity of ferredoxins and related proteins
    • Academic Press, Inc., San Diego
    • Matsubara, H., and K. Saeki. 1992. Structural and functional diversity of ferredoxins and related proteins. In Iron-Sulfur Proteins. Academic Press, Inc., San Diego. 223-281.
    • (1992) Iron-Sulfur Proteins , pp. 223-281
    • Matsubara, H.1    Saeki, K.2
  • 31
    • 0028057108 scopus 로고
    • Raster3D Version 2.0: A program for photorealistic molecular graphics
    • Merritt, E. A., and M. E. P. Murphy. 1994. Raster3D Version 2.0: a program for photorealistic molecular graphics. Acta Cryst. D50: 869-873.
    • (1994) Acta Cryst. , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 32
    • 0020851111 scopus 로고
    • Correlation between rate constant for reduction and redox potential as a basis for systematic investigation of reaction mechanisms of electron transfer proteins
    • Meyer, T. E., J. A. Prezysiecki, J. A. Watkins, A. Bhattacharyya, R. P. Simondsen, M. A. Cusanovich, and G. Tollin. 1983. Correlation between rate constant for reduction and redox potential as a basis for systematic investigation of reaction mechanisms of electron transfer proteins. Proc. Natl. Acad. Sci. U.S.A. 80:6740-6744.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 6740-6744
    • Meyer, T.E.1    Prezysiecki, J.A.2    Watkins, J.A.3    Bhattacharyya, A.4    Simondsen, R.P.5    Cusanovich, M.A.6    Tollin, G.7
  • 33
    • 0000318315 scopus 로고
    • Density functional/Poisson-Boltzmann calculations of redox potentials for iron-sulfur clusters
    • Mouesca, J. M., J. L. Chen, L. Noodleman, D. Bashford, and D. A. Case. 1994. Density functional/Poisson-Boltzmann calculations of redox potentials for iron-sulfur clusters. J. Am. Chem. Soc. 116:11898-11914.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11898-11914
    • Mouesca, J.M.1    Chen, J.L.2    Noodleman, L.3    Bashford, D.4    Case, D.A.5
  • 34
    • 0018569234 scopus 로고
    • Redox studies on rubredoxin from sulphate and sulphur reducing bacteria
    • Moura, I., J. J. G. Moura, M. H. Santos, A. V. Xavier, and J. LeGall. 1979. Redox studies on rubredoxin from sulphate and sulphur reducing bacteria. FEBS Lett. 107:419-421.
    • (1979) FEBS Lett. , vol.107 , pp. 419-421
    • Moura, I.1    Moura, J.J.G.2    Santos, M.H.3    Xavier, A.V.4    LeGall, J.5
  • 35
    • 33845378908 scopus 로고
    • Models for ferredoxins: Electronic structures of iron-sulfur clusters with one, two, and four iron atoms
    • Noodleman, L., J. G. Norman, J. H. Osborne, A. Aizman, and D. A. Case. 1985. Models for ferredoxins: electronic structures of iron-sulfur clusters with one, two, and four iron atoms. J. Am. Chem. Soc. 107:3418-3426.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 3418-3426
    • Noodleman, L.1    Norman, J.G.2    Osborne, J.H.3    Aizman, A.4    Case, D.A.5
  • 36
    • 0025368499 scopus 로고
    • Electrostatic control of charge separation in bacterial photosynthesis
    • Parson, W. W., Z.-T. Chu, and A. Warshel. 1990. Electrostatic control of charge separation in bacterial photosynthesis. Biochim. Biophys. Acta. 1017:251-272.
    • (1990) Biochim. Biophys. Acta , vol.1017 , pp. 251-272
    • Parson, W.W.1    Chu, Z.-T.2    Warshel, A.3
  • 37
    • 0026739955 scopus 로고
    • Three-dimensional structure of the high-potential iron-sulfur protein isolated from purple phototropic bacterium Rhodocyclus tenuis determined and refined at 1.5 Å resolution
    • Rayment, I., G. Wesenberg, T. E. Meyer, M. A. Cusanovich, and H. M. Holden. 1992. Three-dimensional structure of the high-potential iron-sulfur protein isolated from purple phototropic bacterium Rhodocyclus tenuis determined and refined at 1.5 Å resolution. J. Mol Biol. 228: 672-686.
    • (1992) J. Mol Biol. , vol.228 , pp. 672-686
    • Rayment, I.1    Wesenberg, G.2    Meyer, T.E.3    Cusanovich, M.A.4    Holden, H.M.5
  • 38
    • 0000058698 scopus 로고
    • Charge-transfer optical spectra, electron paramagnetic resonance, and redox potentials of cytochromes
    • Schejter, A., and W. A. Eaton. 1984. Charge-transfer optical spectra, electron paramagnetic resonance, and redox potentials of cytochromes. Biochemistry. 23:1081-1084.
    • (1984) Biochemistry , vol.23 , pp. 1081-1084
    • Schejter, A.1    Eaton, W.A.2
  • 40
    • 0027490297 scopus 로고
    • Influence of protein flexibility on the redox potential of rubredoxin: Energy minimization studies
    • Shenoy, V. S., and T. Ichiye. 1993. Influence of protein flexibility on the redox potential of rubredoxin: energy minimization studies. Proteins. 17:152-160.
    • (1993) Proteins , vol.17 , pp. 152-160
    • Shenoy, V.S.1    Ichiye, T.2
  • 41
    • 0022967931 scopus 로고
    • Structure of rubredoxin from the bacterium Desulfovibrio desulfuricans
    • Sieker, L. C., R. E. Stenkamp, L. H. Jensen, B. Pickril, and J. LeGall. 1986. Structure of rubredoxin from the bacterium Desulfovibrio desulfuricans. FEBS Lett. 208:73-76.
    • (1986) FEBS Lett. , vol.208 , pp. 73-76
    • Sieker, L.C.1    Stenkamp, R.E.2    Jensen, L.H.3    Pickril, B.4    LeGall, J.5
  • 43
    • 0018881587 scopus 로고
    • Proteins containing 4Fe-4S clusters: An overview
    • Sweeney, W. V., and J. C. Rabinowitz. 1980. Proteins containing 4Fe-4S clusters: an overview. Ann. Rev. Biochem. 49:139-161.
    • (1980) Ann. Rev. Biochem. , vol.49 , pp. 139-161
    • Sweeney, W.V.1    Rabinowitz, J.C.2
  • 44
    • 0019325181 scopus 로고
    • Crystallographic refinement of rubredoxin at 1.2 Å resolution
    • Watenpaugh, K. D., L. C. Sieker, and L. H. Jensen. 1980. Crystallographic refinement of rubredoxin at 1.2 Å resolution. J. Mol Biol. 138:615-633.
    • (1980) J. Mol Biol. , vol.138 , pp. 615-633
    • Watenpaugh, K.D.1    Sieker, L.C.2    Jensen, L.H.3
  • 45
    • 0028998016 scopus 로고
    • Molecular dynamics simulations of rubredoxin from Clostridium pasteurianum: Changes in structure and electrostatic potential during redox reactions
    • Yelle, R. B., N. S. Park, and T. Ichiye. 1995. Molecular dynamics simulations of rubredoxin from Clostridium pasteurianum: changes in structure and electrostatic potential during redox reactions. Proteins Struct. Funct. Genet. 22:154-167.
    • (1995) Proteins Struct. Funct. Genet. , vol.22 , pp. 154-167
    • Yelle, R.B.1    Park, N.S.2    Ichiye, T.3
  • 46
    • 0001751647 scopus 로고    scopus 로고
    • Protein determinants of metal site reduction potentials: Site directed mutagenesis studies of Clostridium pasteurianum rubredoxin
    • Zeng, Q., E. T. Smith, D. M. Kurtz, and R. A. Scott. 1996. Protein determinants of metal site reduction potentials: site directed mutagenesis studies of Clostridium pasteurianum rubredoxin. Inorg. Chim. Acta. 242:245-251.
    • (1996) Inorg. Chim. Acta , vol.242 , pp. 245-251
    • Zeng, Q.1    Smith, E.T.2    Kurtz, D.M.3    Scott, R.A.4


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