메뉴 건너뛰기




Volumn 321, Issue 5, 2002, Pages 923-938

Computational de novo design, and characterization of an A2B2 diiron protein

Author keywords

Coiled coil; Computational design; de novo design; Heterotetramer; Retrostructural analysis

Indexed keywords

CARRIER PROTEIN; COBALT; DIIRON PROTEIN; METHANE MONOOXYGENASE; PEPTIDE; PROTEIN; RIBONUCLEOTIDE REDUCTASE; UNCLASSIFIED DRUG; ZINC;

EID: 0036385840     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00589-2     Document Type: Article
Times cited : (119)

References (114)
  • 1
    • 0032835617 scopus 로고    scopus 로고
    • De novo design and structural characterization of proteins and metalloproteins
    • DeGrado, W. F., Summa, C. M., Pavone, V., Nastri, F. & Lombardi, A. (1999). De novo design and structural characterization of proteins and metalloproteins. Annu. Rev. Biochem. 68, 779-819.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 779-819
    • DeGrado, W.F.1    Summa, C.M.2    Pavone, V.3    Nastri, F.4    Lombardi, A.5
  • 2
    • 0035471132 scopus 로고    scopus 로고
    • De novo proteins from combinatorial libraries
    • Moffet, D. A. & Hecht, M. H. (2001). De novo proteins from combinatorial libraries. Chem. Rev. 101, 3191-3203.
    • (2001) Chem. Rev. , vol.101 , pp. 3191-3203
    • Moffet, D.A.1    Hecht, M.H.2
  • 3
    • 0032499535 scopus 로고    scopus 로고
    • 2 zinc binding sites in the hydrophobic core of thioredoxin by structure-based design
    • 2 zinc binding sites in the hydrophobic core of thioredoxin by structure-based design. Biochemistry, 37, 8269-8277.
    • (1998) Biochemistry , vol.37 , pp. 8269-8277
    • Wisz, M.S.1    Garrett, C.Z.2    Hellinga, H.W.3
  • 4
    • 0026335211 scopus 로고
    • Construction of new ligand-binding sites in proteins of known structure I. Computer-aided modeling of sites with pre-defined geometry
    • Hellinga, H. W. & Richards, F. M. (1991). Construction of new ligand-binding sites in proteins of known structure I. Computer-aided modeling of sites with pre-defined geometry. J. Mol. Biol. 222, 763-785.
    • (1991) J. Mol. Biol. , vol.222 , pp. 763-785
    • Hellinga, H.W.1    Richards, F.M.2
  • 5
    • 0030917147 scopus 로고    scopus 로고
    • The rational design and construction of a cuboidal iron-sulfur protein
    • Coldren, C., Hellinga, H. W. & Caradonna, J. P. (1997). The rational design and construction of a cuboidal iron-sulfur protein. Proc. Natl Acad. Sci. USA, 94, 6635-6640.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6635-6640
    • Coldren, C.1    Hellinga, H.W.2    Caradonna, J.P.3
  • 6
    • 0032546610 scopus 로고    scopus 로고
    • Construction of a novel redox protein by rational design: Conversion of a disulfide bridge into a mononuclear iron-sulfur center
    • Benson, D. E., Wisz, M. S., Liu, W. & Hellinga, H. W. (1998). Construction of a novel redox protein by rational design: conversion of a disulfide bridge into a mononuclear iron-sulfur center. Biochemistry, 37, 7070-7076.
    • (1998) Biochemistry , vol.37 , pp. 7070-7076
    • Benson, D.E.1    Wisz, M.S.2    Liu, W.3    Hellinga, H.W.4
  • 9
    • 0032477890 scopus 로고    scopus 로고
    • A designed cavity in the hydrophobic core of a four-alpha-helix bundle improves volatile anesthetic binding affinity
    • Johansson, J. S., Gibney, B. R., Rabanal, F., Reddy, K. S. & Dutton, P. L. (1998). A designed cavity in the hydrophobic core of a four-alpha-helix bundle improves volatile anesthetic binding affinity. Biochemistry, 37, 1421-1429.
    • (1998) Biochemistry , vol.37 , pp. 1421-1429
    • Johansson, J.S.1    Gibney, B.R.2    Rabanal, F.3    Reddy, K.S.4    Dutton, P.L.5
  • 10
    • 0033543133 scopus 로고    scopus 로고
    • Determination of nonligand amino acids critical to [4Fe-4S]2 +/+ assembly in ferredoxin maquettes
    • Mulholland, S. E., Gibney, B. R., Rabanal, F. & Dutton, P. L. (1999). Determination of nonligand amino acids critical to [4Fe-4S]2 +/+ assembly in ferredoxin maquettes. Biochemistry, 38, 10442-10448.
    • (1999) Biochemistry , vol.38 , pp. 10442-10448
    • Mulholland, S.E.1    Gibney, B.R.2    Rabanal, F.3    Dutton, P.L.4
  • 11
    • 0030066841 scopus 로고    scopus 로고
    • Toward the synthesis of a photosynthetic reaction center maquette: A cofacial porphyrin pair assembled between two subunits of a synthetic four-helix bundle multiheme protein
    • Rabanal, F., DeGrado, W. F. & Dutton, P. L. (1996). Toward the synthesis of a photosynthetic reaction center maquette: a cofacial porphyrin pair assembled between two subunits of a synthetic four-helix bundle multiheme protein. J. Am. Chem. Soc. 118, 473-474.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 473-474
    • Rabanal, F.1    DeGrado, W.F.2    Dutton, P.L.3
  • 14
    • 0032516785 scopus 로고    scopus 로고
    • From synthetic coiled coils to functional proteins: Automated design of a receptor for the calmodulin-binding domain of calcineurin
    • Ghirlanda, G., Lear, J. D., Lombardi, A. & DeGrado, W. F. (1998). From synthetic coiled coils to functional proteins: automated design of a receptor for the calmodulin-binding domain of calcineurin. J. Mol. Biol. 281, 379-391.
    • (1998) J. Mol. Biol. , vol.281 , pp. 379-391
    • Ghirlanda, G.1    Lear, J.D.2    Lombardi, A.3    DeGrado, W.F.4
  • 15
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root, M. J., Kay, M. S. & Kim, P. S. (2001). Protein design of an HIV-1 entry inhibitor. Science, 291, 884-888.
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 16
    • 0030978103 scopus 로고    scopus 로고
    • Construction of a catalytically active iron superoxide dismutase by rational design
    • Pinto, A., Hellinga, H. W. & Caradonna, J. P. (1997). Construction of a catalytically active iron superoxide dismutase by rational design. Proc. Natl Acad. Sci. USA, 94, 5562-5567.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5562-5567
    • Pinto, A.1    Hellinga, H.W.2    Caradonna, J.P.3
  • 17
    • 0032493468 scopus 로고    scopus 로고
    • Engineering steroid 5 beta;-reductase activity into rat liver 3 α-hydroxysteroid dehydrogenase
    • Jez, J. M. & Penning, T. M. (1998). Engineering steroid 5 β-reductase activity into rat liver 3 α-hydroxysteroid dehydrogenase. Biochemistry, 37, 9695-9703.
    • (1998) Biochemistry , vol.37 , pp. 9695-9703
    • Jez, J.M.1    Penning, T.M.2
  • 19
    • 0027997157 scopus 로고
    • Protein engineering to study enzyme catalytic mechanisms
    • Gerlt, J. A. (1994). Protein engineering to study enzyme catalytic mechanisms. Curr. Opin. Struct. Biol. 4, 593-597.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 593-597
    • Gerlt, J.A.1
  • 20
    • 0026901661 scopus 로고
    • Alteration of enzyme specificity and catalysis
    • Douglas, K. T. (1992). Alteration of enzyme specificity and catalysis. Curr. Opin. Biotechnol. 3, 370-377.
    • (1992) Curr. Opin. Biotechnol. , vol.3 , pp. 370-377
    • Douglas, K.T.1
  • 21
    • 0242449394 scopus 로고    scopus 로고
    • Enzymes by design: Chemogenetic assembly of transamination active sites containing lysine residues for covalent catalysis
    • Haering, D. & Distefano, M. D. (2001). Enzymes by design: chemogenetic assembly of transamination active sites containing lysine residues for covalent catalysis. Bioconj. Chem. 12, 385-390.
    • (2001) Bioconj. Chem. , vol.12 , pp. 385-390
    • Haering, D.1    Distefano, M.D.2
  • 22
    • 0034794047 scopus 로고    scopus 로고
    • Creation of an enantioselective hydrolase by engineered substrate-assisted catalysis
    • Magnusson, A., Hult, K. & Holmquist, M. (2001). Creation of an enantioselective hydrolase by engineered substrate-assisted catalysis. J. Am. Chem. Soc. 123, 4354-4355.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 4354-4355
    • Magnusson, A.1    Hult, K.2    Holmquist, M.3
  • 23
    • 0034470083 scopus 로고    scopus 로고
    • Creating lipoxygenases with new positional specificities by site-directed mutagenesis
    • Hornung, E., Rosahl, S., Kuhn, H. & Feussner, I. (2000). Creating lipoxygenases with new positional specificities by site-directed mutagenesis. Biochem. Soc. Trans. 28, 825-826.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 825-826
    • Hornung, E.1    Rosahl, S.2    Kuhn, H.3    Feussner, I.4
  • 24
    • 0034662931 scopus 로고    scopus 로고
    • Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation
    • Nilsson, L. O., Gustafsson, A. & Mannervik, B. (2000). Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation. Proc. Natl Acad. Sci. USA, 97, 9408-9412.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9408-9412
    • Nilsson, L.O.1    Gustafsson, A.2    Mannervik, B.3
  • 25
    • 0032534916 scopus 로고    scopus 로고
    • Conversion of a catalytic into a structural disulfide bond by circular permutation
    • Hennecke, J. & Glockshuber, R. (1998). Conversion of a catalytic into a structural disulfide bond by circular permutation. Biochemistry, 37, 17590-17597.
    • (1998) Biochemistry , vol.37 , pp. 17590-17597
    • Hennecke, J.1    Glockshuber, R.2
  • 26
    • 0032143901 scopus 로고    scopus 로고
    • The design of protein-based catalysts using semisynthetic methods
    • Distefano, M. D., Kuang, H., Qi, D. & Mazhary, A. (1998). The design of protein-based catalysts using semisynthetic methods. Curr. Opin. Struct. Biol. 8, 459-465.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 459-465
    • Distefano, M.D.1    Kuang, H.2    Qi, D.3    Mazhary, A.4
  • 29
    • 0035313593 scopus 로고    scopus 로고
    • Improved biocatalysis by directed evolution and rational protein design
    • Bornscheuer, U. T. & Pohl, M. (2001). Improved biocatalysis by directed evolution and rational protein design. Curr. Opin. Chem. Biol. 5, 137-143.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 137-143
    • Bornscheuer, U.T.1    Pohl, M.2
  • 31
    • 0031543435 scopus 로고    scopus 로고
    • Directed evolution of enzyme catalyts
    • Kuchner, O. & Arnold, F. H. (1997). Directed evolution of enzyme catalyts. Trends Biotechnol. 15, 523-530.
    • (1997) Trends Biotechnol. , vol.15 , pp. 523-530
    • Kuchner, O.1    Arnold, F.H.2
  • 32
    • 0035424404 scopus 로고    scopus 로고
    • Advances in directed protein evolution by recursive genetic recombination: Applications to therapeutic proteins
    • Kurtzman, A. L., Govindarajan, S., Vahle, K., Jones, J. T., Heinrichs, V. & Patten, P. A. (2001). Advances in directed protein evolution by recursive genetic recombination: applications to therapeutic proteins. Curr. Opin. Biotechnol. 12, 361-370.
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 361-370
    • Kurtzman, A.L.1    Govindarajan, S.2    Vahle, K.3    Jones, J.T.4    Heinrichs, V.5    Patten, P.A.6
  • 33
    • 0033908030 scopus 로고    scopus 로고
    • Designed evolution of enzymatic properties
    • Petrounia, I. P. & Arnold, F. H. (2000). Designed evolution of enzymatic properties. Curr. Opin. Biotechnol. 11, 325-330.
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 325-330
    • Petrounia, I.P.1    Arnold, F.H.2
  • 34
    • 0034603040 scopus 로고    scopus 로고
    • Enantioselective enzymes for organic synthesis created by directed evolution
    • Reetz, M. T. & Jaeger, K. E. (2000). Enantioselective enzymes for organic synthesis created by directed evolution. Chemistry, 6, 407-412.
    • (2000) Chemistry , vol.6 , pp. 407-412
    • Reetz, M.T.1    Jaeger, K.E.2
  • 39
    • 0033178525 scopus 로고    scopus 로고
    • Beyond binding: Using phage display to select for structure, folding, and enzymatic activity in proteins
    • Forrer, P., Jung, S. & Pluckthun, A. (1999). Beyond binding: using phage display to select for structure, folding, and enzymatic activity in proteins. Curr. Opin. Struct. Biol. 9, 514-520.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 514-520
    • Forrer, P.1    Jung, S.2    Pluckthun, A.3
  • 40
    • 0035424963 scopus 로고    scopus 로고
    • In vitro display technologies: Novel developments and applications
    • Amstutz, P., Forrer, P., Zahnd, C. & Pluckthun, A. (2001). In vitro display technologies: novel developments and applications. Curr. Opin. Biotechnol. 12, 400-405.
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 400-405
    • Amstutz, P.1    Forrer, P.2    Zahnd, C.3    Pluckthun, A.4
  • 41
    • 0033578390 scopus 로고    scopus 로고
    • Selection for improved subtiligases by phage display
    • Atwell, S. & Wells, J. A. (1999). Selection for improved subtiligases by phage display. Proc. Natl Acad. Sci. USA, 96, 9497-9502.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 9497-9502
    • Atwell, S.1    Wells, J.A.2
  • 42
    • 0030955262 scopus 로고    scopus 로고
    • Mechanism-based phage display selection of active-site mutants of human glutathione transferase A1-1 catalyzing SNAr reactions
    • Hansson, L. O., Widersten, M. & Mannervik, B. (1997). Mechanism-based phage display selection of active-site mutants of human glutathione transferase A1-1 catalyzing SNAr reactions. Biochemistry, 36, 11252-11260.
    • (1997) Biochemistry , vol.36 , pp. 11252-11260
    • Hansson, L.O.1    Widersten, M.2    Mannervik, B.3
  • 43
    • 0033583548 scopus 로고    scopus 로고
    • A method for the selection of catalytic activity using phage display and proximity coupling
    • Jestin, J. L., Kristensen, P. & Winter, G. (1999). A method for the selection of catalytic activity using phage display and proximity coupling. Angew. Chem. 38, 1124-1127.
    • (1999) Angew. Chem. , vol.38 , pp. 1124-1127
    • Jestin, J.L.1    Kristensen, P.2    Winter, G.3
  • 44
    • 0035926124 scopus 로고    scopus 로고
    • Phage display selection of peptides possessing aldolase activity
    • Tanaka, F. & Barbas, C. F. (2001). Phage display selection of peptides possessing aldolase activity. Chem. Commun. 8, 769-770.
    • (2001) Chem. Commun. , vol.8 , pp. 769-770
    • Tanaka, F.1    Barbas, C.F.2
  • 45
    • 0033819491 scopus 로고    scopus 로고
    • Design and use of phage display libraries for the selection of antibodies and enzymes
    • Viti, F., Nilsson, F., Demartis, S., Huber, A. & Neri, D. (2000). Design and use of phage display libraries for the selection of antibodies and enzymes. Methods Enzymol. 326, 480-505.
    • (2000) Methods Enzymol. , vol.326 , pp. 480-505
    • Viti, F.1    Nilsson, F.2    Demartis, S.3    Huber, A.4    Neri, D.5
  • 46
    • 0033751393 scopus 로고    scopus 로고
    • Use of phage display and transition-state analogs to select enzyme variants with altered catalytic properties: Glutathione transferase as an example
    • Widersten, M., Hansson, L. O., Trontad, L. O. & Mannervik, B. (2000). Use of phage display and transition-state analogs to select enzyme variants with altered catalytic properties: glutathione transferase as an example. Methods Enzymol. 328, 389-404.
    • (2000) Methods Enzymol. , vol.328 , pp. 389-404
    • Widersten, M.1    Hansson, L.O.2    Trontad, L.O.3    Mannervik, B.4
  • 47
    • 0035059933 scopus 로고    scopus 로고
    • Proton and metal ion-dependent assembly of a model diiron protein
    • Pasternak, A., Kaplan, J., Lear, J. D. & DeGrado, W. F. (2001). Proton and metal ion-dependent assembly of a model diiron protein. Protein Sci. 10, 958-969.
    • (2001) Protein Sci. , vol.10 , pp. 958-969
    • Pasternak, A.1    Kaplan, J.2    Lear, J.D.3    DeGrado, W.F.4
  • 50
    • 0028090067 scopus 로고
    • Biochemistry of soluble methane monooxygenase
    • Lipscomb, J. D. (1994). Biochemistry of soluble methane monooxygenase. Annu. Rev. Microbiol. 48, 371-399.
    • (1994) Annu. Rev. Microbiol. , vol.48 , pp. 371-399
    • Lipscomb, J.D.1
  • 51
    • 0001618049 scopus 로고
    • Studies of the soluble methane monooxygenase protein system: Structure, component interactions, and hydroxylation mechanism
    • Liu, K. & Lippard, S. J. (1995). Studies of the soluble methane monooxygenase protein system: structure, component interactions, and hydroxylation mechanism. Advan. Inorg. Chem. 42, 263-289.
    • (1995) Advan. Inorg. Chem. , vol.42 , pp. 263-289
    • Liu, K.1    Lippard, S.J.2
  • 52
    • 0000106976 scopus 로고    scopus 로고
    • Modeling the oxygen activation chemistry of methane monooxygenase and ribonucleotide reductase
    • Que, L. & Dong, Y. (1996). Modeling the oxygen activation chemistry of methane monooxygenase and ribonucleotide reductase. Accts Chem. Res. 29, 190-196.
    • (1996) Accts Chem. Res. , vol.29 , pp. 190-196
    • Que, L.1    Dong, Y.2
  • 53
    • 0031837180 scopus 로고    scopus 로고
    • Substrate binding and C-H bond activation in the soluble methane monooxygenase hydroxylase
    • Whittington, D. A., Valentine, A. M. & Lippard, S. J. (1998). Substrate binding and C-H bond activation in the soluble methane monooxygenase hydroxylase. J. Biol. Inorg. Chem. 3, 307-313.
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 307-313
    • Whittington, D.A.1    Valentine, A.M.2    Lippard, S.J.3
  • 54
    • 0009411657 scopus 로고
    • Reactions of non-heme iron(II) centers with diooxygen in biology and chemistry
    • Feig, A. L. & Lippard, S. J. (1994). Reactions of non-heme iron(II) centers with diooxygen in biology and chemistry. Chem. Rev. 94, 759-805.
    • (1994) Chem. Rev. , vol.94 , pp. 759-805
    • Feig, A.L.1    Lippard, S.J.2
  • 56
    • 33748496035 scopus 로고    scopus 로고
    • Oxygen activation at non-heme diiron active sites in biology: Lessons from model complexes
    • Que, L. (1997). Oxygen activation at non-heme diiron active sites in biology: lessons from model complexes. J. Chem. Soc., Dalton Trans. 21, 3933-3940.
    • (1997) J. Chem. Soc., Dalton Trans. , vol.21 , pp. 3933-3940
    • Que, L.1
  • 57
    • 0000239991 scopus 로고    scopus 로고
    • Dioxygen activation by enzyme containing binuclear non-heme iron clusters
    • Wallar, B. J. & Lipscomb, J. D. (1996). Dioxygen activation by enzyme containing binuclear non-heme iron clusters. Chem. Rev. 96, 2625-2657.
    • (1996) Chem. Rev. , vol.96 , pp. 2625-2657
    • Wallar, B.J.1    Lipscomb, J.D.2
  • 58
    • 0032023777 scopus 로고    scopus 로고
    • Protein radicals in enzyme catalysis
    • Stubbe, J. & van der Donk, W. A. (1996). Protein radicals in enzyme catalysis. Chem. Rev. 98, 705-762.
    • (1996) Chem. Rev. , vol.98 , pp. 705-762
    • Stubbe, J.1    Van der Donk, W.A.2
  • 59
    • 0031796531 scopus 로고    scopus 로고
    • Harnessing free radicals: Formation and function of the tyrosyl radical in ribonucleotide reductase
    • Stubbe, J. & Riggs-Gelasco, P. (1998). Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase. Trends Biochem. Sci. 23, 438-443.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 438-443
    • Stubbe, J.1    Riggs-Gelasco, P.2
  • 60
    • 0029737878 scopus 로고    scopus 로고
    • 9-stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other di-iron proteins
    • Lindqvist, Y., Huang, W., Schneider, G. & Shanklin, J. (1996). Crystal structure of Δ9-stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other diiron proteins. Eur. Mol. Biol. J. 15, 4081-4092.
    • (1996) Eur. Mol. Biol. J. , vol.15 , pp. 4081-4092
    • Lindqvist, Y.1    Huang, W.2    Schneider, G.3    Shanklin, J.4
  • 61
    • 0035877632 scopus 로고    scopus 로고
    • Engineering Δ-9-16:0-acyl carrier protein (ACP) desaturase specificity based on combinatorial saturation mutagenesis and logical redesign of the castor Δ-9-18:0 - ACP desaturase
    • Whittle, E. & Shanklin, J. (2001). Engineering Δ-9-16:0-acyl carrier protein (ACP) desaturase specificity based on combinatorial saturation mutagenesis and logical redesign of the castor Δ-9-18:0 - ACP desaturase. J. Biol. Chem. 276, 21500-21505.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21500-21505
    • Whittle, E.1    Shanklin, J.2
  • 62
    • 0033568346 scopus 로고    scopus 로고
    • Reversible dioxygen binding to hemerythrin. 1. Electronic structures of deoxy- and oxyhemerythrin
    • Brunold, T. C. & Solomon, E. I. (1999). Reversible dioxygen binding to hemerythrin. 1. Electronic structures of deoxy- and oxyhemerythrin. J. Am. Chem. Soc. 121, 8277-8287.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8277-8287
    • Brunold, T.C.1    Solomon, E.I.2
  • 64
    • 0000043761 scopus 로고
    • Dioxygen and hemerythrin
    • Stenkamp, R. E. (1994). Dioxygen and hemerythrin. Chem. Rev. 94, 715-726.
    • (1994) Chem. Rev. , vol.94 , pp. 715-726
    • Stenkamp, R.E.1
  • 65
    • 0029949340 scopus 로고    scopus 로고
    • The structure of desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains
    • DeMare, F., Kurtz, D. M., Jr & Nordlund, P. (1996). The structure of desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains. Nature Struct. Biol. 3, 539-546.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 539-546
    • DeMare, F.1    Kurtz D.M., Jr.2    Nordlund, P.3
  • 66
    • 0002840502 scopus 로고
    • Ferritin and iron biomineralization
    • Suslick, K. S., ed., Elsevier Science, New York
    • Theil, E. C. (1995). Ferritin and iron biomineralization. In Comprehensive Supramolecular Chemisty (Suslick, K. S., ed.), pp. 65-89, Elsevier Science, New York.
    • (1995) Comprehensive Supramolecular Chemisty , pp. 65-89
    • Theil, E.C.1
  • 67
    • 0019316535 scopus 로고
    • Structural and functional diversity in 4-α-helical proteins
    • Weber, P. C. & Salemme, F. R. (1980). Structural and functional diversity in 4-α-helical proteins. Nature, 287, 82-84.
    • (1980) Nature , vol.287 , pp. 82-84
    • Weber, P.C.1    Salemme, F.R.2
  • 69
    • 0034741608 scopus 로고    scopus 로고
    • Rational reprogramming of the R2 subunit of Escherichia coli ribonucleotide reductase into a selfhydroxylating monooxygenase
    • Baldwin, J., Voegtli, W. C., Khidekel, N., Moenne-Loccoz, P., Krebs, C., Pereira, A. S. et al. (2001). Rational reprogramming of the R2 subunit of Escherichia coli ribonucleotide reductase into a selfhydroxylating monooxygenase. J. Am. Chem. Soc. 123, 7017-7030.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7017-7030
    • Baldwin, J.1    Voegtli, W.C.2    Khidekel, N.3    Moenne-Loccoz, P.4    Krebs, C.5    Pereira, A.S.6
  • 70
    • 0034639904 scopus 로고    scopus 로고
    • Crystal structure of the ribonucleotide reductase R2 mutant that accumulates a μ-1,2-peroxodiiron(III) intermediate during oxygen activation
    • Voegtli, W. C., Khidekel, N., Baldwin, J., Ley, B. A., Bollinger, J. M. & Rosenzweig, A. C. (2000). Crystal structure of the ribonucleotide reductase R2 mutant that accumulates a μ-1,2-peroxodiiron(III) intermediate during oxygen activation. J. Am. Chem. Soc. 122, 3255-3261.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3255-3261
    • Voegtli, W.C.1    Khidekel, N.2    Baldwin, J.3    Ley, B.A.4    Bollinger, J.M.5    Rosenzweig, A.C.6
  • 71
    • 0032552729 scopus 로고    scopus 로고
    • Oxygen activation by non-heme diiron proteins: Identification of a symmetric μ-1,2 peroxide in a mutant of ribonucleotide reductase
    • Moeenne-Loccoz, P., Baldwin, J., Ley, B., Loehr, T. M. & Bollinger, J. M. (1998). Oxygen activation by non-heme diiron proteins: identification of a symmetric μ-1,2 peroxide in a mutant of ribonucleotide reductase. Biochemistry, 37, 14659-14663.
    • (1998) Biochemistry , vol.37 , pp. 14659-14663
    • Moeenne-Loccoz, P.1    Baldwin, J.2    Ley, B.3    Loehr, T.M.4    Bollinger, J.M.5
  • 72
    • 0034612192 scopus 로고    scopus 로고
    • Retrostructural analysis of metalloproteins: Application to the design of a minimal model for diiron proteins
    • Lombardi, A., Summa, C. M., Geremia, S., Randaccio, L., Pavone, V. & DeGrado, W. F. (2000). Retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins. Proc. Natl Acad. Sci. USA, 97, 6298-6305.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6298-6305
    • Lombardi, A.1    Summa, C.M.2    Geremia, S.3    Randaccio, L.4    Pavone, V.5    DeGrado, W.F.6
  • 73
    • 0029144593 scopus 로고
    • Characterization of a new four-chain coiled-coil: Influence of chain length on stability
    • Fairman, R., Ghao, H. G., Mueller, L., Lavoie, T. B., Shen, L., Novotny, L. & Matsueda, G. R. (1995). Characterization of a new four-chain coiled-coil: Influence of chain length on stability. Protein Sci. 4, 1457-1469.
    • (1995) Protein Sci. , vol.4 , pp. 1457-1469
    • Fairman, R.1    Ghao, H.G.2    Mueller, L.3    Lavoie, T.B.4    Shen, L.5    Novotny, L.6    Matsueda, G.R.7
  • 76
    • 0028237287 scopus 로고
    • Optimal sequence selection in proteins of known structure by simulated evolution
    • Hellinga, H. W. & Richards, F. M. (1994). Optimal sequence selection in proteins of known structure by simulated evolution. Proc. Natl Acad. Sci. USA, 91, 5803-5807.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5803-5807
    • Hellinga, H.W.1    Richards, F.M.2
  • 77
    • 0029899119 scopus 로고    scopus 로고
    • Controlling topology and native-like behavior of de novo-designed peptides: Design and characterization of antiparallel four-stranded coiled coils
    • Betz, S. F. & DeGrado, W. F. (1996). Controlling topology and native-like behavior of de novo-designed peptides: design and characterization of antiparallel four-stranded coiled coils. Biochemistry, 35, 6955-6962.
    • (1996) Biochemistry , vol.35 , pp. 6955-6962
    • Betz, S.F.1    DeGrado, W.F.2
  • 78
    • 0033694923 scopus 로고    scopus 로고
    • De novo design of helical bundles as models for understanding protein folding and function
    • Hill, R. B., Raleigh, D. P., Lombardi, A. & DeGrado, W. F. (2000). De novo design of helical bundles as models for understanding protein folding and function. Accts Chem. Res. 33, 745-754.
    • (2000) Accts Chem. Res. , vol.33 , pp. 745-754
    • Hill, R.B.1    Raleigh, D.P.2    Lombardi, A.3    DeGrado, W.F.4
  • 79
    • 0002543810 scopus 로고    scopus 로고
    • Design and NMR analyses of compact, independently folded BBA motifs
    • Struthers, M., Ottesen, J. J. & Imperiali, B. (1998). Design and NMR analyses of compact, independently folded BBA motifs. Fold. Des. 3, 95-103.
    • (1998) Fold. Des. , vol.3 , pp. 95-103
    • Struthers, M.1    Ottesen, J.J.2    Imperiali, B.3
  • 80
    • 0024515763 scopus 로고
    • Protein design, a minimalist approach
    • DeGrado, W. F., Wasserman, Z. R. & Lear, J. D. (1989). Protein design, a minimalist approach. Science, 243, 622-628.
    • (1989) Science , vol.243 , pp. 622-628
    • DeGrado, W.F.1    Wasserman, Z.R.2    Lear, J.D.3
  • 82
    • 0030885887 scopus 로고    scopus 로고
    • Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): Implications for substrate gating and component interactions
    • Rosenzweig, A. C., Brandstetter, H., Whittington, D. A., Nordlund, P., Lippard, S. J. & Frederick, C. A. (1997). Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions. Proteins: Struct. Funct. Genet., 29, 141-152.
    • (1997) Proteins: Struct. Funct. Genet. , vol.29 , pp. 141-152
    • Rosenzweig, A.C.1    Brandstetter, H.2    Whittington, D.A.3    Nordlund, P.4    Lippard, S.J.5    Frederick, C.A.6
  • 83
    • 0000726701 scopus 로고    scopus 로고
    • Carbonic anhydrase: Evolution of a zinc binding site by nature and by design
    • Christianson, D. W. & Fierke, C. A. (1996). Carbonic anhydrase: evolution of a zinc binding site by nature and by design. Accts Chem. Res. 29, 331-339.
    • (1996) Accts Chem. Res. , vol.29 , pp. 331-339
    • Christianson, D.W.1    Fierke, C.A.2
  • 84
    • 0343580454 scopus 로고    scopus 로고
    • Perturbation to the active site of phosphotriesterase
    • Kuo, J. M., Chae, M. Y. & Raushel, F. M. (1997). Perturbation to the active site of phosphotriesterase. Biochemistry, 36, 1982-1988.
    • (1997) Biochemistry , vol.36 , pp. 1982-1988
    • Kuo, J.M.1    Chae, M.Y.2    Raushel, F.M.3
  • 85
    • 0033200372 scopus 로고    scopus 로고
    • Secondary ligands enhance affinity at a designed metal-binding site
    • Marino, S. F. & Regan, L. (1999). Secondary ligands enhance affinity at a designed metal-binding site. Chem. Biol. 6, 649-655.
    • (1999) Chem. Biol. , vol.6 , pp. 649-655
    • Marino, S.F.1    Regan, L.2
  • 86
    • 0027231963 scopus 로고
    • The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme
    • Goodin, D. B. & McRee, D. E. (1993). The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme. Biochemistry, 32, 3313-3324.
    • (1993) Biochemistry , vol.32 , pp. 3313-3324
    • Goodin, D.B.1    McRee, D.E.2
  • 87
    • 0032573845 scopus 로고    scopus 로고
    • Simple proposal that can explain the inactivity of metal-substituted superoxide dismutases
    • Vance, C. K. & Miller, A. F. (1998). Simple proposal that can explain the inactivity of metal-substituted superoxide dismutases. J. Am. Chem. Soc. 120, 461-467.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 461-467
    • Vance, C.K.1    Miller, A.F.2
  • 88
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil, K. T. & DeGrado, W. F. (1990). A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science, 250, 646-651.
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 89
    • 85031435170 scopus 로고
    • Structure of the ColE1 rop protein at 1.7 Å resolution
    • Banner, D. W., Kokkinidis, M. & Tsernoglau, D. (1987). Structure of the ColE1 rop protein at 1.7 Å resolution. J. Mol. Biol. 201, 601-619.
    • (1987) J. Mol. Biol. , vol.201 , pp. 601-619
    • Banner, D.W.1    Kokkinidis, M.2    Tsernoglau, D.3
  • 90
    • 0028303384 scopus 로고
    • A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions
    • Krylov, D., Mikhailenko, I. & Vinson, C. (1994). A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions. EMBO J. 13, 2849-2861.
    • (1994) EMBO J. , vol.13 , pp. 2849-2861
    • Krylov, D.1    Mikhailenko, I.2    Vinson, C.3
  • 91
    • 0030844740 scopus 로고    scopus 로고
    • A designed buried salt bridge in a heterodimeric coiled coil
    • Schneider, J. P., Lear, J. D. & DeGrado, W. F. (1997). A designed buried salt bridge in a heterodimeric coiled coil. J. Am. Chem. Soc. 119, 5742-5743.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 5742-5743
    • Schneider, J.P.1    Lear, J.D.2    DeGrado, W.F.3
  • 92
    • 0032497322 scopus 로고    scopus 로고
    • A buried polar interaction can direct the relative orientation of helices in a coiled coil
    • Oakley, M. G. & Kim, P. S. (1998). A buried polar interaction can direct the relative orientation of helices in a coiled coil. Biochemistry, 37, 12603-12610.
    • (1998) Biochemistry , vol.37 , pp. 12603-12610
    • Oakley, M.G.1    Kim, P.S.2
  • 93
    • 0000388506 scopus 로고
    • The formation of a helical complex between polyisnosinic acid polycytidylic acid
    • Davies, D. R. & Rich, A. (1958). The formation of a helical complex between polyisnosinic acid polycytidylic acid. J. Am. Chem. Soc. USA, 80, 1003-1004.
    • (1958) J. Am. Chem. Soc. USA , vol.80 , pp. 1003-1004
    • Davies, D.R.1    Rich, A.2
  • 95
    • 7744244599 scopus 로고    scopus 로고
    • Recent advances in zinc enzymology
    • Lipscomb, W. N. & Strater, N. (1996). Recent advances in zinc enzymology. Chem. Rev. 96, 2375-2433.
    • (1996) Chem. Rev. , vol.96 , pp. 2375-2433
    • Lipscomb, W.N.1    Strater, N.2
  • 97
    • 84978150742 scopus 로고    scopus 로고
    • Analysis and design of 3-stranded coiled coils and 3-helix bundles
    • Schneider, J. P., Lombardi, A. & DeGrado, W. F. (1998). Analysis and design of 3-stranded coiled coils and 3-helix bundles. Fold. Des. 3, R29-R40.
    • (1998) Fold. Des. , vol.3
    • Schneider, J.P.1    Lombardi, A.2    DeGrado, W.F.3
  • 98
    • 0021667647 scopus 로고
    • High spin cobalt(II) as a probe for the investigation of metalloproteins
    • Bertini, I. & Luchinat, C. (1984). High spin cobalt(II) as a probe for the investigation of metalloproteins. Advan. Inorg. Biochem. 6, 71-111.
    • (1984) Advan. Inorg. Biochem. , vol.6 , pp. 71-111
    • Bertini, I.1    Luchinat, C.2
  • 100
    • 0028467772 scopus 로고
    • Structure of a unique twofold symmetric haem-binding site
    • Frolow, F., Kalb, A. J. & Yariv, J. (1994). Structure of a unique twofold symmetric haem-binding site. Nature Struct. Biol. 1, 453-460.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 453-460
    • Frolow, F.1    Kalb, A.J.2    Yariv, J.3
  • 101
    • 0035916893 scopus 로고    scopus 로고
    • Hydrogen peroxide formation during iron deposition in horse spleen ferritin using oxygen as an oxidant
    • Lindsay, S., Brosnahan, D. & Watt, G. D. (2001). Hydrogen peroxide formation during iron deposition in horse spleen ferritin using oxygen as an oxidant. Biochemistry, 40, 3340-3347.
    • (2001) Biochemistry , vol.40 , pp. 3340-3347
    • Lindsay, S.1    Brosnahan, D.2    Watt, G.D.3
  • 102
    • 0032516447 scopus 로고    scopus 로고
    • Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization
    • Peceira, A. S., Small, W., Krebs, C., Tavares, P., Edmondson, D. E., Theil, E. C. & Huynh, B. H. (1998). Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization. Biochemistry, 37, 9871-9876.
    • (1998) Biochemistry , vol.37 , pp. 9871-9876
    • Peceira, A.S.1    Small, W.2    Krebs, C.3    Tavares, P.4    Edmondson, D.E.5    Theil, E.C.6    Huynh, B.H.7
  • 103
    • 0031029483 scopus 로고    scopus 로고
    • Dinuclear center of ferritin: Studies of iron binding and oxidation show differences in the two iron sites
    • Treffry, A., Zhao, Z., Quail, M. A., Guest, J. R. & Harrison, P. M. (1997). Dinuclear center of ferritin: studies of iron binding and oxidation show differences in the two iron sites. Biochemistry, 36, 432-441.
    • (1997) Biochemistry , vol.36 , pp. 432-441
    • Treffry, A.1    Zhao, Z.2    Quail, M.A.3    Guest, J.R.4    Harrison, P.M.5
  • 104
    • 0032493313 scopus 로고    scopus 로고
    • Reaction paths of iron oxidation and hydrolysis in horse spleen and recombinant human ferritins
    • Yang, X., Chen-Barrett, Y., Arosio, P. & Chasteen, N. D. (1998). Reaction paths of iron oxidation and hydrolysis in horse spleen and recombinant human ferritins. Biochemistry, 37, 9743-9750.
    • (1998) Biochemistry , vol.37 , pp. 9743-9750
    • Yang, X.1    Chen-Barrett, Y.2    Arosio, P.3    Chasteen, N.D.4
  • 105
    • 0026062115 scopus 로고
    • Models of the reduced forms of polyiron-oxo proteins: An asymmetric, triply carboxylate bridged diiron(II) complex and its reaction with dioxygen
    • Tolman, W. B., Liu, S., Bentsen, J. G. & Lippard, S. J. (1991). Models of the reduced forms of polyiron-oxo proteins: an asymmetric, triply carboxylate bridged diiron(II) complex and its reaction with dioxygen. J. Am. Chem. Soc. 113, 152-164.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 152-164
    • Tolman, W.B.1    Liu, S.2    Bentsen, J.G.3    Lippard, S.J.4
  • 106
    • 0034712683 scopus 로고    scopus 로고
    • The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin
    • Yang, X., Le Brun, N. E., Thomson, A. J., Moore, G. R. & Chasteen, N. D. (2000). The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin. Biochemistry, 39, 4915-4923.
    • (2000) Biochemistry , vol.39 , pp. 4915-4923
    • Yang, X.1    Le Brun, N.E.2    Thomson, A.J.3    Moore, G.R.4    Chasteen, N.D.5
  • 107
    • 0026347398 scopus 로고
    • Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor or ribonucleotide reductase
    • Bollinger, M. J., Edmondson, D. E., Huynh, B. H., Filley, H., Norton, J. R. & Stubbe, J. (1991). Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor or ribonucleotide reductase. Science, 253, 292-298.
    • (1991) Science , vol.253 , pp. 292-298
    • Bollinger, M.J.1    Edmondson, D.E.2    Huynh, B.H.3    Filley, H.4    Norton, J.R.5    Stubbe, J.6
  • 108
    • 0028170957 scopus 로고
    • Resonance Raman evidence for an Fe-O-Fe center in the stearoyl-ACP desaturase. Primary sequence identity with other diiron-oxo proteins
    • Fox, B. G., Shanklin, J., Ai, J., Loehr, T. M. & Sanders-Loehr, J. (1994). Resonance Raman evidence for an Fe-O-Fe center in the stearoyl-ACP desaturase. Primary sequence identity with other diiron-oxo proteins. Biochemistry, 33, 12776-12786.
    • (1994) Biochemistry , vol.33 , pp. 12776-12786
    • Fox, B.G.1    Shanklin, J.2    Ai, J.3    Loehr, T.M.4    Sanders-Loehr, J.5
  • 109
    • 0028858499 scopus 로고
    • De novo design of the hydrophobic cores of proteins
    • Desjarlais, J. R. & Handel, T. M. (1995). De novo design of the hydrophobic cores of proteins. Protein Sci. 4, 2006-2018.
    • (1995) Protein Sci. , vol.4 , pp. 2006-2018
    • Desjarlais, J.R.1    Handel, T.M.2
  • 110
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • Dahiyat, B. I. & Mayo, S. L. (1997). De novo protein design: fully automated sequence selection. Science, 278, 82-87.
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 111
    • 36449005847 scopus 로고
    • Ground state of random copolymers and the discrete random energy model
    • Gutin, A. M. & Shakhnovich, E. I. (1993). Ground state of random copolymers and the discrete random energy model. J. Chem. Phys. 98, 8174-8177.
    • (1993) J. Chem. Phys. , vol.98 , pp. 8174-8177
    • Gutin, A.M.1    Shakhnovich, E.I.2
  • 112
    • 0027234766 scopus 로고
    • Engineering of stable and fast-folding sequences of model proteins
    • Shakhnovich, E. & Gutin, A. M. (1993). Engineering of stable and fast-folding sequences of model proteins. Proc. Natl Acad. Sci. USA, 90, 7195-7199.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7195-7199
    • Shakhnovich, E.1    Gutin, A.M.2
  • 113
    • 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. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 114
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merrit, E. A. & Bacon, D. J. (1997). Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.