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Volumn 42, Issue 37, 2003, Pages 10923-10930

Hydrogen exchange in a bacterial cytochrome c: A fingerprint of the cytochrome c fold

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; BACTERIA; CHLORIDE MINERALS; CYTOLOGY; HYDROGEN; PROTEINS;

EID: 0141542754     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0348258     Document Type: Article
Times cited : (10)

References (49)
  • 3
    • 0025903766 scopus 로고
    • Sequence variability in bacterial cytochromes
    • Ambler, R. P. (1991) Sequence variability in bacterial cytochromes, Biochim. Biophys. Acta 1058, 42-47.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 42-47
    • Ambler, R.P.1
  • 4
    • 0033595670 scopus 로고    scopus 로고
    • Cytochrome c-553 from the alkalophilic bacterium Bacillus pasteurii has the primary structure characteristics of a lipoprotein
    • Vanderberghe, I. H., Ciurli, S., Benini, S., and Van Beeumen, J. (1999) Cytochrome c-553 from the alkalophilic bacterium Bacillus pasteurii has the primary structure characteristics of a lipoprotein, Biochem. Biophys. Res. Commun. 264, 380-387.
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 380-387
    • Vanderberghe, I.H.1    Ciurli, S.2    Benini, S.3    Van Beeumen, J.4
  • 5
    • 0033573140 scopus 로고    scopus 로고
    • Still a puzzle: Why is haem covalently attached in c-type cytochromes?
    • Barker, P. D., and Ferguson, S. J. (1999) Still a puzzle: why is haem covalently attached in c-type cytochromes?, Struct. Folding Des. 7, R281-R290.
    • (1999) Struct. Folding Des. , vol.7
    • Barker, P.D.1    Ferguson, S.J.2
  • 6
    • 0022399830 scopus 로고
    • Helix movements and the reconstruction of the haem pocket during the evolution of the cytochrome c family
    • Chothia, C., and Lesk, A. M. (1985) Helix movements and the reconstruction of the haem pocket during the evolution of the cytochrome c family, J. Mol. Biol. 182, 151-158.
    • (1985) J. Mol. Biol. , vol.182 , pp. 151-158
    • Chothia, C.1    Lesk, A.M.2
  • 7
    • 0024289198 scopus 로고
    • Spectroscopic characterization of a high-potential monohaem cytochrome from Wolinella succinogenes, a nitrate-respiring organism. Redox and spin equilibria studies
    • Moura, I., Liu, M. Y., Costa, C., Liu, M. C., Pai, G., Xavier, A. V., LeGall, J., Payne, W. J., and Moura, J. J. (1988) Spectroscopic characterization of a high-potential monohaem cytochrome from Wolinella succinogenes, a nitrate-respiring organism. Redox and spin equilibria studies, Eur. J. Biochem. 177, 673-682.
    • (1988) Eur. J. Biochem. , vol.177 , pp. 673-682
    • Moura, I.1    Liu, M.Y.2    Costa, C.3    Liu, M.C.4    Pai, G.5    Xavier, A.V.6    LeGall, J.7    Payne, W.J.8    Moura, J.J.9
  • 8
    • 0037161297 scopus 로고    scopus 로고
    • Solution structure of a mono-heme ferrocytochrome c from Shewanella putrefaciens and structural analysis of sequence-similar proteins: Functional implications
    • Bartalesi, I., Bertini, I., Hajieva, P., Rosato, A., and Vasos, P. (2002) Solution structure of a mono-heme ferrocytochrome c from Shewanella putrefaciens and structural analysis of sequence-similar proteins: functional implications, Biochemistry 41, 5112-5119.
    • (2002) Biochemistry , vol.41 , pp. 5112-5119
    • Bartalesi, I.1    Bertini, I.2    Hajieva, P.3    Rosato, A.4    Vasos, P.5
  • 9
    • 0024596945 scopus 로고
    • NMR study of the alkaline isomerization of ferricytochrome c
    • Hong, X., and Dixon, D. W. (1989) NMR study of the alkaline isomerization of ferricytochrome c, FEBS Lett. 246, 105-108.
    • (1989) FEBS Lett. , vol.246 , pp. 105-108
    • Hong, X.1    Dixon, D.W.2
  • 10
    • 0024603937 scopus 로고
    • Mutation induced perturbation of the cytochrome c alkaline transition
    • Pearce, L. L., Gärtner, A. L., Smith, M., and Mauk, A. G. (1989) Mutation induced perturbation of the cytochrome c alkaline transition, Biochemistry 28, 3152-3156.
    • (1989) Biochemistry , vol.28 , pp. 3152-3156
    • Pearce, L.L.1    Gärtner, A.L.2    Smith, M.3    Mauk, A.G.4
  • 11
    • 0025832142 scopus 로고
    • Effective concentrations of amino acid side chains in an unfolded protein
    • Muthukrishnan, K., and Nall, B. T. (1991) Effective concentrations of amino acid side chains in an unfolded protein, Biochemistry 30, 4706-4710.
    • (1991) Biochemistry , vol.30 , pp. 4706-4710
    • Muthukrishnan, K.1    Nall, B.T.2
  • 12
    • 0034682478 scopus 로고    scopus 로고
    • NMR investigation of ferricytochrome c unfolding: Detection of an equilibrium unfolding intermediate and residual structure in the denatured state
    • Russell, B. S., Melenkivitz, R., and Bren, K. L. (2000) NMR investigation of ferricytochrome c unfolding: detection of an equilibrium unfolding intermediate and residual structure in the denatured state, Proc. Natl. Acad. Sci. U.S.A. 97, 8312-8317.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8312-8317
    • Russell, B.S.1    Melenkivitz, R.2    Bren, K.L.3
  • 13
    • 0036968299 scopus 로고    scopus 로고
    • The unfolding of oxidized c-type cytochromes: The instructive case of B. pasteurii
    • Bartalesi, I., Bertini, I., Ghosh, K., Rosato, A., and Turano, P. (2002) The unfolding of oxidized c-type cytochromes: the instructive case of B. pasteurii, J. Mol. Biol. 321, 693-701.
    • (2002) J. Mol. Biol. , vol.321 , pp. 693-701
    • Bartalesi, I.1    Bertini, I.2    Ghosh, K.3    Rosato, A.4    Turano, P.5
  • 15
    • 0037007168 scopus 로고    scopus 로고
    • NMR solution structure, backbone mobility and homology modeling of c-type cytochromes from gram-positive bacteria
    • Banci, L., Bertini, I., Ciurli, S., Dikiy, A., Dittmer, J., Rosato, A., Sciara, G., and Thompsett, A. (2002) NMR solution structure, backbone mobility and homology modeling of c-type cytochromes from gram-positive bacteria, Chem. Biol. Chem. 3, 299-310.
    • (2002) Chem. Biol. Chem. , vol.3 , pp. 299-310
    • Banci, L.1    Bertini, I.2    Ciurli, S.3    Dikiy, A.4    Dittmer, J.5    Rosato, A.6    Sciara, G.7    Thompsett, A.8
  • 16
    • 6444222991 scopus 로고
    • Use of glass electrodes to measure acidities in deuterium oxide
    • Glasoe, P. K., and Long, F. A. (1960) Use of glass electrodes to measure acidities in deuterium oxide, J. Phys. Chem. 64, 188-190.
    • (1960) J. Phys. Chem. , vol.64 , pp. 188-190
    • Glasoe, P.K.1    Long, F.A.2
  • 17
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen, G., and Ruben, D. J. (1980) Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy, Chem. Phys. Lett. 69, 185-188.
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-188
    • Bodenhausen, G.1    Ruben, D.J.2
  • 18
    • 0001121381 scopus 로고
    • Deuterium exchange of poly-D,L-alanine in aqueous solution
    • Berger, A., and Linderstrøm-Lang, K. (1957) Deuterium exchange of poly-D,L-alanine in aqueous solution, Arch. Biochem. Biophys. 69, 106-118.
    • (1957) Arch. Biochem. Biophys. , vol.69 , pp. 106-118
    • Berger, A.1    Linderstrøm-Lang, K.2
  • 19
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt, A., and Nielsen, S. O. (1966) Hydrogen exchange in proteins, Adv. Protein Chem. 21, 287-386.
    • (1966) Adv. Protein Chem. , vol.21 , pp. 287-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 20
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander, S. W., and Kallenbach, N. R. (1983) Hydrogen exchange and structural dynamics of proteins and nucleic acids, Q. Rev. Biophys. 16, 521-655.
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 26
    • 0036408312 scopus 로고    scopus 로고
    • Thermodynamic and kinetic exploration of the energy landscape of Borrelia burgdorferi OspA by native-state hydrogen exchange
    • Yan, S., Kennedy, S. D., and Koide, S. (2002) Thermodynamic and Kinetic Exploration of the Energy Landscape of Borrelia burgdorferi OspA by Native-state Hydrogen Exchange, J. Mol. Biol. 323, 363-375.
    • (2002) J. Mol. Biol. , vol.323 , pp. 363-375
    • Yan, S.1    Kennedy, S.D.2    Koide, S.3
  • 27
    • 0000159569 scopus 로고    scopus 로고
    • Protein structure and the energetics of protein stability
    • Robertson, A. D., and Murphy, K. P. (1997) Protein structure and the energetics of protein stability, Chem. Rev. 97, 1251-1267.
    • (1997) Chem. Rev. , vol.97 , pp. 1251-1267
    • Robertson, A.D.1    Murphy, K.P.2
  • 28
    • 0036182617 scopus 로고    scopus 로고
    • A residue-specific view of the association and dissociation pathway in protein-DNA recognition
    • Kalodimos, C. G., Boelens, R., and Kaptein, R. (2002) A residue-specific view of the association and dissociation pathway in protein-DNA recognition, Nat. Struct. Biol. 9, 193-197.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 193-197
    • Kalodimos, C.G.1    Boelens, R.2    Kaptein, R.3
  • 29
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai, Y. W., Sosnick, T. R., Mayne, L., and Englander, S. W. (1995) Protein folding intermediates: native-state hydrogen exchange, Science 269, 192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.W.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 30
    • 0037172787 scopus 로고    scopus 로고
    • Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein
    • Chu, R., Pei, W., Takei, J., and Bai, Y. (2002) Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein, Biochemistry 41, 7998-8003.
    • (2002) Biochemistry , vol.41 , pp. 7998-8003
    • Chu, R.1    Pei, W.2    Takei, J.3    Bai, Y.4
  • 31
    • 0037108164 scopus 로고    scopus 로고
    • Populating partially unfolded forms by hydrogen exchange-directed protein engineering
    • Takei, J., Pei, W., Vu, D., and Bai, Y. (2002) Populating partially unfolded forms by hydrogen exchange-directed protein engineering, Biochemistry 41, 12308-12312.
    • (2002) Biochemistry , vol.41 , pp. 12308-12312
    • Takei, J.1    Pei, W.2    Vu, D.3    Bai, Y.4
  • 32
    • 0030840017 scopus 로고    scopus 로고
    • Microsecond protein folding kinetics from native-state hydrogen exchange
    • Arrington, C. B., and Robertson, A. D. (1997) Microsecond protein folding kinetics from native-state hydrogen exchange, Biochemistry 36, 8686-8691.
    • (1997) Biochemistry , vol.36 , pp. 8686-8691
    • Arrington, C.B.1    Robertson, A.D.2
  • 33
    • 0035075187 scopus 로고    scopus 로고
    • Kinetics of unfolding and folding from amide hydrogen exchange in native ubiquitin
    • Sivaraman, T., Arrington, C. B., and Robertson, A. D. (2001) Kinetics of unfolding and folding from amide hydrogen exchange in native ubiquitin, Nat. Struct. Biol. 8, 331-333.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 331-333
    • Sivaraman, T.1    Arrington, C.B.2    Robertson, A.D.3
  • 34
    • 0033593247 scopus 로고    scopus 로고
    • Defining protein ensembles with native-state NH exchange: Kinetics of interconversion and cooperative units from combined NMR and MS analysis
    • Arrington, C. B., Teesch, L. M., and Robertson, A. D. (1999) Defining protein ensembles with native-state NH exchange: kinetics of interconversion and cooperative units from combined NMR and MS analysis, J. Mol. Biol. 285, 1265-1275.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1265-1275
    • Arrington, C.B.1    Teesch, L.M.2    Robertson, A.D.3
  • 35
    • 0034733386 scopus 로고    scopus 로고
    • Correlated motions in native proteins from MS analysis of NH exchange: Evidence for a manifold of unfolding reactions in ovomucoid third domain
    • Arrington, C. B., and Robertson, A. D. (2000) Correlated motions in native proteins from MS analysis of NH exchange: evidence for a manifold of unfolding reactions in ovomucoid third domain, J. Mol. Biol. 300, 221-232.
    • (2000) J. Mol. Biol. , vol.300 , pp. 221-232
    • Arrington, C.B.1    Robertson, A.D.2
  • 36
    • 0031866483 scopus 로고    scopus 로고
    • Amide protection in an early folding intermediate of cytochrome c
    • Sauder, J. M., and Roder, H. (1998) Amide protection in an early folding intermediate of cytochrome c, Folding Des. 3, 293-301.
    • (1998) Folding Des. , vol.3 , pp. 293-301
    • Sauder, J.M.1    Roder, H.2
  • 38
    • 0037214137 scopus 로고    scopus 로고
    • Protein hydrogen exchange mechanism: Local fluctuations
    • Maity, H., Lim, W. K., Rumbley, J. N., and Englander, S. W. (2003) Protein hydrogen exchange mechanism: Local fluctuations, Protein Sci. 12, 153-160.
    • (2003) Protein Sci. , vol.12 , pp. 153-160
    • Maity, H.1    Lim, W.K.2    Rumbley, J.N.3    Englander, S.W.4
  • 40
    • 0037469128 scopus 로고    scopus 로고
    • Structure and dynamics of reduced Bacillus pasteurii cytochrome c: Oxidation state dependent properties and implications for electron-transfer processes
    • Bartalesi, I., Bertini, I., and Rosato, A. (2003) Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron-transfer processes, Biochemistry 42, 739-745.
    • (2003) Biochemistry , vol.42 , pp. 739-745
    • Bartalesi, I.1    Bertini, I.2    Rosato, A.3
  • 42
    • 36849127400 scopus 로고
    • Nuclear magnetic resonance study of the protolysis of trimethylamminium ion in aqueous solution-order of the reaction with respect to solvent
    • Luz, Z., and Meiboom, S. (1963) Nuclear magnetic resonance study of the protolysis of trimethylamminium ion in aqueous solution-order of the reaction with respect to solvent., J. Chem. Phys. 39, 370.
    • (1963) J. Chem. Phys. , vol.39 , pp. 370
    • Luz, Z.1    Meiboom, S.2
  • 43
    • 0031912073 scopus 로고    scopus 로고
    • Determinants of protein hydrogen exchange studied in equine cytochrome c
    • Milne, J. S., Mayne, L., Roder, H., Wand, A. J., and Englander, S. W. (1998) Determinants of protein hydrogen exchange studied in equine cytochrome c, Protein Sci. 7, 739-745.
    • (1998) Protein Sci. , vol.7 , pp. 739-745
    • Milne, J.S.1    Mayne, L.2    Roder, H.3    Wand, A.J.4    Englander, S.W.5
  • 45
    • 0035933343 scopus 로고    scopus 로고
    • Snapshots of protein folding. A study on the multiple transition state pathway of cytochrome c(551) from Pseudomonas aeruginosa
    • Gianni, S., Travaglini-Allocatelli, C., Cutruzzolà, F., Bigotti, M. G., and Brunori, M. (2001) Snapshots of protein folding. A study on the multiple transition state pathway of cytochrome c(551) from Pseudomonas aeruginosa, J. Mol. Biol. 309, 1177-1187.
    • (2001) J. Mol. Biol. , vol.309 , pp. 1177-1187
    • Gianni, S.1    Travaglini-Allocatelli, C.2    Cutruzzolà, F.3    Bigotti, M.G.4    Brunori, M.5
  • 47
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structure
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structure, J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 49
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov, I. N., and Bourne, P. E. (1998) Protein structure alignment by incremental combinatorial extension (CE) of the optimal path, Protein Eng. 11, 739-747.
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2


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