메뉴 건너뛰기




Volumn 6, Issue 11, 2011, Pages

Conformational toggling of yeast iso-1-cytochrome c in the oxidized and reduced states

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CYTOCHROME C; CYTOCHROME C PEROXIDASE; HEME; HISTIDINE; ISOCYTOCHROME C1; MUTANT PROTEIN; UNCLASSIFIED DRUG; CYTOCHROME C1; FUNGAL PROTEIN; IRON;

EID: 80555139961     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0027219     Document Type: Article
Times cited : (9)

References (61)
  • 1
    • 0027295787 scopus 로고
    • Protein engineering as a tool for understanding electron transfer
    • Wuttke DS, Gray HB, (1993) Protein engineering as a tool for understanding electron transfer. Cur Opin Struct Biol 3: 555-563.
    • (1993) Cur Opin Struct Biol , vol.3 , pp. 555-563
    • Wuttke, D.S.1    Gray, H.B.2
  • 3
    • 0026674590 scopus 로고
    • Functional role of heme ligation in cytochrome c. Effects of replacement of methionine 80 with natural and non-natural residues by semisynthesis
    • Wallace CJ, Clark-Lewis I, (1992) Functional role of heme ligation in cytochrome c. Effects of replacement of methionine 80 with natural and non-natural residues by semisynthesis. J Biol Chem 267: 3852-3861.
    • (1992) J Biol Chem , vol.267 , pp. 3852-3861
    • Wallace, C.J.1    Clark-Lewis, I.2
  • 4
    • 0024814209 scopus 로고
    • Axial ligand replacement in horse heart cytochrome c by semisynthesis
    • Raphael AL, Gray HB, (1989) Axial ligand replacement in horse heart cytochrome c by semisynthesis. Proteins 6: 338-40.
    • (1989) Proteins , vol.6 , pp. 338-340
    • Raphael, A.L.1    Gray, H.B.2
  • 5
    • 0000116722 scopus 로고
    • pH-Linked conformational regulation of a metalloprotein oxidation-reduction equilibrium: electrochemical analysis of the alkaline form of cytochrome c
    • Barker PD, Mauk G, (1992) pH-Linked conformational regulation of a metalloprotein oxidation-reduction equilibrium: electrochemical analysis of the alkaline form of cytochrome c. J Am Chem Soc 114: 3619-3624.
    • (1992) J Am Chem Soc , vol.114 , pp. 3619-3624
    • Barker, P.D.1    Mauk, G.2
  • 6
    • 0001541295 scopus 로고
    • Hydrodesulfurization model systems homogeneous and heterogeneous (Solid-Gas) hydrogenation of benzothiophene at Iridium
    • Ferrer JC, Guillemette JG, Bogumil R, Inglis SC, Smith M, et al. (1993) Hydrodesulfurization model systems homogeneous and heterogeneous (Solid-Gas) hydrogenation of benzothiophene at Iridium. J Am Chem Soc 115: 7505-7506.
    • (1993) J Am Chem Soc , vol.115 , pp. 7505-7506
    • Ferrer, J.C.1    Guillemette, J.G.2    Bogumil, R.3    Inglis, S.C.4    Smith, M.5
  • 7
    • 0037433505 scopus 로고    scopus 로고
    • Structural model for an alkaline form of ferricytochrome c
    • Assfalg M, Bertini I, Dolfi A, Turano P, Mauk G, et al. (2003) Structural model for an alkaline form of ferricytochrome c. J Am Chem Soc 125 (10): 2913-2922.
    • (2003) J Am Chem Soc , vol.125 , Issue.10 , pp. 2913-2922
    • Assfalg, M.1    Bertini, I.2    Dolfi, A.3    Turano, P.4    Mauk, G.5
  • 9
  • 10
    • 0032558458 scopus 로고    scopus 로고
    • Direct Voltammetric Observation of Redox Driven Changes in axial coordination and intramolecular rearrangement of the phenylalanine-82 histidine variant of yeast Iso-1-cytochrome c
    • Feinberg BA, Liu X, Ryan MD, Schejter A, Zhang C, et al. (1998) Direct Voltammetric Observation of Redox Driven Changes in axial coordination and intramolecular rearrangement of the phenylalanine-82 histidine variant of yeast Iso-1-cytochrome c. Biochemistry 37: 13091-13101.
    • (1998) Biochemistry , vol.37 , pp. 13091-13101
    • Feinberg, B.A.1    Liu, X.2    Ryan, M.D.3    Schejter, A.4    Zhang, C.5
  • 11
    • 33748271734 scopus 로고    scopus 로고
    • Tuning the rate and pH accessibility of a conformational electron transfer gate
    • Baddam S, Bowler BE, (2006) Tuning the rate and pH accessibility of a conformational electron transfer gate. Inorg Chem 45: 6338-6346.
    • (2006) Inorg Chem , vol.45 , pp. 6338-6346
    • Baddam, S.1    Bowler, B.E.2
  • 12
    • 34548696835 scopus 로고    scopus 로고
    • Alkaline Conformational Transition and Gated Electron Transfer with a Lys79->His Variant of Iso-1-cytochrome c
    • Bandi S, Baddam S, Bowler BE, (2007) Alkaline Conformational Transition and Gated Electron Transfer with a Lys79->His Variant of Iso-1-cytochrome c, Biochemistry 46: 10643-10645.
    • (2007) Biochemistry , vol.46 , pp. 10643-10645
    • Bandi, S.1    Baddam, S.2    Bowler, B.E.3
  • 13
    • 45249112520 scopus 로고    scopus 로고
    • Probing the Bottom of a Folding Funnel Using Conformationally Gated Electron Transfer Reactions
    • Bandi S, Bowler BE, (2008) Probing the Bottom of a Folding Funnel Using Conformationally Gated Electron Transfer Reactions, J Am Chem Soc 130: 7540-7541.
    • (2008) J Am Chem Soc , vol.130 , pp. 7540-7541
    • Bandi, S.1    Bowler, B.E.2
  • 14
    • 1842412487 scopus 로고    scopus 로고
    • Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme
    • Williams PA, Fulop V, Garman EF, Saunders NF, Ferguson SJ, et al. (1997) Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme. Nature 389: 406-412.
    • (1997) Nature , vol.389 , pp. 406-412
    • Williams, P.A.1    Fulop, V.2    Garman, E.F.3    Saunders, N.F.4    Ferguson, S.J.5
  • 15
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands
    • Elove GA, Bhuyan AK, Roder H, (1994) Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands. Biochemistry 33: 6925-6935.
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elove, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 16
    • 0029967474 scopus 로고    scopus 로고
    • Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding
    • Colon W, Elove GA, Wakem LP, Sherman F, Roder H, (1996) Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding. Biochemistry 35: 5538-5549.
    • (1996) Biochemistry , vol.35 , pp. 5538-5549
    • Colon, W.1    Elove, G.A.2    Wakem, L.P.3    Sherman, F.4    Roder, H.5
  • 19
    • 0034013699 scopus 로고    scopus 로고
    • Circular dichroism and resonance raman comparative studies of wild type cytochrome c and F82H mutant
    • Zheng J, Ye S, Lu T, Cotton TM, Chumanov G, (2000) Circular dichroism and resonance raman comparative studies of wild type cytochrome c and F82H mutant. Biopolymers 57 (2): 77-84.
    • (2000) Biopolymers , vol.57 , Issue.2 , pp. 77-84
    • Zheng, J.1    Ye, S.2    Lu, T.3    Cotton, T.M.4    Chumanov, G.5
  • 20
    • 0019888623 scopus 로고
    • Conformation change of cytochrome c: I. Ferrocytochrome c structure refined at 1·5 Å resolution
    • Takano T, Dickerson RE, (1981) Conformation change of cytochrome c: I. Ferrocytochrome c structure refined at 1·5 Å resolution. J Mol Biol 153: 79-94.
    • (1981) J Mol Biol , vol.153 , pp. 79-94
    • Takano, T.1    Dickerson, R.E.2
  • 21
    • 0024292135 scopus 로고
    • Yeast iso-1-cytochrome c: A 2.8 Å resolution three-dimensional structure determination
    • Louie GV, Hutcheon WL, Brayer GD, (1988) Yeast iso-1-cytochrome c: A 2.8 Å resolution three-dimensional structure determination. J Mol Biol 199: 295-314.
    • (1988) J Mol Biol , vol.199 , pp. 295-314
    • Louie, G.V.1    Hutcheon, W.L.2    Brayer, G.D.3
  • 22
    • 0026608669 scopus 로고
    • Oxidation state-dependent conformational changes in cytochrome c
    • Berghuis AM, Brayer GD, (1992) Oxidation state-dependent conformational changes in cytochrome c. J Mol Biol 223: 959-976.
    • (1992) J Mol Biol , vol.223 , pp. 959-976
    • Berghuis, A.M.1    Brayer, G.D.2
  • 23
    • 0023290578 scopus 로고
    • Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein
    • Cutler RL, Pielak GJ, Mauk AG, Smith M, (1987) Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein. Protein Engin 1: 95-99.
    • (1987) Protein Engin , vol.1 , pp. 95-99
    • Cutler, R.L.1    Pielak, G.J.2    Mauk, A.G.3    Smith, M.4
  • 24
    • 0025370793 scopus 로고
    • Assignment of proton resonances, identification of secondary structural elements, and analysis of backbone chemical shifts for the C102T variant of yeast iso-1-cytochrome c and horse cytochrome c
    • Gao Y, Boyd J, Williams RJ, Pielak GJ, (1990) Assignment of proton resonances, identification of secondary structural elements, and analysis of backbone chemical shifts for the C102T variant of yeast iso-1-cytochrome c and horse cytochrome c. Biochemistry 29: 6994-7003.
    • (1990) Biochemistry , vol.29 , pp. 6994-7003
    • Gao, Y.1    Boyd, J.2    Williams, R.J.3    Pielak, G.J.4
  • 25
    • 80555142222 scopus 로고
    • Ph.D. dissertation, University of British Columbia
    • Murphy ME, (1993) pp. 96-112 Ph.D. dissertation, University of British Columbia.
    • (1993) , pp. 96-112
    • Murphy, M.E.1
  • 26
    • 0030781309 scopus 로고    scopus 로고
    • A rationale for the absolute conservation of Asn70 and Pro71 in mitochondrial cytochromes c suggested by protein engineering
    • Wallace CJ, Clark I, (1997) A rationale for the absolute conservation of Asn70 and Pro71 in mitochondrial cytochromes c suggested by protein engineering. Biochemistry 36: 14733-14740.
    • (1997) Biochemistry , vol.36 , pp. 14733-14740
    • Wallace, C.J.1    Clark, I.2
  • 28
    • 0015863377 scopus 로고
    • Thermodynamic studies of the opening of the heme crevice of ferricytochrome c
    • Kaminsky LS, Miller VJ, Davison AJ, (1973) Thermodynamic studies of the opening of the heme crevice of ferricytochrome c. Biochemistry 12: 2215-2221.
    • (1973) Biochemistry , vol.12 , pp. 2215-2221
    • Kaminsky, L.S.1    Miller, V.J.2    Davison, A.J.3
  • 29
    • 0018254177 scopus 로고
    • Alkaline isomerization of horse and yeast cytochromes c. Spectrophotometric and circular dichroism studies
    • Looze Y, Polastro E, Deconinck M, Leonis J, (1978) Alkaline isomerization of horse and yeast cytochromes c. Spectrophotometric and circular dichroism studies. Int J Pept Protein Res 12 (5): 233-236.
    • (1978) Int J Pept Protein Res , vol.12 , Issue.5 , pp. 233-236
    • Looze, Y.1    Polastro, E.2    Deconinck, M.3    Leonis, J.4
  • 30
    • 0030727547 scopus 로고    scopus 로고
    • The soret circular dichroism spectrum as a probe for the heme Fe(III)-Met(80) axial bond in horse cytochrome c
    • Santucci R, Ascoli F, (1997) The soret circular dichroism spectrum as a probe for the heme Fe(III)-Met(80) axial bond in horse cytochrome c. J Inorg Biochem 68 (3): 211-214.
    • (1997) J Inorg Biochem , vol.68 , Issue.3 , pp. 211-214
    • Santucci, R.1    Ascoli, F.2
  • 31
    • 0016283177 scopus 로고
    • Alkaline isomerization of ferricytochrome c from Euglena gracilis
    • Stellwagen E, Cass R, (1974) Alkaline isomerization of ferricytochrome c from Euglena gracilis. Biochem Biophys Res Commun 60 (1): 371-375.
    • (1974) Biochem Biophys Res Commun , vol.60 , Issue.1 , pp. 371-375
    • Stellwagen, E.1    Cass, R.2
  • 32
    • 0027818118 scopus 로고
    • Complete assignment of cytochrome c resonance Raman spectra via enzymic reconstitution with isotopically labeled hemes
    • Hu S, Morris IK, Singh JP, Smith KM, Spiro TG, (1993) Complete assignment of cytochrome c resonance Raman spectra via enzymic reconstitution with isotopically labeled hemes. J Am Chem Soc 115 (26): 12446-12458.
    • (1993) J Am Chem Soc , vol.115 , Issue.26 , pp. 12446-12458
    • Hu, S.1    Morris, I.K.2    Singh, J.P.3    Smith, K.M.4    Spiro, T.G.5
  • 33
    • 0028358619 scopus 로고
    • Novel axial ligand interchange in cytochrome c: incorporation of a histidine at position 82 leads to displacement of the wild-Type methionine-80 ligand
    • Hawkins BK, Hilgen-Willis S, Pielak GJ, Dawson JH, (1994) Novel axial ligand interchange in cytochrome c: incorporation of a histidine at position 82 leads to displacement of the wild-Type methionine-80 ligand. J Am Chem Soc 116 (7): 3111-3112.
    • (1994) J Am Chem Soc , vol.116 , Issue.7 , pp. 3111-3112
    • Hawkins, B.K.1    Hilgen-Willis, S.2    Pielak, G.J.3    Dawson, J.H.4
  • 34
    • 0030024551 scopus 로고    scopus 로고
    • Oxidation state-induced change of iron ligand in the phenylalanine-82 to histidine mutant of yeast Iso-1-cytochrome c
    • Schejter A, Taler G, Navon G, Liu XJ, Margoliash E, (1996) Oxidation state-induced change of iron ligand in the phenylalanine-82 to histidine mutant of yeast Iso-1-cytochrome c. J Am Chem Soc 118 (2): 477-478.
    • (1996) J Am Chem Soc , vol.118 , Issue.2 , pp. 477-478
    • Schejter, A.1    Taler, G.2    Navon, G.3    Liu, X.J.4    Margoliash, E.5
  • 35
    • 0024288939 scopus 로고
    • Two-dimensional NMR as a probe of structural similarity applied to mutants of cytochrome c
    • Pielak GJ, Boyd J, Moore GR, Williams RJ, (1988) Two-dimensional NMR as a probe of structural similarity applied to mutants of cytochrome c. Eur J Biochem 177: 167-177.
    • (1988) Eur J Biochem , vol.177 , pp. 167-177
    • Pielak, G.J.1    Boyd, J.2    Moore, G.R.3    Williams, R.J.4
  • 36
    • 0030748706 scopus 로고    scopus 로고
    • Solution structure of oxidized Saccharomyces cerevisiae iso-1-cytochrome c
    • Banci L, Bertini I, Bren KL, Gray HB, Sompornpisut P, et al. (1997) Solution structure of oxidized Saccharomyces cerevisiae iso-1-cytochrome c. Biochemistry 36: 8992-9001.
    • (1997) Biochemistry , vol.36 , pp. 8992-9001
    • Banci, L.1    Bertini, I.2    Bren, K.L.3    Gray, H.B.4    Sompornpisut, P.5
  • 37
    • 0029855438 scopus 로고    scopus 로고
    • Three-dimensional solution structure of Saccharomyces cerevisiae reduced iso-1-cytochrome c
    • Baistrocchi P, Banci L, Bertini I, Turano P, (1996) Three-dimensional solution structure of Saccharomyces cerevisiae reduced iso-1-cytochrome c. Biochemistry 35: 13788-13796.
    • (1996) Biochemistry , vol.35 , pp. 13788-13796
    • Baistrocchi, P.1    Banci, L.2    Bertini, I.3    Turano, P.4
  • 38
    • 0034296491 scopus 로고    scopus 로고
    • Sources of and solutions to problems in the refinement of protein NMR structures against torsion angle potentials of mean force
    • Kuszewski J, Clore GM, (2000) Sources of and solutions to problems in the refinement of protein NMR structures against torsion angle potentials of mean force. J Magn Reson 146: 249-254.
    • (2000) J Magn Reson , vol.146 , pp. 249-254
    • Kuszewski, J.1    Clore, G.M.2
  • 39
    • 11844263892 scopus 로고    scopus 로고
    • Conversion of the Escherichia coli Cytochrome b562 to an archetype cytochrome b: A mutant with bis-histidine ligation of heme iron
    • Hay S, Wydrzynski T, (2005) Conversion of the Escherichia coli Cytochrome b562 to an archetype cytochrome b: A mutant with bis-histidine ligation of heme iron. Biochemistry 44: 431-439.
    • (2005) Biochemistry , vol.44 , pp. 431-439
    • Hay, S.1    Wydrzynski, T.2
  • 41
    • 0035851190 scopus 로고    scopus 로고
    • Ligand-switching intermediates for the CO-sensing transcriptional activator CooA measured by pulse radiolysis
    • Nakajima H, Nakagawa E, Kobayashi K, Tagawa S, Aono S, (2001) Ligand-switching intermediates for the CO-sensing transcriptional activator CooA measured by pulse radiolysis. J Biol Chem 276 (41): 37895-37899.
    • (2001) J Biol Chem , vol.276 , Issue.41 , pp. 37895-37899
    • Nakajima, H.1    Nakagawa, E.2    Kobayashi, K.3    Tagawa, S.4    Aono, S.5
  • 42
    • 0032475847 scopus 로고    scopus 로고
    • Redox-controlled ligand exchange of the heme in the CO-sensing transcriptional activator CooA
    • Aono S, Ohkubo K, Matsuo T, Nakajima H, (1998) Redox-controlled ligand exchange of the heme in the CO-sensing transcriptional activator CooA. J Biol Chem 273: 25757-25764.
    • (1998) J Biol Chem , vol.273 , pp. 25757-25764
    • Aono, S.1    Ohkubo, K.2    Matsuo, T.3    Nakajima, H.4
  • 43
    • 0032500334 scopus 로고    scopus 로고
    • EPR and electronic absorption spectroscopies of the CO-Sensing CooA protein reveal a cysteine-ligated low-spin ferric heme
    • Reynolds MF, Shelver D, Kerby RL, Park RB, Roberts GP, et al. (1998) EPR and electronic absorption spectroscopies of the CO-Sensing CooA protein reveal a cysteine-ligated low-spin ferric heme. J Am Chem Soc 120: 9080-9081.
    • (1998) J Am Chem Soc , vol.120 , pp. 9080-9081
    • Reynolds, M.F.1    Shelver, D.2    Kerby, R.L.3    Park, R.B.4    Roberts, G.P.5
  • 44
    • 0035831489 scopus 로고    scopus 로고
    • Redox properties and coordination structure of the heme in the CO-sensing transcriptional activator CooA
    • Nakajima H, Honma Y, Tawara T, Kato T, Park S-Y, et al. (2001) Redox properties and coordination structure of the heme in the CO-sensing transcriptional activator CooA. J Biol Chem 276: 7055-7061.
    • (2001) J Biol Chem , vol.276 , pp. 7055-7061
    • Nakajima, H.1    Honma, Y.2    Tawara, T.3    Kato, T.4    Park, S.-Y.5
  • 45
    • 0033514973 scopus 로고    scopus 로고
    • Identification of two important heme site residues (cysteine 75 and histidine 77) in CooA, the CO-Sensing transcription factor of Rhodospirillum rubrum
    • Shelver D, Thorsteinsson MV, Kerby RL, Chung S-Y, Roberts GP, et al. (1999) Identification of two important heme site residues (cysteine 75 and histidine 77) in CooA, the CO-Sensing transcription factor of Rhodospirillum rubrum. Biochemistry 38: 2669-2678.
    • (1999) Biochemistry , vol.38 , pp. 2669-2678
    • Shelver, D.1    Thorsteinsson, M.V.2    Kerby, R.L.3    Chung, S.-Y.4    Roberts, G.P.5
  • 46
    • 0033613069 scopus 로고    scopus 로고
    • Probing the heme axial ligation in the CO-Sensing CooA protein with magnetic circular dichroism spectroscopy
    • Dhawan IK, Shelver D, Thorsteinsson MV, Roberts GP, Johnson MK, (1999) Probing the heme axial ligation in the CO-Sensing CooA protein with magnetic circular dichroism spectroscopy. Biochemistry 39: 12805-12813.
    • (1999) Biochemistry , vol.39 , pp. 12805-12813
    • Dhawan, I.K.1    Shelver, D.2    Thorsteinsson, M.V.3    Roberts, G.P.4    Johnson, M.K.5
  • 47
    • 0033515050 scopus 로고    scopus 로고
    • Resonance raman evidence for a novel charge relay activation mechanism of the CO-dependent heme protein transcription factor CooA
    • Vogel KM, Spiro TG, Shelver D, Thorsteinsson MV, Roberts GP, (1999) Resonance raman evidence for a novel charge relay activation mechanism of the CO-dependent heme protein transcription factor CooA. Biochemistry 38: 2679-2687.
    • (1999) Biochemistry , vol.38 , pp. 2679-2687
    • Vogel, K.M.1    Spiro, T.G.2    Shelver, D.3    Thorsteinsson, M.V.4    Roberts, G.P.5
  • 48
    • 34547854130 scopus 로고    scopus 로고
    • Elucidating the hard/soft acid/base principle: a perspective based on half-reactions
    • Ayers PW, Parr RG, Pearson RG, (2006) Elucidating the hard/soft acid/base principle: a perspective based on half-reactions. J Chem Phys 124 (19): 194107-194113.
    • (2006) J Chem Phys , vol.124 , Issue.19 , pp. 194107-194113
    • Ayers, P.W.1    Parr, R.G.2    Pearson, R.G.3
  • 49
    • 27744433524 scopus 로고    scopus 로고
    • Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors
    • Kagan VE, Tyurin VA, Jiang J, Tyurina YY, et al. (2005) Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors. Nat Chem Biol 1: 223-232.
    • (2005) Nat Chem Biol , vol.1 , pp. 223-232
    • Kagan, V.E.1    Tyurin, V.A.2    Jiang, J.3    Tyurina, Y.Y.4
  • 50
    • 68149136523 scopus 로고    scopus 로고
    • Tyrosine-67 in cytochrome c is a possible apoptotic trigger controlled by hydrogen bonds via a conformational transition
    • Ying T, Wang Z, Lin Y, Xie J, Tan XS, et al. (2009) Tyrosine-67 in cytochrome c is a possible apoptotic trigger controlled by hydrogen bonds via a conformational transition. Chem Commun 30: 4512-4514.
    • (2009) Chem Commun , vol.30 , pp. 4512-4514
    • Ying, T.1    Wang, Z.2    Lin, Y.3    Xie, J.4    Tan, X.S.5
  • 51
    • 77952417739 scopus 로고    scopus 로고
    • Distinct mechanisms for the pro-apoptotic conformational transition and alkaline transition in cytochrome c
    • Ying T, Wang ZH, Zhong F, Tan X, Huang ZX, (2010) Distinct mechanisms for the pro-apoptotic conformational transition and alkaline transition in cytochrome c, Chem Commun 46: 3541-3543.
    • (2010) Chem Commun , vol.46 , pp. 3541-3543
    • Ying, T.1    Wang, Z.H.2    Zhong, F.3    Tan, X.4    Huang, Z.X.5
  • 52
    • 0032574759 scopus 로고    scopus 로고
    • Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in Yeast iso-1-Cytochrome c and the alkaline conformational transition
    • Pollock WB, Rosell FT, Twitchett MB, Dumont ME, Mauk AG, (1998) Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in Yeast iso-1-Cytochrome c and the alkaline conformational transition. Biochemistry 37: 6124-6131.
    • (1998) Biochemistry , vol.37 , pp. 6124-6131
    • Pollock, W.B.1    Rosell, F.T.2    Twitchett, M.B.3    Dumont, M.E.4    Mauk, A.G.5
  • 53
    • 0037129949 scopus 로고    scopus 로고
    • Spectroscopic properties of a mitochondrial Cytochrome c with a single thioether bond to the heme prosthetic group
    • Rosell FI, Mauk AG, (2002) Spectroscopic properties of a mitochondrial Cytochrome c with a single thioether bond to the heme prosthetic group. Biochemistry 41: 7811-8.
    • (2002) Biochemistry , vol.41 , pp. 7811-7818
    • Rosell, F.I.1    Mauk, A.G.2
  • 54
    • 0037054860 scopus 로고    scopus 로고
    • Production and characterisation of Met80X mutants of yeast iso-1-cytochrome c: spectral, photochemical and binding studies on the ferrous derivatives
    • Silkstone G, Stanway G, Brzezinski P, Wilson MT, (2002) Production and characterisation of Met80X mutants of yeast iso-1-cytochrome c: spectral, photochemical and binding studies on the ferrous derivatives. Biophys Chem 98: 65-77.
    • (2002) Biophys Chem , vol.98 , pp. 65-77
    • Silkstone, G.1    Stanway, G.2    Brzezinski, P.3    Wilson, M.T.4
  • 55
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry EA, Trumpower BL, (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra. Anal Biochem 161: 1-15.
    • (1987) Anal Biochem , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 56
    • 0000849756 scopus 로고
    • The relevance of J cross-peaks in two-dimensional NOE experiments of macromolecules
    • Macura S, Wuthrich K, Ernst RR, (1982) The relevance of J cross-peaks in two-dimensional NOE experiments of macromolecules. J Magn Reson 47: 351-357.
    • (1982) J Magn Reson , vol.47 , pp. 351-357
    • Macura, S.1    Wuthrich, K.2    Ernst, R.R.3
  • 57
    • 0001507764 scopus 로고
    • Proton NOE studies on dicopper(II) dicobalt(II) superoxide dismutase
    • Banci L, Bertini I, Luchinat C, Piccioli M, Scozzafava A, et al. (1989) Proton NOE studies on dicopper(II) dicobalt(II) superoxide dismutase. Inorg Chem 28: 4650-4656.
    • (1989) Inorg Chem , vol.28 , pp. 4650-4656
    • Banci, L.1    Bertini, I.2    Luchinat, C.3    Piccioli, M.4    Scozzafava, A.5
  • 58
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A, Davis DG, (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J Magn Reson 65: 355-360.
    • (1985) J Magn Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 59
    • 11844258838 scopus 로고    scopus 로고
    • EPR and optical spectroscopic studies of Met80X Mutants of yeast ferricytochrome c. Models for Intermediates in the alkaline transition
    • Silkstone GG, Cooper CE, Svistunenko D, Wilson MT, (2005) EPR and optical spectroscopic studies of Met80X Mutants of yeast ferricytochrome c. Models for Intermediates in the alkaline transition. J Am Chem Soc 127: 92-9.
    • (2005) J Am Chem Soc , vol.127 , pp. 92-99
    • Silkstone, G.G.1    Cooper, C.E.2    Svistunenko, D.3    Wilson, M.T.4
  • 60
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M, Saudek V, Sklenar V, (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 2: 661-665.
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 61
    • 0029400480 scopus 로고
    • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, et al. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: 277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.