메뉴 건너뛰기




Volumn 51, Issue 30, 2012, Pages 5967-5978

Role of Met80 and Tyr67 in the low-pH conformational equilibria of cytochrome c

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL EQUILIBRIUM; COOPERATIVE TRANSITIONS; CYTOCHROME C; ELECTRONIC ABSORPTION; HYDROGEN BONDING NETWORK; IRON ATOMS; LOW IONIC STRENGTH; MAGNETIC CIRCULAR DICHROISMS; MOLTEN GLOBULE; MOLTEN GLOBULE STATE; PH VALUE; PROTEIN STRUCTURES; RESONANCE RAMAN SPECTROSCOPY; SPIN STATE; THREE-DIMENSIONAL STRUCTURE; WILD TYPES;

EID: 84864434524     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3007302     Document Type: Article
Times cited : (37)

References (110)
  • 1
    • 0030433170 scopus 로고    scopus 로고
    • Protein dynamics and conformational transitions in allosteric proteins
    • Jardetzky, O. (1996) Protein dynamics and conformational transitions in allosteric proteins Prog. Biophys. Mol. Biol. 65, 171-219
    • (1996) Prog. Biophys. Mol. Biol. , vol.65 , pp. 171-219
    • Jardetzky, O.1
  • 2
    • 0031282975 scopus 로고    scopus 로고
    • Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps
    • Lanyi, J. K. (1997) Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps J. Biol. Chem. 272, 31209-31212
    • (1997) J. Biol. Chem. , vol.272 , pp. 31209-31212
    • Lanyi, J.K.1
  • 3
    • 0141918782 scopus 로고    scopus 로고
    • Proteins in action: The physics of structural fluctuations and conformational changes
    • Parak, F. G. (2003) Proteins in action: The physics of structural fluctuations and conformational changes Curr. Opin. Struct. Biol. 13, 552-557
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 552-557
    • Parak, F.G.1
  • 4
    • 0037183064 scopus 로고    scopus 로고
    • Spectroscopic Characterization of Nonnative Conformational States of Cytochrome c
    • Oellerich, S., Wackerbarth, H., and Hildebrandt, P. (2002) Spectroscopic Characterization of Nonnative Conformational States of Cytochrome c J. Phys. Chem. B 106, 6566-6580
    • (2002) J. Phys. Chem. B , vol.106 , pp. 6566-6580
    • Oellerich, S.1    Wackerbarth, H.2    Hildebrandt, P.3
  • 5
    • 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.-H., Lin, Y.-W., Xie, J., Tan, X., and Huang, Z.-X. (2009) Tyrosine-67 in cytochrome c is a possible apoptotic trigger controlled by hydrogen bonds via a conformational transition Chem. Commun., 4512-4514
    • (2009) Chem. Commun. , pp. 4512-4514
    • Ying, T.1    Wang, Z.-H.2    Lin, Y.-W.3    Xie, J.4    Tan, X.5    Huang, Z.-X.6
  • 6
    • 69549120468 scopus 로고    scopus 로고
    • Thermodynamic basis for the optimization of binding-induced biomolecular switches and structure-switching biosensors
    • Valle-Belisle, A., Ricci, F., and Plaxco, K. W. (2009) Thermodynamic basis for the optimization of binding-induced biomolecular switches and structure-switching biosensors Proc. Natl. Acad. Sci. U.S.A. 106, 13802-13807
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 13802-13807
    • Valle-Belisle, A.1    Ricci, F.2    Plaxco, K.W.3
  • 7
    • 0013437682 scopus 로고    scopus 로고
    • Photochemical Biomolecular Switches: The Route to Optobioelectronics
    • (Feringa, B. L. Ed.) Wiley-VCH Verlag GmbH, Weinheim, Germany.
    • Willner, I. and Willner, B. (2001) Photochemical Biomolecular Switches: The Route to Optobioelectronics. In Molecular Switches (Feringa, B. L., Ed.) Wiley-VCH Verlag GmbH, Weinheim, Germany.
    • (2001) Molecular Switches
    • Willner, I.1    Willner, B.2
  • 8
    • 78650419952 scopus 로고    scopus 로고
    • Switch-based biosensors: A new approach towards real-time, in vivo molecular detection
    • Plaxco, K. W. and Soh, H. T. (2011) Switch-based biosensors: A new approach towards real-time, in vivo molecular detection Trends Biotechnol. 29, 1-5
    • (2011) Trends Biotechnol. , vol.29 , pp. 1-5
    • Plaxco, K.W.1    Soh, H.T.2
  • 9
    • 77955984136 scopus 로고    scopus 로고
    • Structure-switching biosensors: Inspired by Nature
    • Valle-Belisle, A. and Plaxco, K. W. (2010) Structure-switching biosensors: Inspired by Nature Curr. Opin. Struct. Biol. 20, 518-526
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 518-526
    • Valle-Belisle, A.1    Plaxco, K.W.2
  • 14
    • 0034306169 scopus 로고    scopus 로고
    • Cardiolipin provides specificity for targeting of tBid to mitochondria
    • Lutter, M., Fang, M., Luo, X., Nishijima, M., Xie, X.-S., and Wang, X. (2000) Cardiolipin provides specificity for targeting of tBid to mitochondria Nat. Cell Biol. 2, 754-756
    • (2000) Nat. Cell Biol. , vol.2 , pp. 754-756
    • Lutter, M.1    Fang, M.2    Luo, X.3    Nishijima, M.4    Xie, X.-S.5    Wang, X.6
  • 15
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck, R. M., Bossy-Wetzel, E., Green, D. R., and Newmayer, D. D. (1997) The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis Science 275, 1132-1136
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmayer, D.D.4
  • 16
    • 3943071150 scopus 로고    scopus 로고
    • Cytochrome c mediated apoptosis
    • Jang, X. and Wang, X. (2004) Cytochrome c mediated apoptosis Annu. Rev. Biochem. 73, 87-106
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 87-106
    • Jang, X.1    Wang, X.2
  • 17
    • 1842639828 scopus 로고    scopus 로고
    • Mitochondria in apoptosis: Past, present and future
    • Degli Esposti, M. (2004) Mitochondria in apoptosis: Past, present and future Biochem. Soc. Trans. 32, 493-495
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 493-495
    • Degli Esposti, M.1
  • 18
    • 83055197001 scopus 로고    scopus 로고
    • Probing a complex of cytochrome c and cardiolipin by magnetic circular dichroism spectroscopy: Implications for the initial events in apoptosis
    • Bradley, J. M., Silkestone, G., Wilson, M. T., Cheesman, M. R., and Butt, J. N. (2011) Probing a complex of cytochrome c and cardiolipin by magnetic circular dichroism spectroscopy: Implications for the initial events in apoptosis J. Am. Chem. Soc. 133, 19676-19679
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 19676-19679
    • Bradley, J.M.1    Silkestone, G.2    Wilson, M.T.3    Cheesman, M.R.4    Butt, J.N.5
  • 21
    • 0033580825 scopus 로고    scopus 로고
    • Ligand exchange during unfolding of cytochrome c
    • Yeh, S.-R. and Rousseau, D. L. (1999) Ligand exchange during unfolding of cytochrome c J. Biol. Chem. 274, 17853-17859
    • (1999) J. Biol. Chem. , vol.274 , pp. 17853-17859
    • Yeh, S.-R.1    Rousseau, D.L.2
  • 22
    • 0000519105 scopus 로고    scopus 로고
    • Cytochrome c folding and unfolding: A biphasic mechanism
    • Yeh, S. R., Han, S., and Rousseau, D. L. (1998) Cytochrome c folding and unfolding: A biphasic mechanism Acc. Chem. Res. 31, 727-736
    • (1998) Acc. Chem. Res. , vol.31 , pp. 727-736
    • Yeh, S.R.1    Han, S.2    Rousseau, D.L.3
  • 23
    • 0031952599 scopus 로고    scopus 로고
    • Folding intermediates in cytochrome c
    • Yeh, S. R. and Rousseau, D. L. (1998) Folding intermediates in cytochrome c Nat. Struct. Biol. 5, 222-228
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 222-228
    • Yeh, S.R.1    Rousseau, D.L.2
  • 27
    • 0038786579 scopus 로고    scopus 로고
    • Cooperative Ω loops in cytochrome c: Role in folding and function
    • Krishna, M. M. G., Lin, Y., Rumbley, J. N., and Englander, S. W. (2003) Cooperative Ω loops in cytochrome c: Role in folding and function J. Mol. Biol. 331, 29-36
    • (2003) J. Mol. Biol. , vol.331 , pp. 29-36
    • Krishna, M.M.G.1    Lin, Y.2    Rumbley, J.N.3    Englander, S.W.4
  • 28
    • 0034025695 scopus 로고    scopus 로고
    • Characterization of equilibrium intermediates in denaturant-induced unfolding of ferrous and ferric cytochromes c using magnetic circular dichroism, circular dichroism, and optical absorption spectroscopies
    • Thomas, Y. G., Goldbeck, R. A., and Kliger, D. S. (2000) Characterization of equilibrium intermediates in denaturant-induced unfolding of ferrous and ferric cytochromes c using magnetic circular dichroism, circular dichroism, and optical absorption spectroscopies Biopolymers 57, 29-36
    • (2000) Biopolymers , vol.57 , pp. 29-36
    • Thomas, Y.G.1    Goldbeck, R.A.2    Kliger, D.S.3
  • 29
    • 79953867209 scopus 로고    scopus 로고
    • Thermodynamic and structural properties of the acid molten globule state of horse cytochrome c
    • Nakamura, S., Seki, Y., Katoh, E., and Kidokoro, S.-I. (2011) Thermodynamic and structural properties of the acid molten globule state of horse cytochrome c Biochemistry 50, 3116-3126
    • (2011) Biochemistry , vol.50 , pp. 3116-3126
    • Nakamura, S.1    Seki, Y.2    Katoh, E.3    Kidokoro, S.-I.4
  • 30
    • 1942467089 scopus 로고    scopus 로고
    • Optical spectroscopic differentiation of various equilibrium denatured states of horse cytochrome c
    • Xu, Q. and Keiderling, T. A. (2004) Optical spectroscopic differentiation of various equilibrium denatured states of horse cytochrome c Biopolymers 73, 716-726
    • (2004) Biopolymers , vol.73 , pp. 716-726
    • Xu, Q.1    Keiderling, T.A.2
  • 31
    • 66349104530 scopus 로고    scopus 로고
    • Compressing the free energy range of substructure stabilities in iso-1-cytochrome c
    • Duncan, M. G., Williams, M. D., and Bowler, B. E. (2009) Compressing the free energy range of substructure stabilities in iso-1-cytochrome c Protein Sci. 18, 1155-1164
    • (2009) Protein Sci. , vol.18 , pp. 1155-1164
    • Duncan, M.G.1    Williams, M.D.2    Bowler, B.E.3
  • 32
    • 10044269982 scopus 로고    scopus 로고
    • Many faces of the unfolded state: Conformational heterogeneity in denatured yeast cytochrome c
    • Pletneva, E. V., Gray, H. B., and Winkler, J. R. (2005) Many faces of the unfolded state: Conformational heterogeneity in denatured yeast cytochrome c J. Mol. Biol. 345, 855-867
    • (2005) J. Mol. Biol. , vol.345 , pp. 855-867
    • Pletneva, E.V.1    Gray, H.B.2    Winkler, J.R.3
  • 33
    • 27644586821 scopus 로고    scopus 로고
    • Nature of the cytochrome c molten globule
    • Pletneva, E. V., Gray, H. B., and Winkler, J. R. (2005) Nature of the cytochrome c molten globule J. Am. Chem. Soc. 127, 15370-15371
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15370-15371
    • Pletneva, E.V.1    Gray, H.B.2    Winkler, J.R.3
  • 34
    • 0043143394 scopus 로고    scopus 로고
    • Cytochrome c folding and stability
    • (Scott, R. A. and Mauk, A. G. Eds.) University Science Books, Sausalito, CA.
    • Nall, B. T. (1996) Cytochrome c folding and stability. In Cytochrome c: A multidisciplinary approach (Scott, R. A. and Mauk, A. G., Eds.) pp 167-200, University Science Books, Sausalito, CA.
    • (1996) Cytochrome C: A Multidisciplinary Approach , pp. 167-200
    • Nall, B.T.1
  • 35
    • 0000431715 scopus 로고    scopus 로고
    • The Alkaline Transition in Ferricytochrome c
    • (Scott, R. A. and Mauk, A. G. Eds.) University Science Books, Sausalito, CA.
    • Wilson, M. T. and Greenwood, C. (1996) The Alkaline Transition in Ferricytochrome c. In Cytochrome c: A multidisciplinary approach (Scott, R. A. and Mauk, A. G., Eds.) pp 611-634, University Science Books, Sausalito, CA.
    • (1996) Cytochrome C: A Multidisciplinary Approach , pp. 611-634
    • Wilson, M.T.1    Greenwood, C.2
  • 36
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto, Y., Takahashi, N., and Finks, A. L. (1990) Mechanism of acid-induced folding of proteins Biochemistry 29, 3480-3488
    • (1990) Biochemistry , vol.29 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Finks, A.L.3
  • 39
    • 0035859878 scopus 로고    scopus 로고
    • A two-process model describes the hydrogen exchange behavior of cytochrome c in the molten globule state with various extents of acetylation
    • Szewczuk, Z., Konishi, Y., and Goto, Y. (2001) A two-process model describes the hydrogen exchange behavior of cytochrome c in the molten globule state with various extents of acetylation Biochemistry 40, 9623-9630
    • (2001) Biochemistry , vol.40 , pp. 9623-9630
    • Szewczuk, Z.1    Konishi, Y.2    Goto, Y.3
  • 40
    • 0015222174 scopus 로고
    • Studies on Ferricytochrome c. 1. Effect of pH, Ionic Strength and Protein Denaturants on the Spectra of Ferricytochrome c
    • Greenwood, C. and Wilson, M. T. (1971) Studies on Ferricytochrome c. 1. Effect of pH, Ionic Strength and Protein Denaturants on the Spectra of Ferricytochrome c Eur. J. Biochem. 22, 5-10
    • (1971) Eur. J. Biochem. , vol.22 , pp. 5-10
    • Greenwood, C.1    Wilson, M.T.2
  • 41
    • 0015526732 scopus 로고
    • Participation of the protein ligands in the folding of cytochrome c
    • Babul, J. and Stellwagen, E. (1972) Participation of the protein ligands in the folding of cytochrome c Biochemistry 11, 1195-1200
    • (1972) Biochemistry , vol.11 , pp. 1195-1200
    • Babul, J.1    Stellwagen, E.2
  • 42
    • 0016717998 scopus 로고
    • Stabilization of the globular structure of ferricytochrome c by chloride in acidic solvents
    • Stellwagen, E. and Babul, J. (1975) Stabilization of the globular structure of ferricytochrome c by chloride in acidic solvents Biochemistry 14, 5135-5140
    • (1975) Biochemistry , vol.14 , pp. 5135-5140
    • Stellwagen, E.1    Babul, J.2
  • 43
    • 0015935372 scopus 로고
    • The interaction of chaotropic anions with acid ferricytochrome c
    • Aviram, I. (1973) The interaction of chaotropic anions with acid ferricytochrome c J. Biol. Chem. 248, 1891-1896
    • (1973) J. Biol. Chem. , vol.248 , pp. 1891-1896
    • Aviram, I.1
  • 44
    • 0018476470 scopus 로고
    • Conformational transitions and vibronic couplings in acid ferricytochrome c: A resonance Raman study
    • Lanir, A., Yu, N.-T., and Felton, R. H. (1979) Conformational transitions and vibronic couplings in acid ferricytochrome c: A resonance Raman study Biochemistry 18, 1656-1660
    • (1979) Biochemistry , vol.18 , pp. 1656-1660
    • Lanir, A.1    Yu, N.-T.2    Felton, R.H.3
  • 46
    • 0020478683 scopus 로고
    • Spin state and unfolding equilibria of ferricytochrome c in acidic solutions
    • Dyson, H. J. and Beattie, J. K. (1982) Spin state and unfolding equilibria of ferricytochrome c in acidic solutions J. Biol. Chem. 257, 2267-2273
    • (1982) J. Biol. Chem. , vol.257 , pp. 2267-2273
    • Dyson, H.J.1    Beattie, J.K.2
  • 47
    • 33846862641 scopus 로고    scopus 로고
    • Conformational transitions of ferricytochrome c in strong inorganic acids
    • Stupak, M., Bagelova, J., Fedunova, D., and Antalik, M. (2006) Conformational transitions of ferricytochrome c in strong inorganic acids Collect. Czech. Chem. Commun. 71, 1627-1641
    • (2006) Collect. Czech. Chem. Commun. , vol.71 , pp. 1627-1641
    • Stupak, M.1    Bagelova, J.2    Fedunova, D.3    Antalik, M.4
  • 48
    • 33645691874 scopus 로고    scopus 로고
    • Mutation of asparagine 52 to glycine promotes the alkaline form of iso-1-cytochrome c and causes loss of cooperativity in acid unfolding
    • Baddam, S. and Bowler, B. E. (2006) Mutation of asparagine 52 to glycine promotes the alkaline form of iso-1-cytochrome c and causes loss of cooperativity in acid unfolding Biochemistry 45, 4611-4619
    • (2006) Biochemistry , vol.45 , pp. 4611-4619
    • Baddam, S.1    Bowler, B.E.2
  • 49
    • 0037732539 scopus 로고    scopus 로고
    • Rupture of the hydrogen bond linking two Ω-loops induces the molten globule state at neutral pH in cytochrome c
    • Sinibaldi, F., Piro, M. C., Howes, B. D., Smulevich, G., Ascoli, F., and Santucci, R. (2003) Rupture of the hydrogen bond linking two Ω-loops induces the molten globule state at neutral pH in cytochrome c Biochemistry 42, 7604-7610
    • (2003) Biochemistry , vol.42 , pp. 7604-7610
    • Sinibaldi, F.1    Piro, M.C.2    Howes, B.D.3    Smulevich, G.4    Ascoli, F.5    Santucci, R.6
  • 50
    • 0043157689 scopus 로고    scopus 로고
    • Anion concentration modulates the conformation and stability of the molten globule of cytochrome c
    • Sinibaldi, F., Howes, B. D., Smulevich, G., Ciaccio, C., Coletta, M., and Santucci, R. (2003) Anion concentration modulates the conformation and stability of the molten globule of cytochrome c J. Biol. Inorg. Chem. 8, 663-670
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 663-670
    • Sinibaldi, F.1    Howes, B.D.2    Smulevich, G.3    Ciaccio, C.4    Coletta, M.5    Santucci, R.6
  • 51
    • 0028953092 scopus 로고
    • Secondary and tertiary structure of the A-state of cytochrome c from resonance Raman spectroscopy
    • Jordan, T., Eads, J. C., and Spiro, T. G. (1995) Secondary and tertiary structure of the A-state of cytochrome c from resonance Raman spectroscopy Protein Sci. 4, 716-728
    • (1995) Protein Sci. , vol.4 , pp. 716-728
    • Jordan, T.1    Eads, J.C.2    Spiro, T.G.3
  • 52
    • 0031555331 scopus 로고    scopus 로고
    • Electrochemical evidence on the molten globule conformation of cytochrome c
    • Pineda, T., Sevilla, J. M., Roman, A. J., and Blazquez, M. (1997) Electrochemical evidence on the molten globule conformation of cytochrome c Biochim. Biophys. Acta 1343, 227-234
    • (1997) Biochim. Biophys. Acta , vol.1343 , pp. 227-234
    • Pineda, T.1    Sevilla, J.M.2    Roman, A.J.3    Blazquez, M.4
  • 53
    • 33646448448 scopus 로고    scopus 로고
    • The redox chemistry of the covalently immobilized native and low-pH forms of yeast iso-1-cytochrome c
    • Bortolotti, C. A., Battistuzzi, G., Borsari, M., Facci, P., Ranieri, A., and Sola, M. (2006) The redox chemistry of the covalently immobilized native and low-pH forms of yeast iso-1-cytochrome c J. Am. Chem. Soc. 128, 5444-5451
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 5444-5451
    • Bortolotti, C.A.1    Battistuzzi, G.2    Borsari, M.3    Facci, P.4    Ranieri, A.5    Sola, M.6
  • 54
    • 39649117135 scopus 로고    scopus 로고
    • Electron transfer and electrocatalytic properties of the immobilized methionine80alanine cytochrome c variant
    • Casalini, S., Battistuzzi, G., Borsari, M., Bortolotti, C. A., Ranieri, A., and Sola, M. (2008) Electron transfer and electrocatalytic properties of the immobilized methionine80alanine cytochrome c variant J. Phys. Chem. B 112, 1555-1563
    • (2008) J. Phys. Chem. B , vol.112 , pp. 1555-1563
    • Casalini, S.1    Battistuzzi, G.2    Borsari, M.3    Bortolotti, C.A.4    Ranieri, A.5    Sola, M.6
  • 55
    • 57349098324 scopus 로고    scopus 로고
    • Catalytic reduction of dioxygen and nitrite ion at a Met80Ala cytochrome c -functionalyzed electrode
    • Casalini, S., Battistuzzi, G., Borsari, M., Ranieri, A., and Sola, M. (2008) Catalytic reduction of dioxygen and nitrite ion at a Met80Ala cytochrome c -functionalyzed electrode J. Am. Chem. Soc. 130, 15099-15104
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15099-15104
    • Casalini, S.1    Battistuzzi, G.2    Borsari, M.3    Ranieri, A.4    Sola, M.5
  • 56
    • 75749100224 scopus 로고    scopus 로고
    • Electron transfer properties and hydrogen peroxide electrocatalysis of cytochrome c variants at positions 67 and 80
    • Casalini, S., Battistuzzi, G., Borsari, M., Bortolotti, C. A., Di Rocco, G., Ranieri, A., and Sola, M. (2010) Electron transfer properties and hydrogen peroxide electrocatalysis of cytochrome c variants at positions 67 and 80 J. Phys. Chem. B 114, 1698-1706
    • (2010) J. Phys. Chem. B , vol.114 , pp. 1698-1706
    • Casalini, S.1    Battistuzzi, G.2    Borsari, M.3    Bortolotti, C.A.4    Di Rocco, G.5    Ranieri, A.6    Sola, M.7
  • 57
    • 0028300174 scopus 로고
    • Mutation of tyrosine-67 to phenylalanine in cytochrome c significantly alters the local heme environment
    • Berghuis, A., Guillemette, J. G., Smith, M. I., and Brayer, G. D. (1994) Mutation of tyrosine-67 to phenylalanine in cytochrome c significantly alters the local heme environment J. Mol. Biol. 235, 1326-1341
    • (1994) J. Mol. Biol. , vol.235 , pp. 1326-1341
    • Berghuis, A.1    Guillemette, J.G.2    Smith, M.I.3    Brayer, G.D.4
  • 58
    • 70349543985 scopus 로고    scopus 로고
    • Conformational flexibility decreased due to Y67F and F82H mutations in cytochrome c: Molecular dynamics simulation studies
    • Raja Singh, S., Prakash, S., Vasu, V., and Karunakaran, C. (2009) Conformational flexibility decreased due to Y67F and F82H mutations in cytochrome c: Molecular dynamics simulation studies J. Mol. Graphics Modell. 28, 270-277
    • (2009) J. Mol. Graphics Modell. , vol.28 , pp. 270-277
    • Raja Singh, S.1    Prakash, S.2    Vasu, V.3    Karunakaran, C.4
  • 59
    • 10544228949 scopus 로고    scopus 로고
    • The role of a conserved water molecule in the redox-dependent thermal stability of iso-1-cytochrome c
    • Lett, C. M., Berghuis, A. M., Frey, H. E., Lepock, J. R., and Guillemette, J. G. (1996) The role of a conserved water molecule in the redox-dependent thermal stability of iso-1-cytochrome c J. Biol. Chem. 271, 29088-29093
    • (1996) J. Biol. Chem. , vol.271 , pp. 29088-29093
    • Lett, C.M.1    Berghuis, A.M.2    Frey, H.E.3    Lepock, J.R.4    Guillemette, J.G.5
  • 61
    • 0026713496 scopus 로고
    • Relationship between local and global stabilities of proteins: Site-directed mutants and chemically-modified derivatives of cytochrome c
    • Schejter, A., Luntz, T. L., Koshy, T. I., and Margoliash, E. (1992) Relationship between local and global stabilities of proteins: Site-directed mutants and chemically-modified derivatives of cytochrome c Biochemistry 31, 8336-8343
    • (1992) Biochemistry , vol.31 , pp. 8336-8343
    • Schejter, A.1    Luntz, T.L.2    Koshy, T.I.3    Margoliash, E.4
  • 62
    • 0024672760 scopus 로고
    • Structural significance of an internal water molecule studied by site-directed mutagenesis of tyrosine-67 in rat cytochrome c
    • Luntz, T. L., Schejter, A., Garber, E. A. E., and Margoliash, E. (1989) Structural significance of an internal water molecule studied by site-directed mutagenesis of tyrosine-67 in rat cytochrome c Proc. Natl. Acad. Sci. U.S.A. 86, 3524-3528
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 3524-3528
    • Luntz, T.L.1    Schejter, A.2    Garber, E.A.E.3    Margoliash, E.4
  • 63
    • 0032898347 scopus 로고    scopus 로고
    • Using entropies of reaction to predict changes in protein stability: Tyrosine-67-phenylalanine variants of rat cytochrome c and yeast iso-1 cytochromes c
    • Feinberg, B. A., Petro, L., Hock, G., Qin, W., and Margoliash, E. (1999) Using entropies of reaction to predict changes in protein stability: Tyrosine-67-phenylalanine variants of rat cytochrome c and yeast iso-1 cytochromes c J. Pharm. Biomed. Anal. 19, 115-125
    • (1999) J. Pharm. Biomed. Anal. , vol.19 , pp. 115-125
    • Feinberg, B.A.1    Petro, L.2    Hock, G.3    Qin, W.4    Margoliash, E.5
  • 64
    • 27744582890 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of formation of the alkaline state of a Lys79/Ala Lys73/His variant of iso-1-cytochrome c
    • Baddam, S. and Bowler, B. E. (2005) Thermodynamics and kinetics of formation of the alkaline state of a Lys79/Ala Lys73/His variant of iso-1-cytochrome c Biochemistry 44, 14956-14968
    • (2005) Biochemistry , vol.44 , pp. 14956-14968
    • Baddam, S.1    Bowler, B.E.2
  • 65
    • 0033524433 scopus 로고    scopus 로고
    • Effect of pH on formation of a nativelike intermediate on the unfolding pathway of a Lys73/His variant of yeast iso-1-cytochrome c
    • Godbole, S. and Bowler, B. E. (1999) Effect of pH on formation of a nativelike intermediate on the unfolding pathway of a Lys73/His variant of yeast iso-1-cytochrome c Biochemistry 38, 487-495
    • (1999) Biochemistry , vol.38 , pp. 487-495
    • Godbole, S.1    Bowler, B.E.2
  • 66
    • 34848826523 scopus 로고    scopus 로고
    • Insights into porphyrin chemistry provided by the microperoxidases, the haempeptides derived from cytochrome c
    • Marques, H. M. (2007) Insights into porphyrin chemistry provided by the microperoxidases, the haempeptides derived from cytochrome c Dalton Trans., 4371-4385
    • (2007) Dalton Trans. , pp. 4371-4385
    • Marques, H.M.1
  • 67
    • 0001645795 scopus 로고    scopus 로고
    • Heme-peptide models for hemoproteins. 1. Solution chemistry of N-acetylmicroperoxidase-8
    • Munro, O. Q. and Marques, H. M. (1996) Heme-peptide models for hemoproteins. 1. Solution chemistry of N-acetylmicroperoxidase-8 Inorg. Chem. 35, 3752-3767
    • (1996) Inorg. Chem. , vol.35 , pp. 3752-3767
    • Munro, O.Q.1    Marques, H.M.2
  • 68
    • 0033618922 scopus 로고    scopus 로고
    • Magnetic circular dichroism studies of the active site heme coordination sphere of exogenous ligand-free ferric cytochrome c peroxidase from yeast: Effects of sample history and pH
    • Pond, A. E., Sono, M., Elenkova, E. A., McRee, D. E., Goodin, D. B., English, A. M., and Dawson, J. H. (1999) Magnetic circular dichroism studies of the active site heme coordination sphere of exogenous ligand-free ferric cytochrome c peroxidase from yeast: Effects of sample history and pH J. Inorg. Biochem. 76, 165-174
    • (1999) J. Inorg. Biochem. , vol.76 , pp. 165-174
    • Pond, A.E.1    Sono, M.2    Elenkova, E.A.3    McRee, D.E.4    Goodin, D.B.5    English, A.M.6    Dawson, J.H.7
  • 69
    • 46749096032 scopus 로고    scopus 로고
    • Detailed assignment of the magnetic circular dichroism and UV-vis spectra of five-coordinate high-spin ferric [Fe(TPP)(Cl)]
    • Paulat, F. and Lehnert, N. (2008) Detailed assignment of the magnetic circular dichroism and UV-vis spectra of five-coordinate high-spin ferric [Fe(TPP)(Cl)] Inorg. Chem. 47, 4963-4976
    • (2008) Inorg. Chem. , vol.47 , pp. 4963-4976
    • Paulat, F.1    Lehnert, N.2
  • 70
    • 0037397638 scopus 로고    scopus 로고
    • Recent applications of MCD spectroscopy to metalloenzymes
    • Kirk, M. L. and Peariso, K. (2003) Recent applications of MCD spectroscopy to metalloenzymes Curr. Opin. Chem. Biol. 7, 220-227
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 220-227
    • Kirk, M.L.1    Peariso, K.2
  • 71
    • 0033464509 scopus 로고    scopus 로고
    • Magnetic spectroscopic (EPR, ESEEM, Mossbauer, MCD and NMR) studies of low-spin ferriheme centers and their corresponding heme proteins
    • Walker, F. A. (1999) Magnetic spectroscopic (EPR, ESEEM, Mossbauer, MCD and NMR) studies of low-spin ferriheme centers and their corresponding heme proteins Coord. Chem. Rev. 185-186, 471-534
    • (1999) Coord. Chem. Rev. , vol.185-186 , pp. 471-534
    • Walker, F.A.1
  • 72
    • 78049428463 scopus 로고    scopus 로고
    • Magnetic circular dichroism spectroscopy as a probe of the structures of the metal sites in metalloproteins
    • McMaster, J. and Oganesyan, V. S. (2010) Magnetic circular dichroism spectroscopy as a probe of the structures of the metal sites in metalloproteins Curr. Opin. Struct. Biol. 20, 615-622
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 615-622
    • McMaster, J.1    Oganesyan, V.S.2
  • 74
    • 0001122336 scopus 로고    scopus 로고
    • Magnetic circular dichroism spectroscopy of heme proteins and model systems
    • (Kadish, K. M. Smith, K. M. and Guilard, R. Eds.) Academic Press, San Diego.
    • Cheek, J. and Dawson, J. H. (2000) Magnetic circular dichroism spectroscopy of heme proteins and model systems. In Porphyrin Handbook (Kadish, K. M., Smith, K. M., and Guilard, R., Eds.) pp 339-369, Academic Press, San Diego.
    • (2000) Porphyrin Handbook , pp. 339-369
    • Cheek, J.1    Dawson, J.H.2
  • 75
    • 0001680832 scopus 로고    scopus 로고
    • CD and MCD Spectroscopy
    • (Que, L. Jr. Ed.) pp, University Science Books, Sausalito, CA.
    • Johnson, M. K. (2000) CD and MCD Spectroscopy. In Physical methods in bioinorganic chemistry (Que, L., Jr., Ed.) pp 233-286, University Science Books, Sausalito, CA.
    • (2000) Physical Methods in Bioinorganic Chemistry , pp. 233-286
    • Johnson, M.K.1
  • 76
    • 0017312372 scopus 로고
    • Magnetic circular dichroism studies of low-spin cytochromes. Temperature dependence and effects of axial coordination on the spectra of cytochrome c and cytochrome b5
    • Vickery, L., Nozawa, T., and Sauer, K. (1976) Magnetic circular dichroism studies of low-spin cytochromes. Temperature dependence and effects of axial coordination on the spectra of cytochrome c and cytochrome b5 J. Am. Chem. Soc. 98, 351-357
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 351-357
    • Vickery, L.1    Nozawa, T.2    Sauer, K.3
  • 77
    • 0017312344 scopus 로고
    • Magnetic circular dichroism studies of myoglobin complexes. Correlations with heme spin state and axial ligation
    • Vickery, L., Nozawa, T., and Sauer, K. (1976) Magnetic circular dichroism studies of myoglobin complexes. Correlations with heme spin state and axial ligation J. Am. Chem. Soc. 98, 343-350
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 343-350
    • Vickery, L.1    Nozawa, T.2    Sauer, K.3
  • 78
    • 79952101620 scopus 로고    scopus 로고
    • The H93G myoglobin cavity mutant as a versatile scaffold for modeling heme iron coordination structures in protein active sites and their characterization with magnetic circular dichroism spectroscopy
    • Du, J., Sono, M., and Dawson, J. H. (2011) The H93G myoglobin cavity mutant as a versatile scaffold for modeling heme iron coordination structures in protein active sites and their characterization with magnetic circular dichroism spectroscopy Coord. Chem. Rev. 255, 700-716
    • (2011) Coord. Chem. Rev. , vol.255 , pp. 700-716
    • Du, J.1    Sono, M.2    Dawson, J.H.3
  • 79
    • 79951619428 scopus 로고    scopus 로고
    • Alkylamine-Ligated H93G Myoglobin Cavity Mutant: A Model System for Endogenous Lysine and Terminal Amine Ligation in Heme Proteins such as Nitrite Reductase and Cytochrome f
    • Du, J., Perera, R., and Dawson, J. H. (2011) Alkylamine-Ligated H93G Myoglobin Cavity Mutant: A Model System for Endogenous Lysine and Terminal Amine Ligation in Heme Proteins such as Nitrite Reductase and Cytochrome f Inorg. Chem. 50, 1242-1249
    • (2011) Inorg. Chem. , vol.50 , pp. 1242-1249
    • Du, J.1    Perera, R.2    Dawson, J.H.3
  • 80
    • 9644268836 scopus 로고    scopus 로고
    • The heme iron coordination of unfolded ferric and ferrous cytochrome c in neutral and acidic urea solutions. Spectroscopic and electrochemical studies
    • Fedurco, M., Augustynski, J., Indiani, C., Smulevich, G., Antalik, M., Bano, M., Sedlak, E., Glascocke, M. C., and Dawson, J. H. (2004) The heme iron coordination of unfolded ferric and ferrous cytochrome c in neutral and acidic urea solutions. Spectroscopic and electrochemical studies Biochim. Biophys. Acta 1703, 31-41
    • (2004) Biochim. Biophys. Acta , vol.1703 , pp. 31-41
    • Fedurco, M.1    Augustynski, J.2    Indiani, C.3    Smulevich, G.4    Antalik, M.5    Bano, M.6    Sedlak, E.7    Glascocke, M.C.8    Dawson, J.H.9
  • 83
    • 0036290597 scopus 로고    scopus 로고
    • H93G myoglobin cavity mutant as versatile template for modeling heme proteins: Magnetic circular dichroism studies of thiolate- and imidazole-ligated complexes
    • Dawson, J. H., Pond, A. E., and Roach, M. P. (2002) H93G myoglobin cavity mutant as versatile template for modeling heme proteins: Magnetic circular dichroism studies of thiolate- and imidazole-ligated complexes Biopolymers 67, 200-206
    • (2002) Biopolymers , vol.67 , pp. 200-206
    • Dawson, J.H.1    Pond, A.E.2    Roach, M.P.3
  • 84
    • 0034716177 scopus 로고    scopus 로고
    • The H93G myoglobin cavity mutant as a versatile template for modeling heme proteins: Ferrous, ferric, and ferryl mixed-ligand complexes with imidazole in the cavity
    • Pond, A. E., Roach, M. P., Thomas, M. R., Boxer, S. G., and Dawson, J. H. (2000) The H93G myoglobin cavity mutant as a versatile template for modeling heme proteins: Ferrous, ferric, and ferryl mixed-ligand complexes with imidazole in the cavity Inorg. Chem. 39, 6061-6066
    • (2000) Inorg. Chem. , vol.39 , pp. 6061-6066
    • Pond, A.E.1    Roach, M.P.2    Thomas, M.R.3    Boxer, S.G.4    Dawson, J.H.5
  • 85
    • 0032613196 scopus 로고    scopus 로고
    • Influence of protein environment on magnetic circular dichroism spectral properties of ferric and ferrous ligand complexes of yeast cytochrome c peroxidase
    • Pond, A. E., Sono, M., Elenkova, E. A., Goodin, D. B., English, A. M., and Dawson, J. H. (1999) Influence of protein environment on magnetic circular dichroism spectral properties of ferric and ferrous ligand complexes of yeast cytochrome c peroxidase Biospectroscopy 5, S42-S52
    • (1999) Biospectroscopy , vol.5
    • Pond, A.E.1    Sono, M.2    Elenkova, E.A.3    Goodin, D.B.4    English, A.M.5    Dawson, J.H.6
  • 87
    • 0026589565 scopus 로고
    • On the use of iron octa-alkylporphyrins as models for protoporphyrin IX-containing heme systems in studies employing magnetic circular dichroism spectroscopy
    • Dawson, J. H., Kadkhodayan, S., Zhuang, C., and Sono, M. (1992) On the use of iron octa-alkylporphyrins as models for protoporphyrin IX-containing heme systems in studies employing magnetic circular dichroism spectroscopy J. Inorg. Biochem. 45, 179-192
    • (1992) J. Inorg. Biochem. , vol.45 , pp. 179-192
    • Dawson, J.H.1    Kadkhodayan, S.2    Zhuang, C.3    Sono, M.4
  • 88
    • 0001597141 scopus 로고
    • Spectroscopic studies of ferric porphyrins with quantum mechanically admixed intermediate-spin states: Models for cytochrome c′
    • Kintnert, E. T. and Dawson, J. H. (1991) Spectroscopic studies of ferric porphyrins with quantum mechanically admixed intermediate-spin states: Models for cytochrome c′ Inorg. Chem. 30, 4892-4897
    • (1991) Inorg. Chem. , vol.30 , pp. 4892-4897
    • Kintnert, E.T.1    Dawson, J.H.2
  • 89
    • 0025894901 scopus 로고
    • Magnetic circular dichroism spectroscopy as a probe for axial heme ligand replacement in semisynthetic mutants of cytochrome c
    • Rux, J. J. and Dawson, J. H. (1991) Magnetic circular dichroism spectroscopy as a probe for axial heme ligand replacement in semisynthetic mutants of cytochrome c FEBS Lett. 290, 49-51
    • (1991) FEBS Lett. , vol.290 , pp. 49-51
    • Rux, J.J.1    Dawson, J.H.2
  • 92
    • 70449234614 scopus 로고
    • Spectrum of horse-heart cytochrome c
    • Margoliash, E. and Frohwirt, N. (1959) Spectrum of horse-heart cytochrome c Biochem. J. 71, 570-572
    • (1959) Biochem. J. , vol.71 , pp. 570-572
    • Margoliash, E.1    Frohwirt, N.2
  • 93
    • 12044252759 scopus 로고
    • Structurally engineered cytochromes with novel ligand binding sites: Oxy and carbon monoxy derivatives of semisynthetic horse heart Ala80 cytochrome c
    • Bren, K. L. and Gray, H. B. (1993) Structurally engineered cytochromes with novel ligand binding sites: Oxy and carbon monoxy derivatives of semisynthetic horse heart Ala80 cytochrome c J. Am. Chem. Soc. 115, 10382-10383
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 10382-10383
    • Bren, K.L.1    Gray, H.B.2
  • 94
    • 36849110609 scopus 로고
    • Magnetic Circular Dichroism of Cytochrome c
    • Sutherland, J. C. and Klein, M. P. (1972) Magnetic Circular Dichroism of Cytochrome c J. Chem. Phys. 57, 76-86
    • (1972) J. Chem. Phys. , vol.57 , pp. 76-86
    • Sutherland, J.C.1    Klein, M.P.2
  • 96
    • 0029310668 scopus 로고
    • PH-dependent equilibria of yeast Met80Ala-iso-l cytochrome c probed by NMR spectroscopy: A comparison with the wild-type protein
    • Banci, L., Bertini, I., Bren, K., Gray, H. B., and Turano, P. (1995) pH-dependent equilibria of yeast Met80Ala-iso-l cytochrome c probed by NMR spectroscopy: A comparison with the wild-type protein Chem. Biol. 2, 377-383
    • (1995) Chem. Biol. , vol.2 , pp. 377-383
    • Banci, L.1    Bertini, I.2    Bren, K.3    Gray, H.B.4    Turano, P.5
  • 98
    • 0033566245 scopus 로고    scopus 로고
    • Hemepeptide models for hemoproteins: The behavior of N- acetylmicroperoxidase-11 in aqueous solution
    • Marques, H. M. and Perry, C. B. (1999) Hemepeptide models for hemoproteins: The behavior of N-acetylmicroperoxidase-11 in aqueous solution J. Inorg. Biochem. 75, 28l-291
    • (1999) J. Inorg. Biochem. , vol.75
    • Marques, H.M.1    Perry, C.B.2
  • 99
    • 0032545334 scopus 로고    scopus 로고
    • Histidine-tailed microperoxidase-10: A pH-dependent ligand switch
    • Cheek, J., Low, D. W., Gray, H. B., and Dawson, J. H. (1998) Histidine-tailed microperoxidase-10: A pH-dependent ligand switch Biochem. Biophys. Res. Commun. 253, 195-198
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 195-198
    • Cheek, J.1    Low, D.W.2    Gray, H.B.3    Dawson, J.H.4
  • 101
    • 0017137394 scopus 로고
    • Study of the biological significance of cytochrome methylation I. Thermal, acid and guanidinium hydrochloride denaturations of baker's yeast ferricytochromes c
    • Polastro, E., Looze, Y., and Léonis, J. (1976) Study of the biological significance of cytochrome methylation I. Thermal, acid and guanidinium hydrochloride denaturations of baker's yeast ferricytochromes c Biochim. Biophys. Acta 446, 310-320
    • (1976) Biochim. Biophys. Acta , vol.446 , pp. 310-320
    • Polastro, E.1    Looze, Y.2    Léonis, J.3
  • 102
    • 0027935843 scopus 로고
    • Stability of yeast iso-1 ferricytochrome c as a function of pH and temperature
    • Cohen, D. S. and Pielak, G. J. (1994) Stability of yeast iso-1 ferricytochrome c as a function of pH and temperature Protein Sci. 3, 1253-1260
    • (1994) Protein Sci. , vol.3 , pp. 1253-1260
    • Cohen, D.S.1    Pielak, G.J.2
  • 103
    • 0022402737 scopus 로고
    • Probing stability and dynamics of proteins by protease digestion. I: Comparison of protease susceptibility and thermal stability of cytochromes c
    • Endo, S., Nagayama, K., and Wada, A. (1985) Probing stability and dynamics of proteins by protease digestion. I: Comparison of protease susceptibility and thermal stability of cytochromes c J. Biomol. Struct. Dyn. 3, 409-421
    • (1985) J. Biomol. Struct. Dyn. , vol.3 , pp. 409-421
    • Endo, S.1    Nagayama, K.2    Wada, A.3
  • 104
    • 0028349676 scopus 로고
    • The significance of denaturant titrations of protein stability: A comparison of rat and baker's yeast cytochrome c and their site-directed asparagine-52-to-isoleucine mutants
    • Koshy, T. I., Luntz, T. L., Plotkin, B., Schejter, A., and Margoliash, E. (1994) The significance of denaturant titrations of protein stability: A comparison of rat and baker's yeast cytochrome c and their site-directed asparagine-52-to-isoleucine mutants Biochem. J. 299, 347-350
    • (1994) Biochem. J. , vol.299 , pp. 347-350
    • Koshy, T.I.1    Luntz, T.L.2    Plotkin, B.3    Schejter, A.4    Margoliash, E.5
  • 106
    • 0014690725 scopus 로고
    • Physicochemical properties of baker's yeast iso-1-cytochrome c
    • Aviram, I. and Schejter, A. (1969) Physicochemical properties of baker's yeast iso-1-cytochrome c J. Biol. Chem. 244, 3773-3778
    • (1969) J. Biol. Chem. , vol.244 , pp. 3773-3778
    • Aviram, I.1    Schejter, A.2
  • 107
    • 0027142050 scopus 로고
    • Structurally expressed cytochromes with novel ligand binding properties: Expression of Saccharomyces cerevisiae Met-80 → Ala iso-1-cytochrome c
    • Lu, Y., Casimiro, D. R., Bren, K. L., Richards, J. H., and Gray, H. B. (1993) Structurally expressed cytochromes with novel ligand binding properties: Expression of Saccharomyces cerevisiae Met-80 → Ala iso-1-cytochrome c Proc. Natl. Acad. Sci. U.S.A. 90, 11456-11459
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 11456-11459
    • Lu, Y.1    Casimiro, D.R.2    Bren, K.L.3    Richards, J.H.4    Gray, H.B.5
  • 108
    • 0032508940 scopus 로고    scopus 로고
    • Alkaline Conformational Transitions of Ferricytochrome c Studied by Resonance Raman Spectroscopy
    • Döpner, S., Hildebrandt, P., Rosell, F. I., and Mauk, A. G. (1998) Alkaline Conformational Transitions of Ferricytochrome c Studied by Resonance Raman Spectroscopy J. Am. Chem. Soc. 120, 11246-11255
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11246-11255
    • Döpner, S.1    Hildebrandt, P.2    Rosell, F.I.3    Mauk, A.G.4
  • 109
    • 0029115741 scopus 로고
    • Three-dimensional solution structure of the cyanide adduct of a Met80Ala variant of Saccharomyces cerevisiae iso-1-cytochrome c. Identification of ligand-residue interactions in the distal heme cavity
    • Banci, L., Bertini, I., Bren, K. L., Gray, H. B., Sompornpisut, P., and Turano, P. (1995) Three-dimensional solution structure of the cyanide adduct of a Met80Ala variant of Saccharomyces cerevisiae iso-1-cytochrome c. Identification of ligand-residue interactions in the distal heme cavity Biochemistry 34, 11385-11398
    • (1995) Biochemistry , vol.34 , pp. 11385-11398
    • Banci, L.1    Bertini, I.2    Bren, K.L.3    Gray, H.B.4    Sompornpisut, P.5    Turano, P.6
  • 110
    • 0013660457 scopus 로고    scopus 로고
    • Nuclear Magnetic Resonance Studies of Class i Cytochromes c
    • (Scott, R. A. and Mauk, A. G. Eds.) University Science Books, Sausalito, CA.
    • Pielak, G. J., Auld, D. S., Betz, S. F., Hilgen-Willis, S. E., and Garcia, L. L. (1996) Nuclear Magnetic Resonance Studies of Class I Cytochromes c. In Cytochrome c: A multidisciplinary approach (Scott, R. A. and Mauk, A. G., Eds.) pp 203-284, University Science Books, Sausalito, CA.
    • (1996) Cytochrome C: A Multidisciplinary Approach , pp. 203-284
    • Pielak, G.J.1    Auld, D.S.2    Betz, S.F.3    Hilgen-Willis, S.E.4    Garcia, L.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.