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Volumn 40, Issue 3, 2011, Pages 259-271

The non-native conformations of cytochrome c in sodium dodecyl sulfate and their modulation by ATP

Author keywords

ATP; Cytochrome c; Docking; GTP; Non native conformation; Sodium dodecyl sulfate

Indexed keywords

EQUIDAE;

EID: 79958721281     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-010-0643-6     Document Type: Article
Times cited : (13)

References (51)
  • 1
    • 0029240825 scopus 로고
    • Effect of nucleotides on thermal stability of ferricytochrome C
    • Antalik M, Bagel'ova J (1995) Effect of nucleotides on thermal stability of ferricytochrome C. Gen Physiol Biophys 14:19-37
    • (1995) Gen Physiol Biophys , vol.14 , pp. 19-37
    • Antalik, M.1    Bagel'Ova, J.2
  • 2
    • 0015154226 scopus 로고
    • The existence of heme-protein coordinate-covalent bonds in denaturing solvents
    • Babul J, Stellwagen E (1971) The existence of heme-protein coordinate-covalent bonds in denaturing solvents. Biopolymers 10:2359-2361
    • (1971) Biopolymers , vol.10 , pp. 2359-2361
    • Babul, J.1    Stellwagen, E.2
  • 3
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai Y, Sosnick TR, Mayne L, Englander SW (1995) Protein folding intermediates: native-state hydrogen exchange. Science 269:192-197
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 5
    • 73649087584 scopus 로고    scopus 로고
    • On the mechanism of SDS-induced protein denaturation
    • Bhuyan AK (2010) On the mechanism of SDS-induced protein denaturation. Biopolymers 93:186-199
    • (2010) Biopolymers , vol.93 , pp. 186-199
    • Bhuyan, A.K.1
  • 6
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart cytochrome c
    • DOI 10.1016/0022-2836(90)90200-6
    • Bushnell GW, Louie GV, Brayer GD (1990) High-resolution three-dimensional structure of horse heart cytochrome c. J Mol Biol 214:585-595 (Pubitemid 20261984)
    • (1990) Journal of Molecular Biology , vol.214 , Issue.2 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3
  • 7
    • 0346850580 scopus 로고    scopus 로고
    • Stabilization of Partially Folded States of Cytochrome C in Aqueous Surfactant: Effects of Ionic and Hydrophobic Interactions
    • DOI 10.1021/bi0351662
    • Chattopadhyay K, Mazumdar S (2003) Stabilization of partially folded states of cytochrome c in aqueous surfactant: effects of ionic and hydrophobic interactions. Biochemistry 42:14606-14613 (Pubitemid 37532007)
    • (2003) Biochemistry , vol.42 , Issue.49 , pp. 14606-14613
    • Chattopadhyay, K.1    Mazumdar, S.2
  • 8
    • 43249087866 scopus 로고    scopus 로고
    • The folding kinetics of the SDS-induced molten globule form of reduced cytochrome c
    • DOI 10.1021/bi702452u
    • Chen E, Van Vranken V, Kliger DS (2008) The folding kinetics of the SDS-induced molten globule form of reduced cytochrome c. Biochemistry 47:5450-5459 (Pubitemid 351656989)
    • (2008) Biochemistry , vol.47 , Issue.19 , pp. 5450-5459
    • Chen, E.1    Van Vranken, V.2    Kliger, D.S.3
  • 9
    • 0030816577 scopus 로고    scopus 로고
    • Identification of the predominant non-native histidine ligand in unfolded cytochrome c
    • DOI 10.1021/bi971697c
    • Colon W, Wakem LP, Sherman F, Roder H (1997) Identification of the predominant non-native histidine ligand in unfolded cytochrome c. Biochemistry 36:12535-12541 (Pubitemid 27446677)
    • (1997) Biochemistry , vol.36 , Issue.41 , pp. 12535-12541
    • Colon, W.1    Wakem, L.P.2    Sherman, F.3    Roder, H.4
  • 10
    • 0032485854 scopus 로고    scopus 로고
    • Multiple conformations of physiological membrane-bound cytochrome c
    • DOI 10.1021/bi9730543
    • Cortese JD, Voglino AL, Hackenbrock CR (1998) Multiple conformations of physiological membrane-bound cytochrome c. Biochemistry 37:6402-6409 (Pubitemid 28213660)
    • (1998) Biochemistry , vol.37 , Issue.18 , pp. 6402-6409
    • Cortese, J.D.1    Voglino, A.L.2    Hackenbrock, C.R.3
  • 11
    • 0026005243 scopus 로고
    • The specificity and Kd at physiological ionic strength of an ATP-binding site on cytochrome c suit it to a regulatory role
    • Craig DB, Wallace CJ (1991) The specificity and Kd at physiological ionic strength of an ATP-binding site on cytochrome c suit it to a regulatory role. Biochem J 279(Pt 3):781-786
    • (1991) Biochem J , vol.279 , Issue.PART 3 , pp. 781-786
    • Craig, D.B.1    Wallace, C.J.2
  • 12
    • 0032525842 scopus 로고    scopus 로고
    • Characterization of a partially unfolded structure of cytochrome c induced by sodium dodecyl sulphate and the kinetics of its refolding
    • Das TK, Mazumdar S, Mitra S (1998) Characterization of a partially unfolded structure of cytochrome c induced by sodium dodecyl sulphate and the kinetics of its refolding. Eur J Biochem 254:662-670 (Pubitemid 28308120)
    • (1998) European Journal of Biochemistry , vol.254 , Issue.3 , pp. 662-670
    • Das, T.K.1    Mazumdar, S.2    Mitra, S.3
  • 17
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC (1998) Mitochondria and apoptosis. Science 281:1309-1312 (Pubitemid 28406816)
    • (1998) Science , vol.281 , Issue.5381 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 18
    • 0027433511 scopus 로고
    • Intermediate conformational states of apocytochrome c
    • DOI 10.1021/bi00090a010
    • Hamada D, Hoshino M, Kataoka M, Fink AL, Goto Y (1993) Intermediate conformational states of apocytochrome c. Biochemistry 32:10351-10358 (Pubitemid 23320158)
    • (1993) Biochemistry , vol.32 , Issue.39 , pp. 10351-10358
    • Hamada, D.1    Hoshino, M.2    Kataoka, M.3    Fink, A.L.4    Goto, Y.5
  • 19
    • 0033596909 scopus 로고    scopus 로고
    • A conformational change in cytochrome c of apoptotic and necrotic cells is detected by monoclonal antibody binding and mimicked by association of the native antigen with synthetic phospholipid vesicles
    • Jemmerson R, Liu J, Hausauer D, Lam KP, Mondino A, Nelson RD (1999) A conformational change in cytochrome c of apoptotic and necrotic cells is detected by monoclonal antibody binding and mimicked by association of the native antigen with synthetic phospholipid vesicles. Biochemistry 38:3599-3609
    • (1999) Biochemistry , vol.38 , pp. 3599-3609
    • Jemmerson, R.1    Liu, J.2    Hausauer, D.3    Lam, K.P.4    Mondino, A.5    Nelson, R.D.6
  • 20
    • 0025203243 scopus 로고
    • Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR
    • Jeng MF, Englander SW, Elove GA, Wand AJ, Roder H (1990) Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR. Biochemistry 29:10433-10437
    • (1990) Biochemistry , vol.29 , pp. 10433-10437
    • Jeng, M.F.1    Englander, S.W.2    Elove, G.A.3    Wand, A.J.4    Roder, H.5
  • 21
    • 0028953092 scopus 로고
    • Secondary and tertiary structure of the A-state of cytochrome c from resonance Raman spectroscopy
    • Jordan T, Eads JC, Spiro TG (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
  • 23
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X (1997) Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91:479-489 (Pubitemid 27508237)
    • (1997) Cell , vol.91 , Issue.4 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 24
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • DOI 10.1016/S0092-8674(00)80085-9
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86:147-157 (Pubitemid 26256586)
    • (1996) Cell , vol.86 , Issue.1 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 27
    • 33645673663 scopus 로고    scopus 로고
    • A unique molten globule state occurs during unfolding of cytochrome c by LiClO4 near physiological pH and temperature: Structural and thermodynamic characterization
    • Moza B, Qureshi SH, Islam A, Singh R, Anjum F, Moosavi-Movahedi AA, Ahmad F (2006) A unique molten globule state occurs during unfolding of cytochrome c by LiClO4 near physiological pH and temperature: structural and thermodynamic characterization. Biochemistry 45:4695-4702
    • (2006) Biochemistry , vol.45 , pp. 4695-4702
    • Moza, B.1    Qureshi, S.H.2    Islam, A.3    Singh, R.4    Anjum, F.5    Moosavi-Movahedi, A.A.6    Ahmad, F.7
  • 28
    • 0014426245 scopus 로고
    • Far ultraviolet circular dichroism spectra of cytochrome c
    • Myer YP (1968) Far ultraviolet circular dichroism spectra of cytochrome c. Biochim Biophys Acta 154:84-90
    • (1968) Biochim Biophys Acta , vol.154 , pp. 84-90
    • Myer, Y.P.1
  • 29
    • 0037183064 scopus 로고    scopus 로고
    • Spectroscopic characterization of nonnative conformational states of cytochrome c
    • DOI 10.1021/jp013841g
    • Oellerich S, Wackerbarth H, Hildebrandt P (2002) Spectroscopic characterization of nonnative conformational states of cytochrome c. J Phys Chem B 106:6566-6580 (Pubitemid 35289249)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.25 , pp. 6566-6580
    • Oellerich, S.1    Wackerbarth, H.2    Hildebrandt, P.3
  • 30
    • 0242526967 scopus 로고    scopus 로고
    • Conformational equilibria and dynamics of cytochrome c induced by binding of sodium dodecyl sulfate monomers and micelles
    • DOI 10.1007/s00249-003-0306-y
    • Oellerich S, Wackerbarth H, Hildebrandt P (2003) Conformational equilibria and dynamics of cytochrome c induced by binding of sodium dodecyl sulfate monomers and micelles. Eur Biophys J 32:599-613 (Pubitemid 37413244)
    • (2003) European Biophysics Journal , vol.32 , Issue.7 , pp. 599-613
    • Oellerich, S.1    Wackerbarth, H.2    Hildebrandt, P.3
  • 32
    • 0028260185 scopus 로고
    • 31P NMR
    • Pinheiro TJ, Watts A (1994) Lipid specificity in the interaction of cytochrome c with anionic phospholipid bilayers revealed by solid-state 31P NMR. Biochemistry 33:2451-2458 (Pubitemid 24099650)
    • (1994) Biochemistry , vol.33 , Issue.9 , pp. 2451-2458
    • Pinheiro, T.J.T.1    Watts, A.2
  • 33
    • 17044441821 scopus 로고    scopus 로고
    • Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles
    • DOI 10.1021/bi971235z
    • Pinheiro TJ, Elove GA, Watts A, Roder H (1997) Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles. Biochemistry 36:13122-13132 (Pubitemid 27465428)
    • (1997) Biochemistry , vol.36 , Issue.42 , pp. 13122-13132
    • Pinheiro, T.J.T.1    Elove, G.A.2    Watts, A.3    Roder, H.4
  • 34
    • 0028057721 scopus 로고
    • Evidence for two distinct acidic phospholipid-binding sites in cytochrome c
    • Rytomaa M, Kinnunen PK (1994) Evidence for two distinct acidic phospholipid-binding sites in cytochrome c. J Biol Chem 269:1770-1774 (Pubitemid 24035373)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.3 , pp. 1770-1774
    • Rytomaa, M.1    Kinnunen, P.K.J.2
  • 35
    • 0028836142 scopus 로고
    • Reversibility of the binding of cytochrome c to liposomes. Implications for lipid-protein interactions
    • Rytomaa M, Kinnunen PK (1995) Reversibility of the binding of cytochrome c to liposomes. Implications for lipid-protein interactions. J Biol Chem 270:3197-3202
    • (1995) J Biol Chem , vol.270 , pp. 3197-3202
    • Rytomaa, M.1    Kinnunen, P.K.2
  • 36
    • 77956178182 scopus 로고    scopus 로고
    • Relationship between the wavelength maximum of a protein and the temperature dependence of its intrinsic tryptophan fluorescence intensity
    • Saini K, Deep S (2010) Relationship between the wavelength maximum of a protein and the temperature dependence of its intrinsic tryptophan fluorescence intensity. Eur Biophys J 39:1445-1451
    • (2010) Eur Biophys J , vol.39 , pp. 1445-1451
    • Saini, K.1    Deep, S.2
  • 37
    • 0033946882 scopus 로고    scopus 로고
    • Unfolding and refolding of cytochrome c driven by the interaction with lipid micelles
    • Sanghera N, Pinheiro TJ (2000) Unfolding and refolding of cytochrome c driven by the interaction with lipid micelles. Protein Sci 9:1194-1202 (Pubitemid 30419153)
    • (2000) Protein Science , vol.9 , Issue.6 , pp. 1194-1202
    • Sanghera, N.1    Pinheiro, T.J.T.2
  • 38
    • 0032851381 scopus 로고    scopus 로고
    • Molten globule-like state of cytochrome c induced by polyanion poly(vinylsulfate) in slightly acidic pH
    • DOI 10.1016/S0167-4838(99)00186-7, PII S0167483899001867
    • Sedlak E, Antalik M (1999) Molten globule-like state of cytochrome c induced by polyanion poly(vinylsulfate) in slightly acidic pH. Biochim Biophys Acta 1434:347-355 (Pubitemid 29486756)
    • (1999) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1434 , Issue.2 , pp. 347-355
    • Sedlak, E.1    Antalik, M.2
  • 39
    • 0037732539 scopus 로고    scopus 로고
    • Rupture of the hydrogen bond linking two Omega-loops induces the molten globule state at neutral pH in cytochrome c
    • DOI 10.1021/bi034132r
    • Sinibaldi F, Piro MC, Howes BD, Smulevich G, Ascoli F, Santucci R (2003) Rupture of the hydrogen bond linking two Omega-loops induces the molten globule state at neutral pH in cytochrome c. Biochemistry 42:7604-7610 (Pubitemid 36735838)
    • (2003) Biochemistry , vol.42 , Issue.24 , pp. 7604-7610
    • Sinibaldi, F.1    Piro, M.C.2    Howes, B.D.3    Smulevich, G.4    Ascoli, F.5    Santucci, R.6
  • 43
    • 0025910862 scopus 로고
    • Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements
    • Spooner PJ, Watts A (1991a) Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements. Biochemistry 30:3871-3879
    • (1991) Biochemistry , vol.30 , pp. 3871-3879
    • Spooner, P.J.1    Watts, A.2
  • 44
    • 0025761403 scopus 로고
    • Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. Evidence from phosphorus-31 NMR measurements
    • Spooner PJ, Watts A (1991b) Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. Evidence from phosphorus-31 NMR measurements. Biochemistry 30:3880-3885
    • (1991) Biochemistry , vol.30 , pp. 3880-3885
    • Spooner, P.J.1    Watts, A.2
  • 45
    • 0026806379 scopus 로고
    • Cytochrome c interactions with cardiolipin in bilayers: A multinuclear magic-angle spinning NMR study
    • Spooner PJ, Watts A (1992) Cytochrome c interactions with cardiolipin in bilayers: a multinuclear magic-angle spinning NMR study. Biochemistry 31:10129-10138
    • (1992) Biochemistry , vol.31 , pp. 10129-10138
    • Spooner, P.J.1    Watts, A.2
  • 46
    • 0016769984 scopus 로고
    • An acid induced conformational transition of denatured cytochrome c in urea and guanidine hydrochloride solutions
    • Tsong TY (1975) An acid induced conformational transition of denatured cytochrome c in urea and guanidine hydrochloride solutions. Biochemistry 14:1542-1547
    • (1975) Biochemistry , vol.14 , pp. 1542-1547
    • Tsong, T.Y.1
  • 47
    • 33947301164 scopus 로고    scopus 로고
    • Micellization behaviour of sodium dodecyl sulfate in different electrolyte media
    • DOI 10.1016/j.colsurfa.2006.11.010, PII S0927775706008521
    • Umlong IM, Ismail K (2007) Micellization behaviour of sodium dodecyl sulfate in different electrolyte media. Colloids Surf A Physicochem Eng Asp 299:8-14 (Pubitemid 46441813)
    • (2007) Colloids and Surfaces A: Physicochemical and Engineering Aspects , vol.299 , Issue.1-3 , pp. 8-14
    • Umlong, I.M.1    Ismail, K.2
  • 48
    • 0022539256 scopus 로고
    • Interaction of Ferricytochrome-C with Cardiolipin Multilayers - A Resonance Raman-Study
    • Vincent JS, Levin IW (1986) Interaction of Ferricytochrome-C with Cardiolipin Multilayers - a Resonance Raman-Study. J Am Chem Soc 108:3551-3554
    • (1986) J Am Chem Soc , vol.108 , pp. 3551-3554
    • Vincent, J.S.1    Levin, I.W.2
  • 49
    • 0023277044 scopus 로고
    • Low-temperature electron paramagnetic resonance study of the ferricytochrome c-cardiolipin complex
    • DOI 10.1021/bi00382a036
    • Vincent JS, Kon H, Levin IW (1987) Low-temperature electron paramagnetic resonance study of the ferricytochrome c-cardiolipin complex. Biochemistry 26:2312-2314 (Pubitemid 17080976)
    • (1987) Biochemistry , vol.26 , Issue.8 , pp. 2312-2314
    • Vincent, J.S.1    Kon, H.2    Levin, I.W.3
  • 50
    • 7244225173 scopus 로고    scopus 로고
    • Effect of sodium dodecyl sulfate on folding and thermal stability of acid-denatured cytochrome c: A spectroscopic approach
    • DOI 10.1110/ps.04827604
    • Xu Q, Keiderling TA (2004) Effect of sodium dodecyl sulfate on folding and thermal stability of acid-denatured cytochrome c: a spectroscopic approach. Protein Sci 13:2949-2959 (Pubitemid 39431257)
    • (2004) Protein Science , vol.13 , Issue.11 , pp. 2949-2959
    • Xu, Q.1    Keiderling, T.A.2
  • 51
    • 33646071241 scopus 로고    scopus 로고
    • Stop-flow kinetics studies of the interaction of surfactant, sodium dodecyl sulfate, with acid-denatured cytochrome c
    • Xu Q, Keiderling TA (2006) Stop-flow kinetics studies of the interaction of surfactant, sodium dodecyl sulfate, with acid-denatured cytochrome c. Proteins 63:571-580
    • (2006) Proteins , vol.63 , pp. 571-580
    • Xu, Q.1    Keiderling, T.A.2


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