메뉴 건너뛰기




Volumn 117, Issue 42, 2013, Pages 12878-12886

Becoming a peroxidase: Cardiolipin-induced unfolding of cytochrome c

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOCHEMISTRY; CELL DEATH; LIPID BILAYERS; LIPOSOMES; PHOSPHOLIPIDS;

EID: 84886703951     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp402104r     Document Type: Article
Times cited : (60)

References (59)
  • 1
    • 1842531459 scopus 로고    scopus 로고
    • Cytochrome c Folding Dynamics
    • Winkler, J. R. Cytochrome c Folding Dynamics Curr. Opin. Chem. Biol. 2004, 8, 169-174
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 169-174
    • Winkler, J.R.1
  • 3
    • 0030584652 scopus 로고    scopus 로고
    • Protein Folding Triggered by Electron Transfer
    • Pascher, T.; Chesick, J. P.; Winkler, J. R.; Gray, H. B. Protein Folding Triggered by Electron Transfer Science 1996, 271, 1558-1560
    • (1996) Science , vol.271 , pp. 1558-1560
    • Pascher, T.1    Chesick, J.P.2    Winkler, J.R.3    Gray, H.B.4
  • 4
    • 45249112520 scopus 로고    scopus 로고
    • Probing the Bottom of a Folding Funnel Using Conformationally Gated Electron Transfer Reactions
    • Bandi, S.; Bowler, B. E. Probing the Bottom of a Folding Funnel Using Conformationally Gated Electron Transfer Reactions J. Am. Chem. Soc. 2008, 130, 7540-7541
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 7540-7541
    • Bandi, S.1    Bowler, B.E.2
  • 10
    • 0031919973 scopus 로고    scopus 로고
    • Evidence for Barrier-Limited Protein-Folding Kinetics on the Microsecond Time-Scale
    • Shastry, M. C. R.; Roder, H. Evidence for Barrier-Limited Protein-Folding Kinetics on the Microsecond Time-Scale Nat. Struct. Biol. 1998, 5, 385-392
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 385-392
    • Shastry, M.C.R.1    Roder, H.2
  • 11
    • 70349492136 scopus 로고    scopus 로고
    • Probing Early Events in Ferrous Cytochrome c Folding with Time-Resolved Natural and Magnetic Circular Dichroism Spectroscopies
    • Chen, E.; Goldbeck, R. A.; Kliger, D. S. Probing Early Events in Ferrous Cytochrome c Folding with Time-Resolved Natural and Magnetic Circular Dichroism Spectroscopies Curr. Protein Pept. Sci. 2009, 10, 464-475
    • (2009) Curr. Protein Pept. Sci. , vol.10 , pp. 464-475
    • Chen, E.1    Goldbeck, R.A.2    Kliger, D.S.3
  • 12
    • 34047194846 scopus 로고    scopus 로고
    • Conformational Equilibration Time of Unfolded Protein Chains and the Folding Speed Limit
    • Abel, C. J.; Goldbeck, R. A.; Latypov, R. F.; Roder, H.; Kliger, D. S. Conformational Equilibration Time of Unfolded Protein Chains and the Folding Speed Limit Biochemistry 2007, 46, 4090-4099
    • (2007) Biochemistry , vol.46 , pp. 4090-4099
    • Abel, C.J.1    Goldbeck, R.A.2    Latypov, R.F.3    Roder, H.4    Kliger, D.S.5
  • 13
    • 84861884623 scopus 로고    scopus 로고
    • Carbon-Deuterium Bonds as Probes of Protein Thermal Unfolding
    • Yu, W.; Dawson, P. E.; Zimmermann, J.; Romesberg, F. E. Carbon-Deuterium Bonds as Probes of Protein Thermal Unfolding J. Phys. Chem. B 2012, 116, 6397-6403
    • (2012) J. Phys. Chem. B , vol.116 , pp. 6397-6403
    • Yu, W.1    Dawson, P.E.2    Zimmermann, J.3    Romesberg, F.E.4
  • 14
    • 77952590099 scopus 로고    scopus 로고
    • The Folding Energy Landscape and Free Energy Excitations of Cytochrome c
    • Weinkam, P.; Zimmermann, J.; Romesberg, F. E.; Wolynes, P. G. The Folding Energy Landscape and Free Energy Excitations of Cytochrome c Acc. Chem. Res. 2010, 43, 652-660
    • (2010) Acc. Chem. Res. , vol.43 , pp. 652-660
    • Weinkam, P.1    Zimmermann, J.2    Romesberg, F.E.3    Wolynes, P.G.4
  • 15
    • 4644359012 scopus 로고    scopus 로고
    • How Cytochrome c Folds, and Why: Submolecular Foldon Units and Their Stepwise Sequential Stabilization
    • Maity, H.; Maity, M.; Englander, S. W. How Cytochrome c Folds, and Why: Submolecular Foldon Units and Their Stepwise Sequential Stabilization J. Mol. Biol. 2004, 343, 223-233
    • (2004) J. Mol. Biol. , vol.343 , pp. 223-233
    • Maity, H.1    Maity, M.2    Englander, S.W.3
  • 16
    • 0242578172 scopus 로고    scopus 로고
    • Intimate View of a Kinetic Protein Folding Intermediate: Residue-Resolved Structure, Interactions, Stability, Folding and Unfolding Rates, Homogeneity
    • Krishna, M. M. G.; Lin, Y.; Mayne, L.; Englander, S. W. Intimate View of a Kinetic Protein Folding Intermediate: Residue-Resolved Structure, Interactions, Stability, Folding and Unfolding Rates, Homogeneity J. Mol. Biol. 2003, 334, 501-513
    • (2003) J. Mol. Biol. , vol.334 , pp. 501-513
    • Krishna, M.M.G.1    Lin, Y.2    Mayne, L.3    Englander, S.W.4
  • 17
    • 66349104530 scopus 로고    scopus 로고
    • Compressing the Free Energy Range of Substructure Stabilities in Iso-1-Cytochrome c
    • Duncan, M. G.; Williams, M. D.; Bowler, B. E. Compressing the Free Energy Range of Substructure Stabilities in Iso-1-Cytochrome c Protein Sci. 2009, 18, 1155-1164
    • (2009) Protein Sci. , vol.18 , pp. 1155-1164
    • Duncan, M.G.1    Williams, M.D.2    Bowler, B.E.3
  • 18
    • 33745137861 scopus 로고    scopus 로고
    • Order of Steps in the Cytochrome c Folding Pathway: Evidence for a Sequential Stabilization Mechanism
    • Krishna, M. M.; Maity, H.; Rumbley, J. N.; Lin, Y.; Englander, S. W. Order of Steps in the Cytochrome c Folding Pathway: Evidence for a Sequential Stabilization Mechanism J. Mol. Biol. 2006, 359, 1410-1419
    • (2006) J. Mol. Biol. , vol.359 , pp. 1410-1419
    • Krishna, M.M.1    Maity, H.2    Rumbley, J.N.3    Lin, Y.4    Englander, S.W.5
  • 19
    • 24644481440 scopus 로고    scopus 로고
    • A Funneled Energy Landscape for Cytochrome c Directly Predicts the Sequential Folding Route Inferred from Hydrogen Exchange Experiments
    • Weinkam, P.; Zong, C.; Wolynes, P. G. A Funneled Energy Landscape for Cytochrome c Directly Predicts the Sequential Folding Route Inferred from Hydrogen Exchange Experiments Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 12401-12406
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 12401-12406
    • Weinkam, P.1    Zong, C.2    Wolynes, P.G.3
  • 20
    • 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.; Bren, K. L. 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. 2000, 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
  • 21
    • 49449094012 scopus 로고    scopus 로고
    • Zinc Porphyrin: A Fluorescent Acceptor in Studies of Zn-Cytochrome c Unfolding by Fluorescence Resonance Energy Transfer
    • Ensign, A. A.; Jo, I.; Yildirim, I.; Krauss, T. D.; Bren, K. L. Zinc Porphyrin: A Fluorescent Acceptor in Studies of Zn-Cytochrome c Unfolding by Fluorescence Resonance Energy Transfer Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 10779-10784
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 10779-10784
    • Ensign, A.A.1    Jo, I.2    Yildirim, I.3    Krauss, T.D.4    Bren, K.L.5
  • 22
    • 33644940724 scopus 로고    scopus 로고
    • Structural Characterization of an Equilibrium Unfolding Intermediate in Cytochrome c
    • Latypov, R. F.; Cheng, H.; Roder, N. A.; Zhang, J.; Roder, H. Structural Characterization of an Equilibrium Unfolding Intermediate in Cytochrome c J. Mol. Biol. 2006, 357, 1009-1025
    • (2006) J. Mol. Biol. , vol.357 , pp. 1009-1025
    • Latypov, R.F.1    Cheng, H.2    Roder, N.A.3    Zhang, J.4    Roder, H.5
  • 23
    • 0018265664 scopus 로고
    • The Unfolding of Cytochromes c in Methanol and Acid
    • Drew, H. R.; Dickerson, R. E. The Unfolding of Cytochromes c in Methanol and Acid J. Mol. Biol. 1978, 253, 8420-8427
    • (1978) J. Mol. Biol. , vol.253 , pp. 8420-8427
    • Drew, H.R.1    Dickerson, R.E.2
  • 26
    • 73649087584 scopus 로고    scopus 로고
    • On the Mechanism of Sds-Induced Protein Denaturation
    • Bhuyan, A. K. On the Mechanism of Sds-Induced Protein Denaturation Biopolymers 2010, 93, 186-199
    • (2010) Biopolymers , vol.93 , pp. 186-199
    • Bhuyan, A.K.1
  • 27
    • 17044441821 scopus 로고    scopus 로고
    • Structural and Kinetic Description of Cytochrome c Unfolding Induced by the Interaction with Lipid Vesicles
    • Pinheiro, T. J.; Elöve, G. A.; Watts, A.; Roder, H. Structural and Kinetic Description of Cytochrome c Unfolding Induced by the Interaction with Lipid Vesicles Biochemistry 1997, 36, 13122-13132
    • (1997) Biochemistry , vol.36 , pp. 13122-13132
    • Pinheiro, T.J.1    Elöve, G.A.2    Watts, A.3    Roder, H.4
  • 31
    • 37049003818 scopus 로고    scopus 로고
    • The Hierarchy of Structural Transitions Induced in Cytochrome c by Anionic Phospholipids Determines Its Peroxidase Activation and Selective Peroxidation during Apoptosis in Cells
    • Kapralov, A. A.; Kurnikov, I. V.; Vlasova, I. I.; Belikova, N. A.; Tyurin, V. A.; Basova, L. V.; Zhao, Q.; Tyurina, Y. Y.; Jiang, J.; Bayir, H. The Hierarchy of Structural Transitions Induced in Cytochrome c by Anionic Phospholipids Determines Its Peroxidase Activation and Selective Peroxidation During Apoptosis in Cells Biochemistry 2007, 46, 14232-14244
    • (2007) Biochemistry , vol.46 , pp. 14232-14244
    • Kapralov, A.A.1    Kurnikov, I.V.2    Vlasova, I.I.3    Belikova, N.A.4    Tyurin, V.A.5    Basova, L.V.6    Zhao, Q.7    Tyurina, Y.Y.8    Jiang, J.9    Bayir, H.10
  • 33
    • 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.; Silkstone, G.; Wilson, M. T.; Cheesman, M. R.; Butt, J. N. Probing a Complex of Cytochrome c and Cardiolipin by Magnetic Circular Dichroism Spectroscopy: Implications for the Initial Events in Apoptosis J. Am. Chem. Soc. 2011, 133, 19676-19679
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 19676-19679
    • Bradley, J.M.1    Silkstone, G.2    Wilson, M.T.3    Cheesman, M.R.4    Butt, J.N.5
  • 34
    • 84867550132 scopus 로고    scopus 로고
    • Nitric Oxide Binding to the Cardiolipin Complex of Ferric Cytochrome C
    • Silkstone, G.; Kapetanaki, S. M.; Husu, I.; Vos, M. H.; Wilson, M. T. Nitric Oxide Binding to the Cardiolipin Complex of Ferric Cytochrome C Biochemistry 2012, 51, 6760-6766
    • (2012) Biochemistry , vol.51 , pp. 6760-6766
    • Silkstone, G.1    Kapetanaki, S.M.2    Husu, I.3    Vos, M.H.4    Wilson, M.T.5
  • 36
    • 84869456778 scopus 로고    scopus 로고
    • His26 Protonation in Cytochrome c Triggers Microsecond β-Sheet Formation and Heme Exposure: Implications for Apoptosis
    • Balakrishnan, G.; Hu, Y.; Spiro, T. G. His26 Protonation in Cytochrome c Triggers Microsecond β-Sheet Formation and Heme Exposure: Implications for Apoptosis J. Am. Chem. Soc. 2012, 134, 19061-19069
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 19061-19069
    • Balakrishnan, G.1    Hu, Y.2    Spiro, T.G.3
  • 37
    • 79958122758 scopus 로고    scopus 로고
    • Single Vesicle Observations of the Cardiolipin-Cytochrome c Interaction: Induction of Membrane Morphology Changes
    • Beales, P. A.; Bergstrom, C. L.; Geerts, N.; Groves, J. T.; Vanderlick, T. K. Single Vesicle Observations of the Cardiolipin-Cytochrome c Interaction: Induction of Membrane Morphology Changes Langmuir 2011, 27, 6107-6115
    • (2011) Langmuir , vol.27 , pp. 6107-6115
    • Beales, P.A.1    Bergstrom, C.L.2    Geerts, N.3    Groves, J.T.4    Vanderlick, T.K.5
  • 40
    • 84869442007 scopus 로고    scopus 로고
    • Origin of the Conformational Heterogeneity of Cardiolipin-Bound Cytochrome c
    • Hong, Y.; Muenzner, J.; Grimm, S. K.; Pletneva, E. V. Origin of the Conformational Heterogeneity of Cardiolipin-Bound Cytochrome c J. Am. Chem. Soc. 2012, 134, 18713-18723
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 18713-18723
    • Hong, Y.1    Muenzner, J.2    Grimm, S.K.3    Pletneva, E.V.4
  • 41
    • 70449234614 scopus 로고
    • Spectrum of Horse-Heart Cytochrome c
    • Margoliash, E.; Frohwirt, N. Spectrum of Horse-Heart Cytochrome c Biochem. J. 1959, 71, 570-572
    • (1959) Biochem. J. , vol.71 , pp. 570-572
    • Margoliash, E.1    Frohwirt, N.2
  • 43
    • 33846462466 scopus 로고    scopus 로고
    • A Conformational Switch to β-Sheet Structure in Cytochrome c Leads to Heme Exposure. Implications for Cardiolipin Peroxidation and Apoptosis
    • Balakrishnan, G.; Hu, Y.; Oyerinde, O. F.; Su, J.; Groves, J. T.; Spiro, T. G. A Conformational Switch to β-Sheet Structure in Cytochrome c Leads to Heme Exposure. Implications for Cardiolipin Peroxidation and Apoptosis J. Am. Chem. Soc. 2007, 129, 504-505
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 504-505
    • Balakrishnan, G.1    Hu, Y.2    Oyerinde, O.F.3    Su, J.4    Groves, J.T.5    Spiro, T.G.6
  • 46
    • 8544284808 scopus 로고    scopus 로고
    • Insertion Kinetics of a Denatured α-Helical Membrane Protein into Phospholipid Bilayer Vesicles
    • Lorch, M.; Booth, P. J. Insertion Kinetics of a Denatured α-Helical Membrane Protein into Phospholipid Bilayer Vesicles J. Mol. Biol. 2004, 344, 1109-1121
    • (2004) J. Mol. Biol. , vol.344 , pp. 1109-1121
    • Lorch, M.1    Booth, P.J.2
  • 47
    • 4444363179 scopus 로고    scopus 로고
    • Folding Kinetics of an α-Helical Membrane Protein in Phospholipid Bilayer Vesicles
    • Allen, S. J.; Curran, A. R.; Templer, R. H.; Meijberg, W.; Booth, P. J. Folding Kinetics of an α-Helical Membrane Protein in Phospholipid Bilayer Vesicles J. Mol. Biol. 2004, 342, 1279-1291
    • (2004) J. Mol. Biol. , vol.342 , pp. 1279-1291
    • Allen, S.J.1    Curran, A.R.2    Templer, R.H.3    Meijberg, W.4    Booth, P.J.5
  • 48
    • 84861050825 scopus 로고    scopus 로고
    • A Close Look at Proteins: Submolecular Resolution of Two- and Three-Dimensionally Folded Cytochrome c at Surfaces
    • Deng, Z.; Thontasen, N.; Malinowski, N.; Rinke, G.; Harnau, L.; Rauschenbach, S.; Kern, K. A Close Look at Proteins: Submolecular Resolution of Two- and Three-Dimensionally Folded Cytochrome c at Surfaces Nano Lett. 2012, 12, 2452-2458
    • (2012) Nano Lett. , vol.12 , pp. 2452-2458
    • Deng, Z.1    Thontasen, N.2    Malinowski, N.3    Rinke, G.4    Harnau, L.5    Rauschenbach, S.6    Kern, K.7
  • 49
    • 0029738341 scopus 로고    scopus 로고
    • Surface Plasmon Resonance Studies of Complex Formation between Cytochrome c and Bovine Cytochrome c Oxidase Incorporated into a Supported Planar Lipid Bilayer. I. Binding of Cytochrome c to Cardiolipin/Phosphatidylcholine Membranes in the Absence of Oxidase
    • Salamon, Z.; Tollin, G. Surface Plasmon Resonance Studies of Complex Formation between Cytochrome c and Bovine Cytochrome c Oxidase Incorporated into a Supported Planar Lipid Bilayer. I. Binding of Cytochrome c to Cardiolipin/Phosphatidylcholine Membranes in the Absence of Oxidase Biophys. J. 1996, 71, 848-857
    • (1996) Biophys. J. , vol.71 , pp. 848-857
    • Salamon, Z.1    Tollin, G.2
  • 50
    • 0039178090 scopus 로고    scopus 로고
    • Membrane Location of Spin-Labeled Cytochrome c Determined by Paramagnetic Relaxation Agents
    • Kostrzewa, A.; Pali, T.; Froncisz, W.; Marsh, D. Membrane Location of Spin-Labeled Cytochrome c Determined by Paramagnetic Relaxation Agents Biochemistry 2000, 39, 6066-6074
    • (2000) Biochemistry , vol.39 , pp. 6066-6074
    • Kostrzewa, A.1    Pali, T.2    Froncisz, W.3    Marsh, D.4
  • 51
    • 0028057721 scopus 로고
    • Evidence for Two Distinct Acidic Phospholipid-Binding Sites in Cytochrome c
    • Rytömaa, M.; Kinnunen, P. K. Evidence for Two Distinct Acidic Phospholipid-Binding Sites in Cytochrome c J. Biol. Chem. 1994, 269, 1770-1774
    • (1994) J. Biol. Chem. , vol.269 , pp. 1770-1774
    • Rytömaa, M.1    Kinnunen, P.K.2
  • 52
    • 81255144005 scopus 로고    scopus 로고
    • Probing the Dynamics of a His73-Heme Alkaline Transition in a Destabilized Variant of Yeast Iso-1-Cytochrome c with Conformationally Gated Electron Transfer Methods
    • Bandi, S.; Bowler, B. E. Probing the Dynamics of a His73-Heme Alkaline Transition in a Destabilized Variant of Yeast Iso-1-Cytochrome c with Conformationally Gated Electron Transfer Methods Biochemistry 2011, 50, 10027-10040
    • (2011) Biochemistry , vol.50 , pp. 10027-10040
    • Bandi, S.1    Bowler, B.E.2
  • 53
    • 34548406580 scopus 로고    scopus 로고
    • Branching in the Sequential Folding Pathway of Cytochrome c
    • Krishna, M. M.; Maity, H.; Rumbley, J. N.; Englander, S. W. Branching in the Sequential Folding Pathway of Cytochrome c Protein Sci. 2007, 16, 1946-1956
    • (2007) Protein Sci. , vol.16 , pp. 1946-1956
    • Krishna, M.M.1    Maity, H.2    Rumbley, J.N.3    Englander, S.W.4
  • 56
    • 77955456084 scopus 로고    scopus 로고
    • Characteriation of Bioactive Cell Penetrating Peptides from Human Cytochrome c: Protein Mimicry and the Development of a Novel Apoptogenic Agent
    • Jones, S.; Holm, T.; Mager, I.; Langel, U.; Howl, J. Characteriation of Bioactive Cell Penetrating Peptides from Human Cytochrome c: Protein Mimicry and the Development of a Novel Apoptogenic Agent Chem. Biol. 2010, 17, 735-744
    • (2010) Chem. Biol. , vol.17 , pp. 735-744
    • Jones, S.1    Holm, T.2    Mager, I.3    Langel, U.4    Howl, J.5
  • 58
    • 0025007598 scopus 로고
    • High-Resolution 3-Dimensional Structure of Horse Heart Cytochrome c
    • Bushnell, G. W.; Louie, G. V.; Brayer, G. D. High-Resolution 3-Dimensional Structure of Horse Heart Cytochrome c J. Mol. Biol. 1990, 214, 585-595
    • (1990) J. Mol. Biol. , vol.214 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3
  • 59
    • 10044269982 scopus 로고    scopus 로고
    • Many Faces of the Unfolded State: Conformational Heterogeneity in Denatured Yeast Cytochrome c
    • Pletneva, E. V.; Gray, H. B.; Winkler, J. R. Many Faces of the Unfolded State: Conformational Heterogeneity in Denatured Yeast Cytochrome c J. Mol. Biol. 2005, 345, 855-867
    • (2005) J. Mol. Biol. , vol.345 , pp. 855-867
    • Pletneva, E.V.1    Gray, H.B.2    Winkler, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.