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Volumn 1827, Issue 6, 2013, Pages 769-778

Atomistic simulations indicate cardiolipin to have an integral role in the structure of the cytochrome bc1 complex

Author keywords

Cardiolipin; Cytochrome bc1; Membrane protein; Molecular dynamics simulation; Proton transfer

Indexed keywords

CARDIOLIPIN; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 84875920201     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2013.03.005     Document Type: Article
Times cited : (57)

References (49)
  • 1
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • D. Lingwood, and K. Simons Lipid rafts as a membrane-organizing principle Science 327 2010 46 50
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 2
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • A.G. Lee How lipids affect the activities of integral membrane proteins Biochim. Biophys. Acta 1666 2004 62 87
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 62-87
    • Lee, A.G.1
  • 4
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • R. Phillips, T. Ursell, P. Wiggins, and P. Sens Emerging roles for lipids in shaping membrane-protein function Nature 459 2009 379 385
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 6
    • 49749095639 scopus 로고    scopus 로고
    • Lipids and membrane protein structures
    • C. Hunte, and S. Richers Lipids and membrane protein structures Curr. Opin. Struct. Biol. 18 2008 406 411
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 406-411
    • Hunte, C.1    Richers, S.2
  • 8
    • 0019320448 scopus 로고
    • Structural role of phospholipids in ubiquinol-cytochrome c reductase
    • C.A. Yu, and L. Yu Structural role of phospholipids in ubiquinol-cytochrome c reductase Biochemistry 19 1980 5715 5720
    • (1980) Biochemistry , vol.19 , pp. 5715-5720
    • Yu, C.A.1    Yu, L.2
  • 10
    • 0041401742 scopus 로고    scopus 로고
    • Structure of the yeast cytochrome bc1 complex with a hydroxyquinone anion Qo site inhibitor bound
    • H. Palsdottir, C.G. Lojero, B.L. Trumpower, and C. Hunte Structure of the yeast cytochrome bc1 complex with a hydroxyquinone anion Qo site inhibitor bound J. Biol. Chem. 278 2003 31303 31311
    • (2003) J. Biol. Chem. , vol.278 , pp. 31303-31311
    • Palsdottir, H.1    Lojero, C.G.2    Trumpower, B.L.3    Hunte, C.4
  • 11
    • 22544467474 scopus 로고    scopus 로고
    • Binding of the respiratory chain inhibitor antimycin to the mitochondrial bc1 complex: A new crystal structure reveals an altered intramolecular hydrogen-bonding pattern
    • L.-S. Huang, D. Cobessi, E.Y. Tung, and E.A. Berry Binding of the respiratory chain inhibitor antimycin to the mitochondrial bc1 complex: a new crystal structure reveals an altered intramolecular hydrogen-bonding pattern J. Mol. Biol. 351 2005 573 597
    • (2005) J. Mol. Biol. , vol.351 , pp. 573-597
    • Huang, L.-S.1    Cobessi, D.2    Tung, E.Y.3    Berry, E.A.4
  • 13
    • 0034663688 scopus 로고    scopus 로고
    • Crystallographic location of two Zn(2 +)-binding sites in the avian cytochrome bc(1) complex
    • E.A. Berry, Z. Zhang, H.D. Bellamy, and L. Huang Crystallographic location of two Zn(2 +)-binding sites in the avian cytochrome bc(1) complex Biochim. Biophys. Acta 1459 2000 440 448
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 440-448
    • Berry, E.A.1    Zhang, Z.2    Bellamy, H.D.3    Huang, L.4
  • 14
    • 4143084952 scopus 로고    scopus 로고
    • Crystallographic studies of quinol oxidation site inhibitors: A modified classification of inhibitors for the cytochrome bc(1) complex
    • L. Esser, B. Quinn, Y.-F. Li, M. Zhang, M. Elberry, L. Yu, C.-A. Yu, and Di Xia Crystallographic studies of quinol oxidation site inhibitors: a modified classification of inhibitors for the cytochrome bc(1) complex J. Mol. Biol. 341 2004 281 302
    • (2004) J. Mol. Biol. , vol.341 , pp. 281-302
    • Esser, L.1    Quinn, B.2    Li, Y.-F.3    Zhang, M.4    Elberry, M.5    Yu, L.6    Yu, C.-A.7    Xia, D.8
  • 16
    • 66749192576 scopus 로고    scopus 로고
    • Role of phospholipids in respiratory cytochrome bc(1) complex catalysis and supercomplex formation
    • T. Wenz, R. Hielscher, P. Hellwig, H. Schägger, S. Richers, and C. Hunte Role of phospholipids in respiratory cytochrome bc(1) complex catalysis and supercomplex formation Biochim. Biophys. Acta 1787 2009 609 616
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 609-616
    • Wenz, T.1    Hielscher, R.2    Hellwig, P.3    Schägger, H.4    Richers, S.5    Hunte, C.6
  • 17
    • 0019887784 scopus 로고
    • Cardiolipin requirement for electron transfer in complex i and III of the mitochondrial respiratory chain
    • M. Fry, and D.E. Green Cardiolipin requirement for electron transfer in complex I and III of the mitochondrial respiratory chain J. Biol. Chem. 256 1981 1874 1880
    • (1981) J. Biol. Chem. , vol.256 , pp. 1874-1880
    • Fry, M.1    Green, D.E.2
  • 18
    • 0039843110 scopus 로고    scopus 로고
    • Phospholipase digestion of bound cardiolipin reversibly inactivates bovine cytochrome bc1
    • B. Gomez, and N.C. Robinson Phospholipase digestion of bound cardiolipin reversibly inactivates bovine cytochrome bc1 Biochemistry 38 1999 9031 9038
    • (1999) Biochemistry , vol.38 , pp. 9031-9038
    • Gomez, B.1    Robinson, N.C.2
  • 19
    • 0026603840 scopus 로고
    • Cardiolipins and biomembrane function
    • F. Hoch Cardiolipins and biomembrane function Biochim. Biophys. Acta 1113 1992 71 133
    • (1992) Biochim. Biophys. Acta , vol.1113 , pp. 71-133
    • Hoch, F.1
  • 20
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • M. Schlame, D. Rua, and M.L. Greenberg The biosynthesis and functional role of cardiolipin Prog. Lipid Res. 39 2000 257 288
    • (2000) Prog. Lipid Res. , vol.39 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 21
    • 0037113864 scopus 로고    scopus 로고
    • Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane
    • M. Zhang, E. Mileykovskaya, and W. Dowhan Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane J. Biol. Chem. 277 2002 43553 43556
    • (2002) J. Biol. Chem. , vol.277 , pp. 43553-43556
    • Zhang, M.1    Mileykovskaya, E.2    Dowhan, W.3
  • 22
    • 0035803487 scopus 로고    scopus 로고
    • Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure
    • C. Lange, J.H. Nett, B.L. Trumpower, and C. Hunte Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure EMBO J. 20 2001 6591 6600
    • (2001) EMBO J. , vol.20 , pp. 6591-6600
    • Lange, C.1    Nett, J.H.2    Trumpower, B.L.3    Hunte, C.4
  • 23
    • 0037174138 scopus 로고    scopus 로고
    • Cardiolipin: A proton trap for oxidative phosphorylation
    • T.H. Haines, and N.A. Dencher Cardiolipin: a proton trap for oxidative phosphorylation FEBS Lett. 528 2002 35 39
    • (2002) FEBS Lett. , vol.528 , pp. 35-39
    • Haines, T.H.1    Dencher, N.A.2
  • 24
    • 0038730358 scopus 로고    scopus 로고
    • Protonmotive pathways and mechanisms in the cytochrome bc1 complex
    • C. Hunte, H. Palsdottir, and B.L. Trumpower Protonmotive pathways and mechanisms in the cytochrome bc1 complex FEBS Lett. 545 2003 39 46
    • (2003) FEBS Lett. , vol.545 , pp. 39-46
    • Hunte, C.1    Palsdottir, H.2    Trumpower, B.L.3
  • 25
    • 47749126543 scopus 로고    scopus 로고
    • Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer
    • S.R.N. Solmaz, and C. Hunte Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer J. Biol. Chem. 283 2008 17542 17549
    • (2008) J. Biol. Chem. , vol.283 , pp. 17542-17549
    • Solmaz, S.R.N.1    Hunte, C.2
  • 26
    • 14544292020 scopus 로고    scopus 로고
    • Electrostatic interactions between model mitochondrial membranes
    • S. Nichols-Smith, and T. Kuhl Electrostatic interactions between model mitochondrial membranes Colloids Surf. B Biointerfaces 41 2005 121 127
    • (2005) Colloids Surf. B Biointerfaces , vol.41 , pp. 121-127
    • Nichols-Smith, S.1    Kuhl, T.2
  • 27
  • 28
    • 71549166641 scopus 로고    scopus 로고
    • Mitochondrial membranes with mono- and divalent salt: Changes induced by salt ions on structure and dynamics
    • S. Pöyry, T. Róg, M. Karttunen, and I. Vattulainen Mitochondrial membranes with mono- and divalent salt: changes induced by salt ions on structure and dynamics J. Phys. Chem. B 113 2009 15513 15521
    • (2009) J. Phys. Chem. B , vol.113 , pp. 15513-15521
    • Pöyry, S.1    Róg, T.2    Karttunen, M.3    Vattulainen, I.4
  • 29
    • 53049083198 scopus 로고    scopus 로고
    • Molecular dynamics simulations of cardiolipin bilayers
    • M. Dahlberg, and A. Maliniak Molecular dynamics simulations of cardiolipin bilayers J. Phys. Chem. B 112 2008 11655 11663
    • (2008) J. Phys. Chem. B , vol.112 , pp. 11655-11663
    • Dahlberg, M.1    Maliniak, A.2
  • 30
    • 84860778070 scopus 로고    scopus 로고
    • Insight into the properties of cardiolipin containing bilayers from molecular dynamics simulations, using a hybrid all-atom/united-atom force field
    • D. Aguayo, F.D. González-Nilo, and C. Chipot Insight into the properties of cardiolipin containing bilayers from molecular dynamics simulations, using a hybrid all-atom/united-atom force field J. Chem. Theory Comput. 8 2012 1765 1773
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 1765-1773
    • Aguayo, D.1    González-Nilo, F.D.2    Chipot, C.3
  • 31
    • 84876898313 scopus 로고    scopus 로고
    • Parameterization of the prosthetic redox centers of the bacterial cytochrome bc1 complex for atomistic molecular dynamics simulations
    • in press
    • K. Kaszuba, P.A. Postila, O. Cramariuc, M. Sarewicz, A. Osyczka, I. Vattulainen, T. Róg, Parameterization of the prosthetic redox centers of the bacterial cytochrome bc1 complex for atomistic molecular dynamics simulations. Theoretical Chemistry Accounts. in press.
    • Theoretical Chemistry Accounts
    • Kaszuba, K.1
  • 32
    • 84875951229 scopus 로고    scopus 로고
    • Key role of water in proton transfer at the Qo-site of the cytochrome bc1 complex predicted by atomistic molecular dynamics simulations
    • doi:10.1016/j.bbabio.2013.02.005 in press
    • P.A. Postila, K. Kaszuba, M. Sarewicz, A. Osyczka, I. Vattulainen, T. Róg, Key role of water in proton transfer at the Qo-site of the cytochrome bc1 complex predicted by atomistic molecular dynamics simulations. BBA Bioenerg. in press, http://dx.doi.org/10.1016/j.bbabio.2013.02.005.
    • BBA Bioenerg
    • Postila, P.A.1
  • 33
    • 4043152888 scopus 로고    scopus 로고
    • X-ray structure of Rhodobacter capsulatus cytochrome bc (1): Comparison with its mitochondrial and chloroplast counterparts
    • E.A. Berry, L.-S. Huang, L.K. Saechao, N.G. Pon, M. Valkova-Valchanova, and F. Daldal X-ray structure of Rhodobacter capsulatus cytochrome bc (1): comparison with its mitochondrial and chloroplast counterparts Photosynth. Res. 81 2004 251 275
    • (2004) Photosynth. Res. , vol.81 , pp. 251-275
    • Berry, E.A.1    Huang, L.-S.2    Saechao, L.K.3    Pon, N.G.4    Valkova-Valchanova, M.5    Daldal, F.6
  • 35
    • 65249133096 scopus 로고    scopus 로고
    • Role of cardiolipins in the inner mitochondrial membrane: Insight gained through atom-scale simulations
    • T. Róg, H. Martinez-Seara, N. Munck, M. Oresic, M. Karttunen, and I. Vattulainen Role of cardiolipins in the inner mitochondrial membrane: insight gained through atom-scale simulations J. Phys. Chem. B 113 2009 3413 3422
    • (2009) J. Phys. Chem. B , vol.113 , pp. 3413-3422
    • Róg, T.1    Martinez-Seara, H.2    Munck, N.3    Oresic, M.4    Karttunen, M.5    Vattulainen, I.6
  • 37
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • A.D. Mackerell, M. Feig, and C.L. Brooks Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations J. Comput. Chem. 25 2004 1400 1415
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • MacKerell, A.D.1    Feig, M.2    Brooks, C.L.3
  • 38
    • 60649103257 scopus 로고    scopus 로고
    • Validation of all-atom phosphatidylcholine lipid force fields in the tensionless NPT ensemble
    • J. Taylor, N.E. Whiteford, G. Bradley, and G.W. Watson Validation of all-atom phosphatidylcholine lipid force fields in the tensionless NPT ensemble Biochim. Biophys. Acta 1788 2009 638 649
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 638-649
    • Taylor, J.1    Whiteford, N.E.2    Bradley, G.3    Watson, G.W.4
  • 39
    • 77953967138 scopus 로고    scopus 로고
    • Molecular dynamics simulations reveal fundamental role of water as factor determining affinity of binding of beta-blocker nebivolol to beta(2)-adrenergic receptor
    • K. Kaszuba, T. Róg, K. Bryl, I. Vattulainen, and M. Karttunen Molecular dynamics simulations reveal fundamental role of water as factor determining affinity of binding of beta-blocker nebivolol to beta(2)-adrenergic receptor J. Phys. Chem. B 114 2010 8374 8386
    • (2010) J. Phys. Chem. B , vol.114 , pp. 8374-8386
    • Kaszuba, K.1    Róg, T.2    Bryl, K.3    Vattulainen, I.4    Karttunen, M.5
  • 42
    • 22244445788 scopus 로고    scopus 로고
    • Imaging alpha-hemolysin with molecular dynamics: Ionic conductance, osmotic permeability, and the electrostatic potential map
    • A. Aksimentiev, and K. Schulten Imaging alpha-hemolysin with molecular dynamics: ionic conductance, osmotic permeability, and the electrostatic potential map Biophys. J. 88 2005 3745 3761
    • (2005) Biophys. J. , vol.88 , pp. 3745-3761
    • Aksimentiev, A.1    Schulten, K.2
  • 43
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24 1991 946 950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 44
    • 0028057108 scopus 로고
    • Raster3D Version 2.0. A program for photorealistic molecular graphics
    • E.A. Merritt, and M.E.P. Murphy Raster3D Version 2.0. A program for photorealistic molecular graphics Acta Crystallogr. D: Biol. Crystallogr. 50 1994 869 873
    • (1994) Acta Crystallogr. D: Biol. Crystallogr. , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 45
  • 47
    • 27844436560 scopus 로고    scopus 로고
    • Specific protein-lipid interactions in membrane proteins
    • C. Hunte Specific protein-lipid interactions in membrane proteins Biochem. Soc. Trans. 33 2005 938 942
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 938-942
    • Hunte, C.1
  • 48
    • 84874599376 scopus 로고    scopus 로고
    • Evidence for cardiolipin binding sites on the membrane-exposed surface of the cytochrome bc1
    • 10.1021/ja310577u
    • C. Arnarez, J.-P. Mazat, J. Elezgaray, S.-J. Marrink, and X. Periole Evidence for cardiolipin binding sites on the membrane-exposed surface of the cytochrome bc1 J. Am. Chem. Soc. 135 8 2013 3112 3120 10.1021/ja310577u
    • (2013) J. Am. Chem. Soc. , vol.135 , Issue.8 , pp. 3112-3120
    • Arnarez, C.1    Mazat, J.-P.2    Elezgaray, J.3    Marrink, S.-J.4    Periole, X.5


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