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Volumn 5, Issue 6, 1996, Pages 1081-1092

The heme redox center of chloroplast cytochrome f is linked to a buried five-water chain

Author keywords

cytochrome b6 f complex; electron transfer; energy transduction; heme protein; proton translocation

Indexed keywords

CYTOCHROME F; PLASTOCYANIN;

EID: 0029897140     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050610     Document Type: Article
Times cited : (134)

References (45)
  • 2
    • 0028172534 scopus 로고
    • The immunoglobulin fold: Structural classification, sequence patterns and common core
    • Bork P, Holm L, Sander C. 1994. The immunoglobulin fold: Structural classification, sequence patterns and common core. J Mol Biol 242:309-320.
    • (1994) J Mol Biol , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 3
    • 0026332339 scopus 로고
    • Water is required for proton transfer from aspartate 96 to bacteriorhodopsin Schiff base
    • Cao Y, Varo G, Chang M, Ni B, Needleman R, Lanyi JK. 1991. Water is required for proton transfer from aspartate 96 to bacteriorhodopsin Schiff base. Biochemistry 30:10972-10979.
    • (1991) Biochemistry , vol.30 , pp. 10972-10979
    • Cao, Y.1    Varo, G.2    Chang, M.3    Ni, B.4    Needleman, R.5    Lanyi, J.K.6
  • 8
    • 0001217574 scopus 로고
    • The preparation and some properties of cytochrome f
    • Davenport HE, Hill R. 1952. The preparation and some properties of cytochrome f. Proc R Soc London B 139:327-345.
    • (1952) Proc R Soc London B , vol.139 , pp. 327-345
    • Davenport, H.E.1    Hill, R.2
  • 9
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: Cofactors and protein-cofactor interactions
    • Ermler U, Fritzsch G, Buchanan S, Michel H. 1994. Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.65 Å resolution: Cofactors and protein-cofactor interactions. Structure 2:925-936.
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.3    Michel, H.4
  • 10
    • 0000121207 scopus 로고
    • Cytochrome f: Structure, function, and biosynthesis
    • Gray J. 1992. Cytochrome f: Structure, function, and biosynthesis. Photosyn Res 34:359-374.
    • (1992) Photosyn Res , vol.34 , pp. 359-374
    • Gray, J.1
  • 11
    • 0000303843 scopus 로고
    • Plastocyanin: Structure and function
    • Gross EL. 1993. Plastocyanin: Structure and function. Photosyn Res 37:103-116.
    • (1993) Photosyn Res , vol.37 , pp. 103-116
    • Gross, E.L.1
  • 12
    • 0024577061 scopus 로고
    • A denaturation-induced proton-uptake study of horse ferricytochrome c
    • Hartshorn T, Moore GR. 1989. A denaturation-induced proton-uptake study of horse ferricytochrome c. Biochem J 238:595-598.
    • (1989) Biochem J , vol.238 , pp. 595-598
    • Hartshorn, T.1    Moore, G.R.2
  • 13
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R, Baldwin JM, Ceska TA, Zemlin F, Beckmann E, Downing KH. 1990. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol Biol 213:899-929.
    • (1990) J Mol Biol , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 14
    • 0027690997 scopus 로고
    • Crystal structure of neocarzinostatin, an antitumor protein-chromophore complex
    • Kim KH, Kwon BM, Myers AG, Rees DC. 1993. Crystal structure of neocarzinostatin, an antitumor protein-chromophore complex. Science 262:1042-1046.
    • (1993) Science , vol.262 , pp. 1042-1046
    • Kim, K.H.1    Kwon, B.M.2    Myers, A.G.3    Rees, D.C.4
  • 15
    • 0023650593 scopus 로고
    • Sequence of the apocytochrome f gene encoded by the Vicia faba chloroplast genome
    • Ko K, Straus NA. 1987. Sequence of the apocytochrome f gene encoded by the Vicia faba chloroplast genome. Nucleic Acids Res 15:2391.
    • (1987) Nucleic Acids Res , vol.15 , pp. 2391
    • Ko, K.1    Straus, N.A.2
  • 16
    • 0027769837 scopus 로고
    • Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin
    • Lanyi JK. 1993. Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin. Biochim Biophys Acta 1183:241-261.
    • (1993) Biochim Biophys Acta , vol.1183 , pp. 241-261
    • Lanyi, J.K.1
  • 17
    • 0027245581 scopus 로고
    • What information do inhibitors provide about the structure of the hydroquinone oxidation site of ubihydroquinone: Cytochrome c oxidoreductase?
    • Link TA, Haase U, Brandt U, von Jagow G. 1993. What information do inhibitors provide about the structure of the hydroquinone oxidation site of ubihydroquinone: Cytochrome c oxidoreductase? J Bioenerg Biomem 25:221-232.
    • (1993) J Bioenerg Biomem , vol.25 , pp. 221-232
    • Link, T.A.1    Haase, U.2    Brandt, U.3    Von Jagow, G.4
  • 19
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati PV. 1952. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallogr 5:802-810.
    • (1952) Acta Crystallogr , vol.5 , pp. 802-810
    • Luzzati, P.V.1
  • 20
  • 21
    • 0028773015 scopus 로고
    • Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation
    • Martinez SE, Huang D, Szczepaniak A, Cramer WA, Smith JL. 1994. Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation. Structure 2:95-105.
    • (1994) Structure , vol.2 , pp. 95-105
    • Martinez, S.E.1    Huang, D.2    Szczepaniak, A.3    Cramer, W.A.4    Smith, J.L.5
  • 23
    • 0014179056 scopus 로고
    • Ligand-protein interactions in imidazole and 1,2,4-triazole complexes of methaemoglobin from Chironomus plumosus
    • Mohr P, Scheler W, Schumann H, Müller K. 1967. Ligand-protein interactions in imidazole and 1,2,4-triazole complexes of methaemoglobin from Chironomus plumosus. Eur J Biochem 3:158-163.
    • (1967) Eur J Biochem , vol.3 , pp. 158-163
    • Mohr, P.1    Scheler, W.2    Schumann, H.3    Müller, K.4
  • 25
    • 0018897965 scopus 로고
    • Proton NMR study of hemoproteins: Ionization and orientation of iron-bound imidazole in methemoglobin and metmyoglobin
    • Morishima I, Neya S, Yonezawa T. 1980. Proton NMR study of hemoproteins: Ionization and orientation of iron-bound imidazole in methemoglobin and metmyoglobin. Biochim Biophys Acta 621:218-226.
    • (1980) Biochim Biophys Acta , vol.621 , pp. 218-226
    • Morishima, I.1    Neya, S.2    Yonezawa, T.3
  • 27
    • 0345613372 scopus 로고
    • Molecular mechanisms for proton transport in membranes
    • Nagle J, Morowitz H. 1978. Molecular mechanisms for proton transport in membranes. Proc Natl Acad Sci USA 75:298-302.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 298-302
    • Nagle, J.1    Morowitz, H.2
  • 28
    • 0024726467 scopus 로고
    • Pathway of proton transfer in bacterial reaction centers: Role of aspartate-L213 in proton transfers associated with reduction of quinone to dihydroquinone
    • Paddock ML, Rongey SH, Feher G, Okamura MY. 1989. Pathway of proton transfer in bacterial reaction centers: Role of aspartate-L213 in proton transfers associated with reduction of quinone to dihydroquinone. Proc Natl Acad Sci USA 86:6602-6606.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6602-6606
    • Paddock, M.L.1    Rongey, S.H.2    Feher, G.3    Okamura, M.Y.4
  • 29
    • 0028009920 scopus 로고
    • Pathway of proton transfer in bacterial reaction centers: Replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover
    • Paddock ML, Rongey SH, McPherson PH, Juth A, Feher G, Okamura MY. 1994. Pathway of proton transfer in bacterial reaction centers: Replacement of glutamic acid 212 in the L subunit by glutamine inhibits quinone (secondary acceptor) turnover. Biochemistry 33:734-745.
    • (1994) Biochemistry , vol.33 , pp. 734-745
    • Paddock, M.L.1    Rongey, S.H.2    McPherson, P.H.3    Juth, A.4    Feher, G.5    Okamura, M.Y.6
  • 30
    • 0025298852 scopus 로고
    • Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction
    • Papadopoulos G, Dencher NA, Zaccai G, Bueldt G. 1990. Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. J Mol Biol 214:15-19.
    • (1990) J Mol Biol , vol.214 , pp. 15-19
    • Papadopoulos, G.1    Dencher, N.A.2    Zaccai, G.3    Bueldt, G.4
  • 32
    • 9344249605 scopus 로고
    • Structure and dynamics of a proton wire: A theoretical study of the gramicidin channel
    • Pomes R, Roux B. 1995. Structure and dynamics of a proton wire: A theoretical study of the gramicidin channel. Biophys J 68:A150.
    • (1995) Biophys J , vol.68
    • Pomes, R.1    Roux, B.2
  • 33
    • 0028246555 scopus 로고
    • Solution structure of horse heart ferrocytochrome c determined by high resolution NMR and restrained simulated annealing
    • Qi PX, DiStefano DL, Wand AJ. 1994a. Solution structure of horse heart ferrocytochrome c determined by high resolution NMR and restrained simulated annealing. Biochemistry 33:6408-6417.
    • (1994) Biochemistry , vol.33 , pp. 6408-6417
    • Qi, P.X.1    DiStefano, D.L.2    Wand, A.J.3
  • 35
    • 0026720247 scopus 로고
    • Crystalline ribonuclease a loses function below the dynamical transition at 220 K
    • Rasmussen BF, Stock AM, Ringe D, Petsko GA. 1992. Crystalline ribonuclease A loses function below the dynamical transition at 220 K. Nature 357:423-424.
    • (1992) Nature , vol.357 , pp. 423-424
    • Rasmussen, B.F.1    Stock, A.M.2    Ringe, D.3    Petsko, G.A.4
  • 36
    • 0019321226 scopus 로고
    • The redox potentials of the b-type cytochromes of higher plant chloroplasts
    • Rich PR, Bendall DS. 1980. The redox potentials of the b-type cytochromes of higher plant chloroplasts. Biochim Biophys Acta 591:153-161.
    • (1980) Biochim Biophys Acta , vol.591 , pp. 153-161
    • Rich, P.R.1    Bendall, D.S.2
  • 37
    • 0027405698 scopus 로고
    • Pathway of proton transfer in bacterial reaction centers: Second-site mutation Asn-M44 → Asn mutant of Rhodobacter sphaeroides
    • Rongey SH, Paddock ML, Feher G, Okamura MY. 1993. Pathway of proton transfer in bacterial reaction centers: Second-site mutation Asn-M44 → Asn mutant of Rhodobacter sphaeroides. Proc Natl Acad Sci USA 90:1325-1329.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1325-1329
    • Rongey, S.H.1    Paddock, M.L.2    Feher, G.3    Okamura, M.Y.4
  • 38
    • 0015530586 scopus 로고
    • Determination of ΔpH in chloroplasts
    • Rottenberg H, Grunwald T. 1973. Determination of ΔpH in chloroplasts. Eur J Biochem 25:71-74.
    • (1973) Eur J Biochem , vol.25 , pp. 71-74
    • Rottenberg, H.1    Grunwald, T.2
  • 39
    • 0028918454 scopus 로고
    • Ion transport in the gramicidin channel: Molecular dynamics study of single and double occupancy
    • Roux B, Prod'hom B, Karplus M. 1995. Ion transport in the gramicidin channel: Molecular dynamics study of single and double occupancy. Biophys J 68:876-892.
    • (1995) Biophys J , vol.68 , pp. 876-892
    • Roux, B.1    Prod'hom, B.2    Karplus, M.3
  • 40
    • 0015909175 scopus 로고
    • Nitrogen-carbon linkage isomerism of histidine in ruthenium ammine complexes
    • Sundberg RJ, Gupta G. 1973. Nitrogen-carbon linkage isomerism of histidine in ruthenium ammine complexes. Biomorganic Chem 3:39-48.
    • (1973) Biomorganic Chem , vol.3 , pp. 39-48
    • Sundberg, R.J.1    Gupta, G.2
  • 41
    • 0025169243 scopus 로고
    • L213 in the proton transfer pathway to the secondary quinone of reaction centers from Rhodobacter sphaeroides
    • L213 in the proton transfer pathway to the secondary quinone of reaction centers from Rhodobacter sphaeroides. Biochim Biophys Acta 1020:107-111.
    • (1990) Biochim Biophys Acta , vol.1020 , pp. 107-111
    • Takahashi, E.1    Wraight, C.A.2
  • 44
    • 0028095182 scopus 로고
    • Buried waters and internal cavities in monomeric proteins
    • Williams MA, Goodfellow JM, Thornton JM. 1994. Buried waters and internal cavities in monomeric proteins. Protein Sci 3:1224-1235.
    • (1994) Protein Sci , vol.3 , pp. 1224-1235
    • Williams, M.A.1    Goodfellow, J.M.2    Thornton, J.M.3
  • 45
    • 0014096443 scopus 로고
    • The proton dissociation constant of pyrrole, indole and related compounds
    • Yagil G. 1967. The proton dissociation constant of pyrrole, indole and related compounds. Tetrahedron 23:2855-2861.
    • (1967) Tetrahedron , vol.23 , pp. 2855-2861
    • Yagil, G.1


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