메뉴 건너뛰기




Volumn 9, Issue 3, 2004, Pages 130-137

Cytochrome b6f: Structure for signalling and vectorial metabolism

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B6F; LIGAND; PLASTOQUINONE; PROTON PUMP; VEGETABLE PROTEIN;

EID: 1542321529     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tplants.2004.01.009     Document Type: Review
Times cited : (69)

References (50)
  • 1
    • 0344497439 scopus 로고    scopus 로고
    • 6f complex
    • 6f complex. Nature. 426:2003;413-418.
    • (2003) Nature , vol.426 , pp. 413-418
    • Stroebel, D.1
  • 2
    • 0242494128 scopus 로고    scopus 로고
    • Structure of the cytochrome b6f complex of oxygenic photosynthesis: Tuning the cavity
    • Kurisu G., et al. Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity. Science. 302:2003;1009-1014.
    • (2003) Science , vol.302 , pp. 1009-1014
    • Kurisu, G.1
  • 3
    • 0000055138 scopus 로고
    • Function of the two cytochrome components in chloroplasts - A working hypothesis
    • Hill R., Bendall F. Function of the two cytochrome components in chloroplasts - a working hypothesis. Nature. 186:1960;136-137.
    • (1960) Nature , vol.186 , pp. 136-137
    • Hill, R.1    Bendall, F.2
  • 4
    • 0037268248 scopus 로고    scopus 로고
    • Cyclic, pseudocyclic and noncyclic photophosphorylation: New links in the chain
    • Allen J.F. Cyclic, pseudocyclic and noncyclic photophosphorylation: new links in the chain. Trends Plant Sci. 8:2003;15-19.
    • (2003) Trends Plant Sci. , vol.8 , pp. 15-19
    • Allen, J.F.1
  • 5
    • 0036550933 scopus 로고    scopus 로고
    • The Z-scheme - Down hill all the way
    • Walker D.A. The Z-scheme - down hill all the way. Trends Plant Sci. 7:2002;183-185.
    • (2002) Trends Plant Sci. , vol.7 , pp. 183-185
    • Walker, D.A.1
  • 6
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • Mitchell P. Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature. 191:1961;144.
    • (1961) Nature , vol.191 , pp. 144
    • Mitchell, P.1
  • 7
    • 3042728346 scopus 로고    scopus 로고
    • Protons, proteins and ATP
    • (in press).
    • Junge, W. Protons, proteins and ATP. Photosynth. Res. (in press).
    • Photosynth. Res.
    • Junge, W.1
  • 8
    • 0037421839 scopus 로고    scopus 로고
    • Chemiosmotic coupling: The cost of living
    • Rich P. Chemiosmotic coupling: the cost of living. Nature. 421:2003;583.
    • (2003) Nature , vol.421 , pp. 583
    • Rich, P.1
  • 9
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of protonmotive function of cytochrome systems
    • Mitchell P. Possible molecular mechanisms of protonmotive function of cytochrome systems. J. Theor. Biol. 62:1976;327-367.
    • (1976) J. Theor. Biol. , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 10
    • 0016754421 scopus 로고
    • The protonmotive Q cycle: A general formulation
    • Mitchell P. The protonmotive Q cycle: a general formulation. FEBS Lett. 59:1975;137-139.
    • (1975) FEBS Lett. , vol.59 , pp. 137-139
    • Mitchell, P.1
  • 11
    • 3042767574 scopus 로고    scopus 로고
    • The Q-cycle, a personal perspective
    • (in press).
    • Crofts, A.R. The Q-cycle, a personal perspective. Photosynth. Res. (in press).
    • Photosynth. Res.
    • Crofts, A.R.1
  • 12
    • 0037047319 scopus 로고    scopus 로고
    • Photosynthesis of ATP-electrons, proton pumps, rotors, and poise
    • Allen J. Photosynthesis of ATP-electrons, proton pumps, rotors, and poise. Cell. 110:2002;273-276.
    • (2002) Cell , vol.110 , pp. 273-276
    • Allen, J.1
  • 13
    • 0033609010 scopus 로고    scopus 로고
    • ATP synthase and other motor proteins
    • Junge W. ATP synthase and other motor proteins. Proc. Natl. Acad. Sci. U. S. A. 96:1999;4735-4737.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4735-4737
    • Junge, W.1
  • 14
    • 0037471678 scopus 로고    scopus 로고
    • The redox protein construction kit: Pre-last universal common ancestor evolution of energy-conserving enzymes
    • Baymann F., et al. The redox protein construction kit: pre-last universal common ancestor evolution of energy-conserving enzymes. Philos. Trans. R. Soc. London Ser. B Biol. Sci. 358:2003;267-274.
    • (2003) Philos. Trans. R. Soc. London Ser. B Biol. Sci. , vol.358 , pp. 267-274
    • Baymann, F.1
  • 15
    • 0034697992 scopus 로고    scopus 로고
    • Early evolution of Cytochrome bc complexes
    • Schutz M., et al. Early evolution of Cytochrome bc complexes. J. Mol. Biol. 300:2000;663-675.
    • (2000) J. Mol. Biol. , vol.300 , pp. 663-675
    • Schutz, M.1
  • 16
    • 1542368744 scopus 로고    scopus 로고
    • On the origins of cells. An hypothesis for the evolutionary transitions from abiotic geochemistry to chemoautotrophic prokaryotes, and from prokaryotes to nucleated cells
    • (in press).
    • Martin, W. and Russell, M.J. On the origins of cells. An hypothesis for the evolutionary transitions from abiotic geochemistry to chemoautotrophic prokaryotes, and from prokaryotes to nucleated cells. Philos. Trans. R. Soc. London Ser. B Biol. Sci. (in press).
    • Philos. Trans. R. Soc. London Ser. B Biol. Sci.
    • Martin, W.1    Russell, M.J.2
  • 17
    • 1542339055 scopus 로고    scopus 로고
    • On the dissipation of thermal and chemical energies on the early Earth
    • R. et al. Ikan. Kluwer Academic Publishers
    • Russell M.J., et al. On the dissipation of thermal and chemical energies on the early Earth. Ikan R., et al. Natural and Laboratory Simulated Thermal Geochemical Processes. 2003;325-388 Kluwer Academic Publishers.
    • (2003) Natural and Laboratory Simulated Thermal Geochemical Processes , pp. 325-388
    • Russell, M.J.1
  • 18
    • 0035399478 scopus 로고    scopus 로고
    • Large scale domain movement in Cytochrome bc(1): A new device for electron transfer in proteins
    • Darrouzet E., et al. Large scale domain movement in Cytochrome bc(1): a new device for electron transfer in proteins. Trends Biochem. Sci. 26:2001;445-451.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 445-451
    • Darrouzet, E.1
  • 20
    • 0030596417 scopus 로고    scopus 로고
    • Separate sexes and the mitochondrial theory of ageing
    • Allen J.F. Separate sexes and the mitochondrial theory of ageing. J. Theor. Biol. 180:1996;135-140.
    • (1996) J. Theor. Biol. , vol.180 , pp. 135-140
    • Allen, J.F.1
  • 21
    • 1342325555 scopus 로고    scopus 로고
    • Reversible redox energy coupling in electron transfer chains
    • Osyczka, A. et al. (2004) Reversible redox energy coupling in electron transfer chains. Nature 427, 607-612.
    • (2004) Nature , vol.427 , pp. 607-612
    • Osyczka, A.1
  • 22
    • 0026444410 scopus 로고
    • Pro- and antioxidant functions of quinones and quinone reductases in mammalian cells
    • Cadenas E., et al. Pro- and antioxidant functions of quinones and quinone reductases in mammalian cells. Adv. Enzymol. Relat. Areas Mol. Biol. 65:1992;97-146.
    • (1992) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.65 , pp. 97-146
    • Cadenas, E.1
  • 23
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B., et al. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59:1979;527-605.
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1
  • 24
    • 0037298085 scopus 로고    scopus 로고
    • Participation of photosynthetic electron transport in production and scavenging of reactive oxygen species
    • Ivanov B., Khorobrykh S. Participation of photosynthetic electron transport in production and scavenging of reactive oxygen species. Antioxid. Redox Signal. 5:2003;43-53.
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 43-53
    • Ivanov, B.1    Khorobrykh, S.2
  • 25
    • 0029933923 scopus 로고    scopus 로고
    • Free-radical-induced mutation vs redox regulation: Costs and benefits of genes in organelles
    • Allen J.F., Raven J.A. Free-radical-induced mutation vs redox regulation: costs and benefits of genes in organelles. J. Mol. Evol. 42:1996;482-492.
    • (1996) J. Mol. Evol. , vol.42 , pp. 482-492
    • Allen, J.F.1    Raven, J.A.2
  • 26
    • 0031863230 scopus 로고    scopus 로고
    • Fluorescence and absorption spectroscopy of the weakly fluorescent chlorophyll a in cytochrome b6f of Synechocystis PCC6803
    • Peterman E.J., et al. Fluorescence and absorption spectroscopy of the weakly fluorescent chlorophyll a in cytochrome b6f of Synechocystis PCC6803. Biophys. J. 75:1998;389-398.
    • (1998) Biophys. J. , vol.75 , pp. 389-398
    • Peterman, E.J.1
  • 27
    • 0030824327 scopus 로고    scopus 로고
    • On the presence and role of a molecule of chlorophyll a in the cytochrome b6f complex
    • Pierre Y., et al. On the presence and role of a molecule of chlorophyll a in the cytochrome b6f complex. J. Biol. Chem. 272:1997;21901-21908.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21901-21908
    • Pierre, Y.1
  • 28
    • 0033556297 scopus 로고    scopus 로고
    • Stoichiometrically bound β-carotene in the cytochrome b6f complex of oxygenic photosynthesis protects against oxygen damage
    • Zhang H., et al. Stoichiometrically bound β-carotene in the cytochrome b6f complex of oxygenic photosynthesis protects against oxygen damage. J. Biol. Chem. 274:1999;1581-1587.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1581-1587
    • Zhang, H.1
  • 29
    • 0036414764 scopus 로고    scopus 로고
    • A cytochrome b origin of photosynthetic reaction centers: An evolutionary link between respiration and photosynthesis
    • Xiong J., Bauer C.E. A cytochrome b origin of photosynthetic reaction centers: an evolutionary link between respiration and photosynthesis. J. Mol. Biol. 322:2002;1025-1037.
    • (2002) J. Mol. Biol. , vol.322 , pp. 1025-1037
    • Xiong, J.1    Bauer, C.E.2
  • 30
    • 0031435688 scopus 로고    scopus 로고
    • Molecular genetic identification of a pathway for heme binding to cytochrome b6
    • Kuras R., et al. Molecular genetic identification of a pathway for heme binding to cytochrome b6. J. Biol. Chem. 272:1997;32427-32435.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32427-32435
    • Kuras, R.1
  • 33
    • 0028840368 scopus 로고
    • The cytochrome bc complex (menaquinone:cytochrome c reductase) in Bacillus subtilis has a nontraditional subunit organization
    • Yu J., et al. The cytochrome bc complex (menaquinone:cytochrome c reductase) in Bacillus subtilis has a nontraditional subunit organization. J. Bacteriol. 177:1995;6751-6760.
    • (1995) J. Bacteriol. , vol.177 , pp. 6751-6760
    • Yu, J.1
  • 34
    • 0032502756 scopus 로고    scopus 로고
    • Studies of the cytochrome subunits of menaquinone:cytochrome c reductase (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of heme to the cytochrome b subunit
    • Yu, J. and Le Brun, N.E. (1998) Studies of the cytochrome subunits of menaquinone:cytochrome c reductase (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of heme to the cytochrome b subunit. J. Biol. Chem. 273, 8860-8866.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8860-8866
    • Yu, J.1    Le Brun, N.E.2
  • 35
    • 36849155728 scopus 로고
    • Chloroplast protein-phosphorylation couples plastoquinone redox state to distribution of excitation-energy between photosystems
    • Allen J.F., et al. Chloroplast protein-phosphorylation couples plastoquinone redox state to distribution of excitation-energy between photosystems. Nature. 291:1981;25-29.
    • (1981) Nature , vol.291 , pp. 25-29
    • Allen, J.F.1
  • 36
    • 0026556851 scopus 로고
    • Protein phosphorylation in regulation of photosynthesis
    • Allen J.F. Protein phosphorylation in regulation of photosynthesis. Biochim. Biophys. Acta. 1098:1992;275-335.
    • (1992) Biochim. Biophys. Acta , vol.1098 , pp. 275-335
    • Allen, J.F.1
  • 37
    • 0035898532 scopus 로고    scopus 로고
    • State transitions reveal the dynamics and flexibility of the photosynthetic apparatus
    • Wollman F.A. State transitions reveal the dynamics and flexibility of the photosynthetic apparatus. EMBO J. 20:2001;3623-3630.
    • (2001) EMBO J. , vol.20 , pp. 3623-3630
    • Wollman, F.A.1
  • 38
    • 0033580325 scopus 로고    scopus 로고
    • Photosynthetic control of chloroplast gene expression
    • Pfannschmidt T., et al. Photosynthetic control of chloroplast gene expression. Nature. 397:1999;625-628.
    • (1999) Nature , vol.397 , pp. 625-628
    • Pfannschmidt, T.1
  • 39
    • 0037423885 scopus 로고    scopus 로고
    • Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas
    • Depège N., et al. Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas. Science. 299:2003;1572-1575.
    • (2003) Science , vol.299 , pp. 1572-1575
    • Depège, N.1
  • 40
    • 0037423884 scopus 로고    scopus 로고
    • Botany. State transitions - A question of balance
    • Allen J.F. Botany. State transitions - a question of balance. Science. 299:2003;1530-1532.
    • (2003) Science , vol.299 , pp. 1530-1532
    • Allen, J.F.1
  • 41
    • 0032479524 scopus 로고    scopus 로고
    • Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex
    • Iwata S., et al. Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex. Science. 281:1998;64-71.
    • (1998) Science , vol.281 , pp. 64-71
    • Iwata, S.1
  • 42
    • 0034660152 scopus 로고    scopus 로고
    • 1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment
    • 1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Structure Fold. Des. 8:2000;669-684.
    • (2000) Structure Fold. Des. , vol.8 , pp. 669-684
    • Hunte, C.1
  • 43
    • 0030867866 scopus 로고    scopus 로고
    • Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria
    • Xia D., et al. Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria. Science. 277:1997;60-66.
    • (1997) Science , vol.277 , pp. 60-66
    • Xia, D.1
  • 44
    • 0037267882 scopus 로고    scopus 로고
    • Chloroplast redox signals: How photosynthesis controls its own genes
    • Pfannschmidt T. Chloroplast redox signals: how photosynthesis controls its own genes. Trends Plant Sci. 8:2003;33-41.
    • (2003) Trends Plant Sci. , vol.8 , pp. 33-41
    • Pfannschmidt, T.1
  • 45
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • Jordan P., et al. Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature. 411:2001;909-917.
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1
  • 46
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • Zouni A., et al. Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature. 409:2001;739-743.
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1
  • 47
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-Å resolution
    • Kamiya N., Shen J.R. Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-Å resolution. Proc. Natl. Acad. Sci. U. S. A. 100:2003;98-103.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.R.2
  • 48
    • 0348148910 scopus 로고    scopus 로고
    • Crystal structure of plant photosystem I
    • Ben-Shem A., et al. Crystal structure of plant photosystem I. Nature. 426:2003;630-635.
    • (2003) Nature , vol.426 , pp. 630-635
    • Ben-Shem, A.1
  • 49
    • 0035910654 scopus 로고    scopus 로고
    • Electrogenic events associated with electron and proton transfers within the cytochrome b(6)/f complex
    • Joliot P., Joliot A. Electrogenic events associated with electron and proton transfers within the cytochrome b(6)/f complex. Biochim. Biophys. Acta. 1503:2001;369-376.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 369-376
    • Joliot, P.1    Joliot, A.2
  • 50
    • 0000577528 scopus 로고    scopus 로고
    • Chimera: An extensible molecular modeling application constructed using standard components
    • Huang C.C., et al. Chimera: an extensible molecular modeling application constructed using standard components. Pacific Symposium on Biocomputing. 1:1996;724.
    • (1996) Pacific Symposium on Biocomputing , vol.1 , pp. 724
    • Huang, C.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.