메뉴 건너뛰기




Volumn 91, Issue 10, 2006, Pages 3707-3717

Dynamics and diffusion in photosynthetic membranes from Rhodospirillum photometricum

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOCHLOROPHYLL; QUINONE DERIVATIVE;

EID: 33751257776     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.083709     Document Type: Article
Times cited : (30)

References (47)
  • 4
    • 28944431668 scopus 로고    scopus 로고
    • Architecture of the native photosynthetic apparatus of Phaeospirillum molischianum
    • Gonçalves, R. P., A. Bernadac, J. N. Sturgis, and S. Scheuring. 2005. Architecture of the native photosynthetic apparatus of Phaeospirillum molischianum. J. Struct. Biol. 152:221-228.
    • (2005) J. Struct. Biol. , vol.152 , pp. 221-228
    • Gonçalves, R.P.1    Bernadac, A.2    Sturgis, J.N.3    Scheuring, S.4
  • 5
    • 12544254339 scopus 로고    scopus 로고
    • Structure of the dimeric PufX-containing core complex of Rhodobacter blasticus by in situ AFM
    • Scheuring, S., J. Busselez, and D. Levy. 2005. Structure of the dimeric PufX-containing core complex of Rhodobacter blasticus by in situ AFM. J. Biol. Chem. 180:1426-1431.
    • (2005) J. Biol. Chem. , vol.180 , pp. 1426-1431
    • Scheuring, S.1    Busselez, J.2    Levy, D.3
  • 6
    • 33645100807 scopus 로고    scopus 로고
    • The photosynthetic apparatus of Rhodopseudomonas palustris: Structures and organization
    • Scheuring, S., R. P. Gonçalves, V. Prima, and J. N. Sturgis. 2006. The photosynthetic apparatus of Rhodopseudomonas palustris: structures and organization. J. Mol. Biol. 358:83-96.
    • (2006) J. Mol. Biol. , vol.358 , pp. 83-96
    • Scheuring, S.1    Gonçalves, R.P.2    Prima, V.3    Sturgis, J.N.4
  • 7
    • 9144264281 scopus 로고    scopus 로고
    • Variable LH2 stoichiometry and core clustering in native membranes of Rhodospirillum photometricum
    • Scheuring, S., J.-L. Rigaud, and J. N. Sturgis. 2004. Variable LH2 stoichiometry and core clustering in native membranes of Rhodospirillum photometricum. EMBO J. 23:4127-4133.
    • (2004) EMBO J. , vol.23 , pp. 4127-4133
    • Scheuring, S.1    Rigaud, J.-L.2    Sturgis, J.N.3
  • 8
    • 0037452675 scopus 로고    scopus 로고
    • Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core-complex in native membranes by AFM
    • Scheuring, S., J. Seguin, S. Marco, D. Lévy, B. Robert, and J.-L. Rigaud. 2003. Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core-complex in native membranes by AFM. Proc. Natl. Acad. Sci. USA. 100:1690-1693.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1690-1693
    • Scheuring, S.1    Seguin, J.2    Marco, S.3    Lévy, D.4    Robert, B.5    Rigaud, J.-L.6
  • 9
    • 22344456559 scopus 로고    scopus 로고
    • Chromatic adaptation of photosynthetic membranes
    • Scheuring, S., and J. N. Sturgis. 2005. Chromatic adaptation of photosynthetic membranes. Science. 309:484-487.
    • (2005) Science , vol.309 , pp. 484-487
    • Scheuring, S.1    Sturgis, J.N.2
  • 11
    • 0342907750 scopus 로고
    • Structure of a bacterial photosynthetic membrane
    • Miller, K. R. 1979. Structure of a bacterial photosynthetic membrane. Proc. Natl. Acad. Sci. USA. 76:6415-6419.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 6415-6419
    • Miller, K.R.1
  • 12
    • 0002249157 scopus 로고
    • Three-dimensional structure of a photosynthetic membrane
    • Miller, K. R. 1982. Three-dimensional structure of a photosynthetic membrane. Nature. 300:53-55.
    • (1982) Nature , vol.300 , pp. 53-55
    • Miller, K.R.1
  • 13
    • 0022386598 scopus 로고
    • The Rhodopseudomonas viridis photosynthetic membrane: Arrangement in situ
    • Miller, K. R., and J. S. Jacob. 1985. The Rhodopseudomonas viridis photosynthetic membrane: arrangement in situ. Arch. Microbiol. 142:333-339.
    • (1985) Arch. Microbiol. , vol.142 , pp. 333-339
    • Miller, K.R.1    Jacob, J.S.2
  • 14
    • 0033081638 scopus 로고    scopus 로고
    • Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides
    • Jungas, C., J.-L. Ranck, J.-L. Rigaud, P. Joliot, and A. Vermeglio. 1999. Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides. EMBO J. 18:534-542.
    • (1999) EMBO J. , vol.18 , pp. 534-542
    • Jungas, C.1    Ranck, J.-L.2    Rigaud, J.-L.3    Joliot, P.4    Vermeglio, A.5
  • 15
    • 0942287196 scopus 로고    scopus 로고
    • Structural role of PufX in the dimerization of the photosynthetic core-complex of Rhodobacter sphaeroides
    • Scheuring, S., F. Francia, J. Busselez, B. Melandri, J.-L. Rigaud, and D. Lévy. 2004. Structural role of PufX in the dimerization of the photosynthetic core-complex of Rhodobacter sphaeroides. J. Biol. Chem. 279:3620-3626.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3620-3626
    • Scheuring, S.1    Francia, F.2    Busselez, J.3    Melandri, B.4    Rigaud, J.-L.5    Lévy, D.6
  • 16
    • 20344374627 scopus 로고    scopus 로고
    • The 8.5 Å projection structure of the core RC-LH1-PufX dimer of Rhodobacter sphaeroides
    • Qian, P., C. N. Hunter, and P. A. Bullough. 2005. The 8.5 Å projection structure of the core RC-LH1-PufX dimer of Rhodobacter sphaeroides. J. Mol. Biol. 349:948-960.
    • (2005) J. Mol. Biol. , vol.349 , pp. 948-960
    • Qian, P.1    Hunter, C.N.2    Bullough, P.A.3
  • 18
    • 20444382012 scopus 로고    scopus 로고
    • Watching the components of photosynthetic bacterial membranes and their "in situ" organization by atomic force microscopy
    • Scheuring, S., D. Levy, and J.-L. Rigaud. 2005. Watching the components of photosynthetic bacterial membranes and their "in situ" organization by atomic force microscopy. Biochim. Biophys. Acta. 1712:109-127.
    • (2005) Biochim. Biophys. Acta , vol.1712 , pp. 109-127
    • Scheuring, S.1    Levy, D.2    Rigaud, J.-L.3
  • 19
    • 27644585264 scopus 로고    scopus 로고
    • Localization of coenzyme Q(10) in the center of a deuterated lipid membrane by neutron diffraction
    • Hauss, T., S. Dante, T. H. Haines, and N. A. Dencher. 2005. Localization of coenzyme Q(10) in the center of a deuterated lipid membrane by neutron diffraction. Biochim. Biophys. Acta. 1710:57-62.
    • (2005) Biochim. Biophys. Acta , vol.1710 , pp. 57-62
    • Hauss, T.1    Dante, S.2    Haines, T.H.3    Dencher, N.A.4
  • 20
    • 0000786989 scopus 로고
    • Evidence for super-complexes between reaction centers, cytochrome c2 and cytochrome bc1 complex in Rhodobacter sphaeroides whole cells
    • Joliot, P., A. Vermeglio, and A. Joliot. 1989. Evidence for super-complexes between reaction centers, cytochrome c2 and cytochrome bc1 complex in Rhodobacter sphaeroides whole cells. Biochim. Biophys. Acta. 975:336-345.
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 336-345
    • Joliot, P.1    Vermeglio, A.2    Joliot, A.3
  • 21
    • 15744405284 scopus 로고    scopus 로고
    • Functional consequences of the organization of the photosynthetic apparatus in R. sphaeroides: 2. A study of PufX-membranes
    • Comayras, F., C. Jungas, and J. Lavergne. 2005. Functional consequences of the organization of the photosynthetic apparatus in R. sphaeroides: 2. A study of PufX-membranes. J. Biol. Chem. 280:11214-11223.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11214-11223
    • Comayras, F.1    Jungas, C.2    Lavergne, J.3
  • 22
    • 15744401383 scopus 로고    scopus 로고
    • Functional consequences of the organization of the photosynthetic apparatus in R. sphaeroides: 1. Quinone domains and excitation transfer in chromatophores and reaction center-antenna complexes
    • Comayras, F., C. Jungas, and J. Lavergne. 2005. Functional consequences of the organization of the photosynthetic apparatus in R. sphaeroides: 1. Quinone domains and excitation transfer in chromatophores and reaction center-antenna complexes. J. Biol. Chem. 280:11203-11213.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11203-11213
    • Comayras, F.1    Jungas, C.2    Lavergne, J.3
  • 23
    • 13444287778 scopus 로고    scopus 로고
    • Fast oxidation of the primary electron acceptor under anaerobic conditions requires the organization of the photosynthetic chain of Rhodobacter sphaeroides in supercomplexes
    • Joliot, P., A. Joliot, and A. Vermeglio. 2005. Fast oxidation of the primary electron acceptor under anaerobic conditions requires the organization of the photosynthetic chain of Rhodobacter sphaeroides in supercomplexes. Biochim. Biophys. Acta. 1706:204-214.
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 204-214
    • Joliot, P.1    Joliot, A.2    Vermeglio, A.3
  • 24
    • 0034691753 scopus 로고    scopus 로고
    • Control of the photosynthetic electron transport by PQ diffusion microdomains in thylakoids of higher plants
    • Kirchhoff, H., S. Horstmann, and E. Weis. 2000. Control of the photosynthetic electron transport by PQ diffusion microdomains in thylakoids of higher plants. Biochim. Biophys. Acta. 1459:148-168.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 148-168
    • Kirchhoff, H.1    Horstmann, S.2    Weis, E.3
  • 25
  • 26
    • 0024723988 scopus 로고
    • Lateral diffusion in an archipelago. Distance dependence of the diffusion coefficient
    • Saxton, M. J. 1989. Lateral diffusion in an archipelago. Distance dependence of the diffusion coefficient. Biophys. J. 56:615-622.
    • (1989) Biophys. J. , vol.56 , pp. 615-622
    • Saxton, M.J.1
  • 27
    • 0025084901 scopus 로고
    • Lateral diffusion in a mixture of mobile and immobile particles. A Monte Carlo study
    • Saxton, M. J. 1990. Lateral diffusion in a mixture of mobile and immobile particles. A Monte Carlo study. Biophys. J. 58:1303-1306.
    • (1990) Biophys. J. , vol.58 , pp. 1303-1306
    • Saxton, M.J.1
  • 28
    • 0027163092 scopus 로고
    • Lateral diffusion in an archipelago. Dependence on tracer size
    • Saxton, M. J. 1993. Lateral diffusion in an archipelago. Dependence on tracer size. Biophys. J. 64:1053-1062.
    • (1993) Biophys. J. , vol.64 , pp. 1053-1062
    • Saxton, M.J.1
  • 29
    • 0027197103 scopus 로고
    • Lateral diffusion in an archipelago. Single-particle diffusion
    • Saxton, M. J. 1993. Lateral diffusion in an archipelago. Single-particle diffusion. Biophys. J. 64:1766-1780.
    • (1993) Biophys. J. , vol.64 , pp. 1766-1780
    • Saxton, M.J.1
  • 30
    • 0028140412 scopus 로고
    • Anomalous diffusion due to obstacles: A Monte Carlo study
    • Saxton, M. J. 1994. Anomalous diffusion due to obstacles: a Monte Carlo study. Biophys. J. 66:394-401.
    • (1994) Biophys. J. , vol.66 , pp. 394-401
    • Saxton, M.J.1
  • 31
    • 0034805503 scopus 로고    scopus 로고
    • Anomalous subdiffusion in fluorescence photobleaching recovery: A Monte Carlo study
    • Saxton, M. J. 2001. Anomalous subdiffusion in fluorescence photobleaching recovery: a Monte Carlo study. Biophys. J. 81:2226-2240.
    • (2001) Biophys. J. , vol.81 , pp. 2226-2240
    • Saxton, M.J.1
  • 32
    • 0028584124 scopus 로고
    • Influence of obstacles on lipid lateral diffusion: Computer simulation of FRAP experiments and application to proteoliposomes and biomembranes
    • Schram, V., J. F. Tocanne, and A. Lopez. 1994. Influence of obstacles on lipid lateral diffusion: computer simulation of FRAP experiments and application to proteoliposomes and biomembranes. Eur. Biophys. J. 23:337-348.
    • (1994) Eur. Biophys. J. , vol.23 , pp. 337-348
    • Schram, V.1    Tocanne, J.F.2    Lopez, A.3
  • 33
    • 0345170107 scopus 로고    scopus 로고
    • Dependence of plastoquinol diffusion on the shape, size and density of integral thylakoid proteins
    • Tremmel, I. G., H. Kirchhoff, E. Weiss, and G. D. Farquhar. 2003. Dependence of plastoquinol diffusion on the shape, size and density of integral thylakoid proteins. Biochim. Biophys. Acta. 1607:97-109.
    • (2003) Biochim. Biophys. Acta , vol.1607 , pp. 97-109
    • Tremmel, I.G.1    Kirchhoff, H.2    Weiss, E.3    Farquhar, G.D.4
  • 34
    • 3142776351 scopus 로고    scopus 로고
    • Supramolecular photosystem II organisation in grana thylakoid membranes: Evidence for a structured arrangement
    • Kirchhoff, H., I. Tremmel, W. Haase, and U. Kubitscheck. 2004. Supramolecular photosystem II organisation in grana thylakoid membranes: evidence for a structured arrangement. Biochemistry. 43:9204-9213.
    • (2004) Biochemistry , vol.43 , pp. 9204-9213
    • Kirchhoff, H.1    Tremmel, I.2    Haase, W.3    Kubitscheck, U.4
  • 35
    • 0027504198 scopus 로고
    • Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells
    • Kusumi, A., Y. Sako, and M. Yamamoto. 1993. Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells. Biophys. J. 65:2021-2040.
    • (1993) Biophys. J. , vol.65 , pp. 2021-2040
    • Kusumi, A.1    Sako, Y.2    Yamamoto, M.3
  • 36
    • 21244494104 scopus 로고    scopus 로고
    • Detection of non-Brownian diffusion in the cell membrane in single molecule tracking
    • Ritchie, K., X. Y. Shan, J. Kondo, K. Iwasawa, T. Fujiwara, and A. Kusumi. 2005. Detection of non-Brownian diffusion in the cell membrane in single molecule tracking. Biophys. J. 88:2266-2277.
    • (2005) Biophys. J. , vol.88 , pp. 2266-2277
    • Ritchie, K.1    Shan, X.Y.2    Kondo, J.3    Iwasawa, K.4    Fujiwara, T.5    Kusumi, A.6
  • 37
    • 0032563615 scopus 로고    scopus 로고
    • Regulation mechanism of the lateral diffusion of band 3 in erythrocyte membranes by the membrane skeleton
    • Tomishige, M., Y. Sako, and A. Kusumi. 1998. Regulation mechanism of the lateral diffusion of band 3 in erythrocyte membranes by the membrane skeleton. J. Cell Biol. 142:989-1000.
    • (1998) J. Cell Biol. , vol.142 , pp. 989-1000
    • Tomishige, M.1    Sako, Y.2    Kusumi, A.3
  • 38
    • 28444443820 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy diffusion laws to probe the submicron cell membrane organization
    • Wawrezinieck, L., H. Rigneault, D. Marguet, and P.-F. Lenne. 2005. Fluorescence correlation spectroscopy diffusion laws to probe the submicron cell membrane organization. Biophys. J. 89:4029-4042.
    • (2005) Biophys. J. , vol.89 , pp. 4029-4042
    • Wawrezinieck, L.1    Rigneault, H.2    Marguet, D.3    Lenne, P.-F.4
  • 39
    • 0028020713 scopus 로고
    • Reproducible acquisition of Escherichia coli porin surface topographs by atomic force microscopy
    • Schabert, F. A., and A. Engel. 1994. Reproducible acquisition of Escherichia coli porin surface topographs by atomic force microscopy. Biophys. J. 67:2394-2403.
    • (1994) Biophys. J. , vol.67 , pp. 2394-2403
    • Schabert, F.A.1    Engel, A.2
  • 42
    • 4444384368 scopus 로고    scopus 로고
    • The hexatic phase of the two-dimensional hard disk system
    • Jaster, A. 2004. The hexatic phase of the two-dimensional hard disk system. Phys. Lett. A. 330:120-125.
    • (2004) Phys. Lett. A , vol.330 , pp. 120-125
    • Jaster, A.1
  • 43
    • 0032311227 scopus 로고    scopus 로고
    • Molecular crowding: Analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion
    • Minton, A. P. 1998. Molecular crowding: analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion. Methods Enzymol. 295:127-149.
    • (1998) Methods Enzymol. , vol.295 , pp. 127-149
    • Minton, A.P.1
  • 44
    • 0025278396 scopus 로고
    • Energy-transfer dynamics in three light-harvesting mutants of Rhodobacter sphaeroides: A picosecond spectroscopy study
    • Hunter, C. N., H. Bergstrom, R. van Grondelle, and V. Sundstrom. 1990. Energy-transfer dynamics in three light-harvesting mutants of Rhodobacter sphaeroides: a picosecond spectroscopy study. Biochem. 29:3203-3207.
    • (1990) Biochem. , vol.29 , pp. 3203-3207
    • Hunter, C.N.1    Bergstrom, H.2    Van Grondelle, R.3    Sundstrom, V.4
  • 45
    • 0027179313 scopus 로고
    • Picosecond dynamics of excitations in light-harvesting complex B800-850 from Chromatium minutissimum studied using fluorescence spectrochronography
    • Godik, V., K. Timpmann, A. Freiberg, and A. A. Moskalenko. 1993. Picosecond dynamics of excitations in light-harvesting complex B800-850 from Chromatium minutissimum studied using fluorescence spectrochronography. FEBS Lett. 327:68-70.
    • (1993) FEBS Lett. , vol.327 , pp. 68-70
    • Godik, V.1    Timpmann, K.2    Freiberg, A.3    Moskalenko, A.A.4
  • 46
    • 1942423239 scopus 로고    scopus 로고
    • In vitro self assembly of the light harvesting pigment protein LH2 revealed by ultrafast spectroscopy and electron microscopy
    • Schubert, A., A. Stenstam, W. J. D. Beenken, J. L. Harek, R. Cogdell, T. Pullerits, and V. Sundström. 2004. In vitro self assembly of the light harvesting pigment protein LH2 revealed by ultrafast spectroscopy and electron microscopy. Biophys. J. 86:2363-2373.
    • (2004) Biophys. J. , vol.86 , pp. 2363-2373
    • Schubert, A.1    Stenstam, A.2    Beenken, W.J.D.3    Harek, J.L.4    Cogdell, R.5    Pullerits, T.6    Sundström, V.7
  • 47
    • 0035909829 scopus 로고    scopus 로고
    • Dynamics of excitation energy transfer in the LH1 and LH2 light-harvesting complexes of photosynthetic bacteria
    • van Grondelle, R., and V. Novoderezhkin. 2001. Dynamics of excitation energy transfer in the LH1 and LH2 light-harvesting complexes of photosynthetic bacteria. Biochem. 40:15057-15068.
    • (2001) Biochem. , vol.40 , pp. 15057-15068
    • Van Grondelle, R.1    Novoderezhkin, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.