메뉴 건너뛰기




Volumn 104, Issue 1-2, 2011, Pages 19-34

Lipids in photosystem II: Multifunctional cofactors

Author keywords

Lipid cofactor interactions; Lipid protein interactions; Lipids; Photosystem II; Water oxidation

Indexed keywords

CAROTENOID; CHLOROPHYLL; HOMODIMER; LIPID; MEMBRANE PROTEIN; MONOMER; OXYGEN; PLASTOQUINONE;

EID: 79958017528     PISSN: 10111344     EISSN: 18732682     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2011.02.025     Document Type: Review
Times cited : (44)

References (76)
  • 1
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial photosystem II at 2.9-angstrom resolution and the role of quinones, lipids, channels and chloride
    • A. Guskov, J. Kern, A. Gabdulkhakov, M. Broser, A. Zouni, and W. Saenger Cyanobacterial photosystem II at 2.9-angstrom resolution and the role of quinones, lipids, channels and chloride Nat. Struct. Mol. Biol. 16 2009 334 342
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 334-342
    • Guskov, A.1    Kern, J.2    Gabdulkhakov, A.3    Broser, M.4    Zouni, A.5    Saenger, W.6
  • 2
    • 33745197457 scopus 로고    scopus 로고
    • Photosystem II: The light-driven water:plastoquinone oxidoreductase
    • Govindjee Springer Dordrecht, The Netherlands
    • T. Wydrzynski, and K. Satoh Photosystem II: the light-driven water:plastoquinone oxidoreductase Govindjee Advances in Photosynthesis 2005 Springer Dordrecht, The Netherlands
    • (2005) Advances in Photosynthesis
    • Wydrzynski, T.1    Satoh, K.2
  • 3
    • 36849071982 scopus 로고    scopus 로고
    • Photosystem II: Structure and mechanism of the water:plastoquinone oxidoreductase
    • DOI 10.1007/s11120-007-9201-1, Govindjee Special Issue: Part B, Celebrating Govindjee's 50 Years in Photosynthesis Research and his 75th Birthday
    • J. Kern, and G. Renger Photosystem II: structure and mechanism of the water:plastoquinone oxidoreductase Photosynth. Res. 94 2007 183 202 (Pubitemid 350229101)
    • (2007) Photosynthesis Research , vol.94 , Issue.2-3 , pp. 183-202
    • Kern, J.1    Renger, G.2
  • 4
    • 33751287149 scopus 로고    scopus 로고
    • Photosystem II: An enzyme of global significance
    • DOI 10.1042/BST0340619
    • J. Barber Photosystem II: an enzyme of global significance Biochem. Soc. Trans. 34 2006 619 631 (Pubitemid 44796391)
    • (2006) Biochemical Society Transactions , vol.34 , Issue.5 , pp. 619-631
    • Barber, J.1
  • 5
    • 0001213161 scopus 로고
    • Pigment-protein interactions in the photosynthetic reaction centre from Rhodopseudomonas viridis
    • H. Michel, O. Epp, and J. Deisenhofer Pigment-protein interactions in the photosynthetic reaction centre from Rhodopseudomonas viridis EMBO J. 5 1986 2445 2451
    • (1986) EMBO J. , vol.5 , pp. 2445-2451
    • Michel, H.1    Epp, O.2    Deisenhofer, J.3
  • 6
    • 25444445784 scopus 로고    scopus 로고
    • The antenna system of photosystem II from Thermosynechococcus elongatus at 3.2 A resolution
    • DOI 10.1007/s11120-005-4117-0
    • B. Loll, J. Kern, A. Zouni, W. Saenger, J. Biesiadka, and K.D. Irrgang The antenna system of photosystem II from Thermosynechococcus elongatus at 3.2 angstrom resolution Photosynth. Res. 86 2005 175 184 (Pubitemid 41361272)
    • (2005) Photosynthesis Research , vol.86 , Issue.1-2 , pp. 175-184
    • Loll, B.1    Kern, J.2    Zouni, A.3    Saenger, W.4    Biesiadka, J.5    Irrgang, K.-D.6
  • 7
    • 40849139152 scopus 로고    scopus 로고
    • Crystal structure of cyanobacterial photosystem II at 3.0 resolution: A closer look at the antenna system and the small membrane-intrinsic subunits
    • F. Müh, T. Renger, and A. Zouni Crystal structure of cyanobacterial photosystem II at 3.0 resolution: a closer look at the antenna system and the small membrane-intrinsic subunits Plant Physiol. Biochem. 46 2008 238 264
    • (2008) Plant Physiol. Biochem. , vol.46 , pp. 238-264
    • Müh, F.1    Renger, T.2    Zouni, A.3
  • 8
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobaoterial photosystem I at 2.5 A resolution
    • DOI 10.1038/35082000
    • P. Jordan, P. Fromme, H.T. Witt, O. Klukas, W. Saenger, and N. Krauss Three-dimensional structure of cyanobacterial photosystem I at 2.5 resolution Nature 411 2001 909 917 (Pubitemid 32601481)
    • (2001) Nature , vol.411 , Issue.6840 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 10
    • 77956154786 scopus 로고    scopus 로고
    • Structure of CyanoP at 2.8 angstrom: Implications for the evolution and function of the PsbP subunit of photosystem II
    • F. Michoux, K. Takasaka, M. Boehm, P.J. Nixon, and J.W. Murray Structure of CyanoP at 2.8 angstrom: implications for the evolution and function of the PsbP subunit of photosystem II Biochemistry 49 2010 7411 7413
    • (2010) Biochemistry , vol.49 , pp. 7411-7413
    • Michoux, F.1    Takasaka, K.2    Boehm, M.3    Nixon, P.J.4    Murray, J.W.5
  • 11
    • 84891372882 scopus 로고    scopus 로고
    • Crystal structure of PsbQ from Synechocystis sp. PCC 6803 at 1.8 : Implications for binding and function in cyanobacterial photosystem II
    • S.A. Jackson, R.D. Fagerlund, S.M. Wilbanks, and J.J. Eaton-Rye Crystal structure of PsbQ from Synechocystis sp. PCC 6803 at 1.8 : Implications for binding and function in cyanobacterial photosystem II Biochemistry 49 2010 2765 2767
    • (2010) Biochemistry , vol.49 , pp. 2765-2767
    • Jackson, S.A.1    Fagerlund, R.D.2    Wilbanks, S.M.3    Eaton-Rye, J.J.4
  • 12
    • 77956375190 scopus 로고    scopus 로고
    • Recent advances in understanding the assembly and repair of photosystem II
    • P.J. Nixon, F. Michoux, J.F. Yu, M. Boehm, and J. Komenda Recent advances in understanding the assembly and repair of photosystem II Ann. Bot. 106 2010 1 16
    • (2010) Ann. Bot. , vol.106 , pp. 1-16
    • Nixon, P.J.1    Michoux, F.2    Yu, J.F.3    Boehm, M.4    Komenda, J.5
  • 13
    • 77954370874 scopus 로고    scopus 로고
    • LPA19, a Psb27 homolog in Arabidopsis thaliana, facilitates D1 protein precursor processing during PSII biogenesis
    • L.L. Wei, J.K. Guo, M. Ouyang, X.W. Sun, J.F. Ma, W. Chi, C.M. Lu, and L.X. Zhang LPA19, a Psb27 homolog in Arabidopsis thaliana, facilitates D1 protein precursor processing during PSII biogenesis J. Biol. Chem. 285 2010 21391 21398
    • (2010) J. Biol. Chem. , vol.285 , pp. 21391-21398
    • Wei, L.L.1    Guo, J.K.2    Ouyang, M.3    Sun, X.W.4    Ma, J.F.5    Chi, W.6    Lu, C.M.7    Zhang, L.X.8
  • 15
    • 70349108408 scopus 로고    scopus 로고
    • Structure of Psb27 in solution: Implications for transient binding to photosystem II during biogenesis and repair
    • K.U. Cormann, J.A. Bangert, M. Ikeuchi, M. Rogner, R. Stoll, and M.M. Nowaczyk Structure of Psb27 in solution: implications for transient binding to photosystem II during biogenesis and repair Biochemistry 48 2009 8768 8770
    • (2009) Biochemistry , vol.48 , pp. 8768-8770
    • Cormann, K.U.1    Bangert, J.A.2    Ikeuchi, M.3    Rogner, M.4    Stoll, R.5    Nowaczyk, M.M.6
  • 16
    • 34547893503 scopus 로고    scopus 로고
    • Oxidative photosynthetic water splitting: Energetics, kinetics and mechanism
    • DOI 10.1007/s11120-007-9185-x, Photosynthetic Water Oxidation
    • G. Renger Oxidative photosynthetic water splitting: energetics, kinetics and mechanism Photosynth. Res. 92 2007 407 425 (Pubitemid 47248573)
    • (2007) Photosynthesis Research , vol.92 , Issue.3 , pp. 407-425
    • Renger, G.1
  • 18
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II
    • DOI 10.1038/nature04224, PII NATURE04224
    • B. Loll, J. Kern, W. Saenger, A. Zouni, and J. Biesiadka Towards complete cofactor arrangement in the 3.0 resolution structure of photosystem II Nature 438 2005 1040 1044 (Pubitemid 43093979)
    • (2005) Nature , vol.438 , Issue.7070 , pp. 1040-1044
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 20
    • 66649106614 scopus 로고    scopus 로고
    • Location of chloride and its possible functions in oxygen-evolving photosystem II revealed by X-ray crystallography
    • K. Kawakami, Y. Umena, N. Kamiya, and J.R. Shen Location of chloride and its possible functions in oxygen-evolving photosystem II revealed by X-ray crystallography Proc. Natl. Acad. Sci. USA 106 2009 8567 8572
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 8567-8572
    • Kawakami, K.1    Umena, Y.2    Kamiya, N.3    Shen, J.R.4
  • 21
    • 16844375171 scopus 로고    scopus 로고
    • Energetics of proton transfer pathways in reaction centers from Rhodobacter sphaeroides. The Glu-H173 activated mutants
    • H. Ishikita, and E.W. Knapp Energetics of proton transfer pathways in reaction centers from Rhodobacter sphaeroides. The Glu-H173 activated mutants J. Biol. Chem. 280 2005 12446 12450
    • (2005) J. Biol. Chem. , vol.280 , pp. 12446-12450
    • Ishikita, H.1    Knapp, E.W.2
  • 22
    • 34547116864 scopus 로고    scopus 로고
    • Structural characteristics of channels and pathways in photosystem II including the identification of an oxygen channel
    • DOI 10.1016/j.jsb.2007.01.016, PII S1047847707000238
    • J.W. Murray, and J. Barber Structural characteristics of channels and pathways in photosystem II including the identification of an oxygen channel J. Struct. Biol. 159 2007 228 237 (Pubitemid 47096868)
    • (2007) Journal of Structural Biology , vol.159 , Issue.2 SPEC. ISS. , pp. 228-237
    • Murray, J.W.1    Barber, J.2
  • 23
    • 38849188029 scopus 로고    scopus 로고
    • 4 cluster in Photosystem II based on solvent accessibility simulations, with implications for substrate water access
    • DOI 10.1016/j.bbabio.2007.08.009, PII S0005272807002009
    • 4 cluster in photosystem II based on solvent accessibility simulations, with implications for substrate water access Biochim. Biophys. Acta 1777 2008 140 153 (Pubitemid 351187745)
    • (2008) Biochimica et Biophysica Acta - Bioenergetics , vol.1777 , Issue.2 , pp. 140-153
    • Ho, F.M.1    Styring, S.2
  • 24
    • 57849114287 scopus 로고    scopus 로고
    • Uncovering channels in photosystem II by computer modelling: Current progress, future prospects, and lessons from analogous systems
    • DOI 10.1007/s11120-008-9358-2
    • F.M. Ho Uncovering channels in photosystem II by computer modelling: current progress, future prospects, and lessons from analogous systems Photosynth. Res. 98 2008 503 522 (Pubitemid 50274589)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 503-522
    • Ho, F.M.1
  • 26
    • 77749255459 scopus 로고    scopus 로고
    • Tracking the flow of water through photosystem II using molecular dynamics and streamline tracing
    • S. Vassiliev, P. Comte, A. Mahboob, and D. Bruce Tracking the flow of water through photosystem II using molecular dynamics and streamline tracing Biochemistry 49 2010 1873 1881
    • (2010) Biochemistry , vol.49 , pp. 1873-1881
    • Vassiliev, S.1    Comte, P.2    Mahboob, A.3    Bruce, D.4
  • 29
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 A resolution
    • DOI 10.1038/nature02373
    • Z. Liu, H. Yan, K. Wang, T. Kuang, J. Zhang, L. Gui, X. An, and W. Chang Crystal structure of spinach major light-harvesting complex at 2.72 resolution Nature 428 2004 287 292 (Pubitemid 38418793)
    • (2004) Nature , vol.428 , Issue.6980 , pp. 287-292
    • Liu, Z.1    Yan, H.2    Wang, K.3    Kuang, T.4    Zhang, J.5    Gui, L.6    An, X.7    Chang, W.8
  • 30
    • 16344363252 scopus 로고    scopus 로고
    • Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 A resolution
    • DOI 10.1038/sj.emboj.7600585
    • J. Standfuss, A.C. Terwisscha van Scheltinga, M. Lamborghini, and W. Kuehlbrandt Mechanisms of photoprotection and nonphotochemical quenching in pea light-harvesting complex at 2.5 resolution EMBO J. 24 2005 919 928 (Pubitemid 40470141)
    • (2005) EMBO Journal , vol.24 , Issue.5 , pp. 919-928
    • Standfuss, J.1    Van Scheltinga, A.C.T.2    Lamborghini, M.3    Kuhlbrandt, W.4
  • 32
    • 34249811783 scopus 로고    scopus 로고
    • Lipids in photosystem II: Interactions with protein and cofactors
    • DOI 10.1016/j.bbabio.2006.12.009, PII S0005272806003872, Structure and Function of Photosystems
    • B. Loll, J. Kern, W. Saenger, A. Zouni, and J. Biesiadka Lipids in photosystem II: interactions with protein and cofactors Biochim. Biophys. Acta 1767 2007 509 519 (Pubitemid 46855733)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.6 , pp. 509-519
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 33
    • 33750328873 scopus 로고    scopus 로고
    • Lipids in oxygen-evolving photosystem II complexes of cyanobacteria and higher plants
    • DOI 10.1093/jb/mvj141
    • I. Sakurai, J.R. Shen, J. Leng, S. Ohashi, M. Kobayashi, and H. Wada Lipids in oxygen-evolving photosystem II complexes of cyanobacteria and higher plants J. Biochem. (Tokyo) 140 2006 201 209 (Pubitemid 44618906)
    • (2006) Journal of Biochemistry , vol.140 , Issue.2 , pp. 201-209
    • Sakurai, I.1    Shen, J.-R.2    Leng, J.3    Ohashi, S.4    Kobayashi, M.5    Wada, H.6
  • 34
    • 33751197485 scopus 로고    scopus 로고
    • Lipids in photosynthetic reaction centres: Structural roles and functional holes
    • M.R. Jones Lipids in photosynthetic reaction centres: structural roles and functional holes Prog. Lipid Res. 46 2007 56 87
    • (2007) Prog. Lipid Res. , vol.46 , pp. 56-87
    • Jones, M.R.1
  • 35
    • 11144285975 scopus 로고    scopus 로고
    • Purification, characterisation and crystallisation of photosystem II from Thermosynechococcus elongatus cultivated in a new type of photobioreactor
    • DOI 10.1016/j.bbabio.2004.10.007, PII S0005272804002956
    • J. Kern, B. Loll, C. Lüneberg, D. DiFiore, J. Biesiadka, K.D. Irrgang, and A. Zouni Purification, characterisation and crystallisation of photosystem II from Thermosynechococcus elongatus cultivated in a new type of photobioreactor Biochim. Biophys. Acta 1706 2005 147 157 (Pubitemid 40037770)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1706 , Issue.1-2 , pp. 147-157
    • Kern, J.1    Loll, B.2    Luneberg, C.3    DiFiore, D.4    Biesiadka, J.5    Irrgang, K.-D.6    Zouni, A.7
  • 36
    • 0023023405 scopus 로고
    • Chemical composition of purified oxygen-evolving complexes from the thermophilic cyanobacterium Synechococcus sp
    • DOI 10.1016/0005-2728(86)90049-6
    • T. Ohno, K. Satoh, and S. Katoh Chemical composition of purified oxygen-evolving complexes from the thermophilic cyanobacterium Synechococcus sp Biochim. Biophys. Acta 852 1986 1 8 (Pubitemid 17182245)
    • (1986) Biochimica et Biophysica Acta - Bioenergetics , vol.852 , Issue.1 , pp. 1-8
    • Ohno, T.1    Satoh, K.2    Katoh, S.3
  • 37
    • 57849127574 scopus 로고    scopus 로고
    • Effects of phospholipase and lipase treatments on photosystem II core dimer from a thermophilic cyanobacterium
    • DOI 10.1007/s11120-008-9335-9
    • J. Leng, I. Sakurai, H. Wada, and J.-R. Shen Effects of phospholipase and lipase treatments on photosystem II core dimer from a thermophilic cyanobacterium Photosynth. Res. 98 2008 469 478 (Pubitemid 50224949)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 469-478
    • Leng, J.1    Sakurai, I.2    Wada, H.3    Shen, J.-R.4
  • 39
    • 0035028257 scopus 로고    scopus 로고
    • Unsaturated fatty acids in membrane lipids protect the photosynthetic machinery against salt-induced damage in Synechococcus
    • DOI 10.1104/pp.125.4.1842
    • S.I. Allakhverdiev, M. Kinoshita, M. Inaba, I. Suzuki, and N. Murata Unsaturated fatty acids in membrane lipids protect the photosynthetic machinery against salt-induced damage in Synechococcus Plant Physiol. 125 2001 1842 1853 (Pubitemid 32375767)
    • (2001) Plant Physiology , vol.125 , Issue.4 , pp. 1842-1853
    • Allakhverdiev, S.I.1    Kinoshita, M.2    Inaba, M.3    Suzuki, I.4    Murata, N.5
  • 42
    • 77956220438 scopus 로고    scopus 로고
    • Crystal structure of monomeric photosystem II from Thermosynechococcus elongatus at 3.6-angstrom resolution
    • M. Broser, A. Gabdulkhakov, J. Kern, A. Guskov, F. Muh, W. Saenger, and A. Zouni Crystal structure of monomeric photosystem II from Thermosynechococcus elongatus at 3.6-angstrom resolution J. Biol. Chem. 285 2010 26255 26262
    • (2010) J. Biol. Chem. , vol.285 , pp. 26255-26262
    • Broser, M.1    Gabdulkhakov, A.2    Kern, J.3    Guskov, A.4    Muh, F.5    Saenger, W.6    Zouni, A.7
  • 43
    • 0033515557 scopus 로고    scopus 로고
    • A heptad motif of leucine residues found in membrane proteins can drive self-assembly of artificial transmembrane segments
    • R. Gurezka, R. Laage, B. Brosig, and D. Langosch A heptad motif of leucine residues found in membrane proteins can drive self-assembly of artificial transmembrane segments J. Biol. Chem. 274 1999 9265 9270
    • (1999) J. Biol. Chem. , vol.274 , pp. 9265-9270
    • Gurezka, R.1    Laage, R.2    Brosig, B.3    Langosch, D.4
  • 45
    • 19544376279 scopus 로고    scopus 로고
    • Synthesis and assembly of thylakoid protein complexes. Multiple assembly steps of photosystem II
    • A. Rokka, M. Suorsa, A. Saleem, N. Battchikova, and E.M. Aro Synthesis and assembly of thylakoid protein complexes. Multiple assembly steps of photosystem II Biochem. J. 388 2005 159 168
    • (2005) Biochem. J. , vol.388 , pp. 159-168
    • Rokka, A.1    Suorsa, M.2    Saleem, A.3    Battchikova, N.4    Aro, E.M.5
  • 47
    • 13944284179 scopus 로고    scopus 로고
    • Singlet oxygen production in photosynthesis
    • DOI 10.1093/jxb/erh237, Light Stress in Plants: Mechanisms and Interactions
    • A. Krieger-Liszkay Singlet oxygen production in photosynthesis J. Exp. Bot. 56 2005 337 346 (Pubitemid 40263280)
    • (2005) Journal of Experimental Botany , vol.56 , Issue.411 , pp. 337-346
    • Krieger-Liszkay, A.1
  • 48
    • 0026668044 scopus 로고
    • Structural-changes and lateral redistribution of photosystem-II during donor side photoinhibition of thylakoids
    • R. Barbato, G. Friso, F. Rigoni, F. Dalla Vecchia, and G.M. Giacometti Structural-changes and lateral redistribution of photosystem-II during donor side photoinhibition of thylakoids J. Cell Biol. 119 1992 325 335
    • (1992) J. Cell Biol. , vol.119 , pp. 325-335
    • Barbato, R.1    Friso, G.2    Rigoni, F.3    Dalla Vecchia, F.4    Giacometti, G.M.5
  • 50
    • 0037133542 scopus 로고    scopus 로고
    • B in the photosystem II reaction center
    • DOI 10.1021/bi011884h
    • Z. Gombos, Z. Varkonyi, M. Hagio, M. Iwaki, L. Kovacs, K. Masamoto, S. Itoh, and H. Wada Phosphatidylglycerol requirement for the function of electron acceptor plastoquinone Q(B) in the photosystem II reaction center Biochemistry 41 2002 3796 3802 (Pubitemid 34224694)
    • (2002) Biochemistry , vol.41 , Issue.11 , pp. 3796-3802
    • Gombos, Z.1    Varkonyi, Z.2    Hagio, M.3    Iwaki, M.4    Kovacs, L.5    Masamoto, K.6    Itoh, S.7    Wada, H.8
  • 51
    • 49349095972 scopus 로고    scopus 로고
    • Role of phosphatidylglycerol in the function and assembly of photosystem II reaction center, studied in a cdsA-inactivated PAL mutant strain of Synechocystis sp. PCC6803 that lacks phycobilisomes
    • H. Laczkó-Dobos, B. Ughy, S.Z. Tóth, J. Komenda, O. Zsiros, I. Domonkos, Á. Párducz, B. Bogos, M. Komura, S. Itoh, and Z. Gombos Role of phosphatidylglycerol in the function and assembly of photosystem II reaction center, studied in a cdsA-inactivated PAL mutant strain of Synechocystis sp. PCC6803 that lacks phycobilisomes Biochim. Biophys. Acta 1777 2008 1184 1194
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1184-1194
    • Laczkó-Dobos, H.1    Ughy, B.2    Tóth, S.Z.3    Komenda, J.4    Zsiros, O.5    Domonkos, I.6    Párducz, Á.7    Bogos, B.8    Komura, M.9    Itoh, S.10    Gombos, Z.11
  • 53
    • 0029294101 scopus 로고
    • The role of phosphatidylglycerol as a functional effector and membrane anchor of the D1-core peptide from photosystem II-particles of the cyanobacterium Oscillatoria chalybea
    • O. Kruse, and G.H. Schmid The role of phosphatidylglycerol as a functional effector and membrane anchor of the D1-core peptide from photosystem II-particles of the cyanobacterium Oscillatoria chalybea Z. Naturforsch. 50c 1995 380 390
    • (1995) Z. Naturforsch. , vol.50 , pp. 380-390
    • Kruse, O.1    Schmid, G.H.2
  • 55
    • 34249811783 scopus 로고    scopus 로고
    • Lipids in photosystem II: Interactions with protein and cofactors
    • DOI 10.1016/j.bbabio.2006.12.009, PII S0005272806003872, Structure and Function of Photosystems
    • B. Loll, J. Kern, W. Saenger, A. Zouni, and J. Biesiadka Lipids in photosystem II: interactions with protein and cofactors Biochim. Biophys. Acta 1767 2007 509 519 (Pubitemid 46855733)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.6 , pp. 509-519
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 56
    • 0030852458 scopus 로고    scopus 로고
    • Modification of the water oxidizing complex in leaves of the dgd1 mutant of Arabidopsis thaliana deficient in the galactolipid digalactosyldiacylglycerol
    • DOI 10.1021/bi9709654
    • F. Reifarth, G. Christen, A.G. Seeliger, P. Dormann, C. Benning, and G. Renger Modification of the water oxidizing complex in leaves of the dgd1 mutant of Arabidopsis thaliana deficient in the galactolipid digalactosyldiacylglycerol Biochemistry 36 1997 11769 11776 (Pubitemid 27424102)
    • (1997) Biochemistry , vol.36 , Issue.39 , pp. 11769-11776
    • Reifarth, F.1    Christen, G.2    Seeliger, A.G.3    Dormann, P.4    Benning, C.5    Renger, G.6
  • 57
    • 14644397253 scopus 로고    scopus 로고
    • Investigations on the reaction pattern of photosystem II in leaves from Arabidopsis thaliana wild type plants and mutants with genetically modified lipid content
    • DOI 10.1021/bi048465f
    • R. Steffen, A.A. Kelly, J. Huyer, P. Doermann, and G. Renger Investigations on the reaction pattern of photosystem II in leaves from Arabidopsis thaliana wild type plants and mutants with genetically modified lipid content Biochemistry 44 2005 3134 3142 (Pubitemid 40321985)
    • (2005) Biochemistry , vol.44 , Issue.9 , pp. 3134-3142
    • Steffen, R.1    Kelly, A.A.2    Huyer, J.3    Dormann, P.4    Renger, G.5
  • 58
    • 37249008619 scopus 로고    scopus 로고
    • Digalactosyldiacylglycerol is required for stabilization of the oxygen-evolving complex in photosystem II
    • DOI 10.1104/pp.107.106781
    • I. Sakurai, N. Mizusawa, H. Wada, and N. Sato Digalactosyldiacylglycerol is required for stabilization of the oxygen-evolving complex in photosystem II Plant Physiol. 145 2007 1361 1370 (Pubitemid 350276756)
    • (2007) Plant Physiology , vol.145 , Issue.4 , pp. 1361-1370
    • Sakurai, I.1    Mizusawa, N.2    Wada, H.3    Sato, N.4
  • 60
    • 34547661911 scopus 로고    scopus 로고
    • The essential role of phosphatidylglycerol in photosynthesis
    • DOI 10.1007/s11120-007-9203-z, A Tribute to Andrew A. Benson
    • H. Wada, and N. Murata The essential role of phosphatidylglycerol in photosynthesis Photosynth. Res. 92 2007 205 215 (Pubitemid 47222263)
    • (2007) Photosynthesis Research , vol.92 , Issue.2 , pp. 205-215
    • Wada, H.1    Murata, N.2
  • 62
    • 52949148561 scopus 로고    scopus 로고
    • Lipid-assisted protein-protein interactions that support photosynthetic and other cellular activities
    • I. Domonkos, H. Laczko-Dobos, and Z. Gombos Lipid-assisted protein-protein interactions that support photosynthetic and other cellular activities Prog. Lipid Res. 47 2008 422 435
    • (2008) Prog. Lipid Res. , vol.47 , pp. 422-435
    • Domonkos, I.1    Laczko-Dobos, H.2    Gombos, Z.3
  • 63
    • 0141794511 scopus 로고    scopus 로고
    • Decrease in the efficiency of the electron donation to tyrosine Z of photosystem II in an SQDG-deficient mutant of Chlamydomonas
    • DOI 10.1016/S0014-5793(03)00981-5
    • A. Minoda, K. Sonoike, K. Okada, N. Sato, and M. Tsuzuki Decrease in the efficiency of the electron donation to tyrosine Z of photosystem II in an SQDG-deficient mutant of Chlamydomonas FEBS Lett. 553 2003 109 112 (Pubitemid 37206334)
    • (2003) FEBS Letters , vol.553 , Issue.1-2 , pp. 109-112
    • Minoda, A.1    Sonoike, K.2    Okada, K.3    Sato, N.4    Tsuzuki, M.5
  • 64
  • 65
    • 27644585264 scopus 로고    scopus 로고
    • 10 in the center of a deuterated lipid membrane by neutron diffraction
    • DOI 10.1016/j.bbabio.2005.08.007, PII S0005272805002240
    • T. Hauss, S. Dante, T.H. Haines, and N.A. Dencher Localization of coenzyme Q10 in the center of a deuterated lipid membrane by neutron diffraction Biochim. Biophys. Acta 1710 2005 57 62 (Pubitemid 41566999)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1710 , Issue.1 , pp. 57-62
    • Hauss, T.1    Dante, S.2    Haines, T.H.3    Dencher, N.A.4
  • 66
    • 0032502940 scopus 로고    scopus 로고
    • 10 might be related to a folded structure
    • DOI 10.1016/S0014-5793(98)00313-5, PII S0014579398003135
    • S. Di Bernardo, R. Fato, R. Casadio, P. Fariselli, and G. Lenaz A high diffusion coefficient for coenzyme Q(10) might be related to a folded structure FEBS Lett. 426 1998 77 80 (Pubitemid 28198159)
    • (1998) FEBS Letters , vol.426 , Issue.1 , pp. 77-80
    • Di Bernardo, S.1    Fato, R.2    Casadio, R.3    Fariselli, P.4    Lenaz, G.5
  • 67
    • 33846617289 scopus 로고    scopus 로고
    • Evidence for a novel quinone-binding site in the photosystem II (PS II) complex that regulates the redox potential of cytochrome b559
    • DOI 10.1021/bi0613022
    • O. Kaminskaya, V.A. Shuvalov, and G. Renger Evidence for a novel quinone-binding site in the photosystem II (PS II) complex that regulates the redox potential of cytochrome b559 Biochemistry 46 2007 1091 1105 (Pubitemid 46184996)
    • (2007) Biochemistry , vol.46 , Issue.4 , pp. 1091-1105
    • Kaminskaya, O.1    Shuvalov, V.A.2    Renger, G.3
  • 69
    • 38549112315 scopus 로고    scopus 로고
    • Plastoquinol as a singlet oxygen scavenger in photosystem II
    • DOI 10.1016/j.bbabio.2007.10.008, PII S0005272807002368
    • J. Kruk, and A. Trebst Plastoquinol as a singlet oxygen scavenger in photosystem II Biochim. Biophys. Acta 1777 2008 154 162 (Pubitemid 351162863)
    • (2008) Biochimica et Biophysica Acta - Bioenergetics , vol.1777 , Issue.2 , pp. 154-162
    • Kruk, J.1    Trebst, A.2
  • 70
    • 0032551765 scopus 로고    scopus 로고
    • Oxygen permeability of thylakoid membranes: Electron paramagnetic resonance spin labeling study
    • DOI 10.1016/S0005-2728(98)00098-X, PII S000527289800098X
    • A. Ligeza, A.N. Tikhonov, J.S. Hyde, and W.K. Subczynski Oxygen permeability of thylakoid membranes: electron paramagnetic resonance spin labeling study Biochim. Biophys. Acta 1365 1998 453 463 (Pubitemid 29012402)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1365 , Issue.3 , pp. 453-463
    • Ligeza, A.1    Tikhonov, A.N.2    Hyde, J.S.3    Subczynski, W.K.4
  • 71
    • 0034569695 scopus 로고    scopus 로고
    • Physical properties of lipid bilayer membranes: Relevance to membrane biological functions
    • W.K. Subczynski, and A. Wisniewska Physical properties of lipid bilayer membranes: relevance to membrane biological functions Acta Biochim. Pol. 47 2000 613 625
    • (2000) Acta Biochim. Pol. , vol.47 , pp. 613-625
    • Subczynski, W.K.1    Wisniewska, A.2
  • 72
    • 33646543348 scopus 로고    scopus 로고
    • Lipid conformation in crystalline bilayers and in crystals of transmembrane proteins
    • DOI 10.1016/j.chemphyslip.2006.02.005, PII S0009308406000247
    • D. Marsh, and T. Pali Lipid conformation in crystalline bilayers and in crystals of transmembrane proteins Chem. Phys. Lipids 141 2006 48 65 (Pubitemid 43728807)
    • (2006) Chemistry and Physics of Lipids , vol.141 , Issue.1-2 , pp. 48-65
    • Marsh, D.1    Pali, T.2
  • 74
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • M. Svensson-Ek, J. Abramson, G. Larsson, S. Tornroth, P. Brzezinski, and S. Iwata The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides J. Mol. Biol. 321 2002 329 339
    • (2002) J. Mol. Biol. , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Tornroth, S.4    Brzezinski, P.5    Iwata, S.6
  • 75
    • 42349083650 scopus 로고    scopus 로고
    • 3 from Thermus thermophilus: Structural analysis and role of oxygen transport channels in the heme-Cu oxidases
    • DOI 10.1021/bi800045y
    • V.M. Luna, Y. Chen, J.A. Fee, and C.D. Stout Crystallographic studies of Xe and Kr binding within the large internal cavity of cytochrome ba3 from Thermus thermophilus: structural analysis and role of oxygen transport channels in the heme-Cu oxidases Biochemistry 47 2008 4657 4665 (Pubitemid 351555486)
    • (2008) Biochemistry , vol.47 , Issue.16 , pp. 4657-4665
    • Luna, V.M.1    Chen, Y.2    Fee, J.A.3    Stout, C.D.4
  • 76
    • 57849169340 scopus 로고    scopus 로고
    • Analysis of xenon binding to photosystem II by X-ray crystallography
    • DOI 10.1007/s11120-008-9366-2
    • J.W. Murray, K. Maghlaoui, J. Kargul, M. Sugiura, and J. Barber Analysis of xenon binding to photosystem II by X-ray crystallography Photosynth. Res. 98 2008 523 527 (Pubitemid 50294457)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 523-527
    • Murray, J.W.1    Maghlaoui, K.2    Kargul, J.3    Sugiura, M.4    Barber, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.