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Volumn 1827, Issue 10, 2013, Pages 1174-1182

The Tll0287 protein is a hemoprotein associated with the PsbA2-Photosystem II complex in Thermosynechococcus elongatus

Author keywords

Cyanobacterium; D1; Photosystem II; PsbA; Thermosynechococcus elongates; Tll0287

Indexed keywords

BACTERIAL PROTEIN; HEMOPROTEIN; TLL0287 PROTEIN; UNCLASSIFIED DRUG;

EID: 84884290034     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2013.06.002     Document Type: Article
Times cited : (9)

References (61)
  • 1
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the Photosynthetic Oxygen-Evolving Center
    • DOI 10.1126/science.1093087
    • K.N. Ferreira, T.M. Iverson, K. Maghlaoui, J. Barber, S. Iwata, Architecture of the photosynthetic oxygen-evolving center, Science 303 (2004) 1831-1838. (Pubitemid 38374869)
    • (2004) Science , vol.303 , Issue.5665 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 3
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å
    • Y. Umena, K. Kawakami, J.-R. Shen, N. Kamiya, Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å, Nature 473 (2011) 55-60.
    • (2011) Nature , vol.473 , pp. 55-60
    • Umena, Y.1    Kawakami, K.2    Shen, J.-R.3    Kamiya, N.4
  • 5
    • 84859631223 scopus 로고    scopus 로고
    • Recent developments in research on water oxidation by photosystem II
    • H. Dau, H. Zaharieva, M. Haumann, Recent developments in research on water oxidation by photosystem II, Curr. Op. Chem. Biol. 16 (2012) 3-10.
    • (2012) Curr. Op. Chem. Biol , vol.16 , pp. 3-10
    • Dau, H.1    Zaharieva, H.2    Haumann, M.3
  • 7
    • 33144472069 scopus 로고    scopus 로고
    • Kinetics and mechanism of electron transfer in intact photosystem II and in the isolated reaction center: Pheophytin is the primary electron acceptor
    • A.R. Holzwarth, M.G. Muller, M. Reus, M. Nowaczyk, J. Sander, M. Rogner, Kinetics and mechanism of electron transfer in intact photosystem II and in the isolated reaction center: pheophytin is the primary electron acceptor, Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 6895-6900.
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 6895-6900
    • Holzwarth, A.R.1    Muller, M.G.2    Reus, M.3    Nowaczyk, M.4    Sander, J.5    Rogner, M.6
  • 8
    • 48749143707 scopus 로고
    • The electrochemical domain of photosynthesis
    • A.R. Crofts, C.A. Wraight, The electrochemical domain of photosynthesis, Biochim. Biophys. Acta 726 (1983) 149-185.
    • (1983) Biochim. Biophys. Acta , vol.726 , pp. 149-185
    • Crofts, A.R.1    Wraight, C.A.2
  • 9
    • 0015957318 scopus 로고
    • Charge accumulation at the reducing side of system 2 of photosynthesis
    • B.R. Velthuys, J. Amesz, Charge accumulation at the reducing side of system 2 of photosynthesis, Biochim. Biophys. Acta 333 (1974) 85-94.
    • (1974) Biochim. Biophys. Acta , vol.333 , pp. 85-94
    • Velthuys, B.R.1    Amesz, J.2
  • 10
    • 0014805072 scopus 로고
    • Cooperation of charges in photosyntheticO2 evolution- I. A linear four step mechanism
    • B. Kok, B. Forbush, M. McGloin, Cooperation of charges in photosyntheticO2 evolution- I. A linear four step mechanism, Photochem. Photobiol. 11 (1970) 457-475.
    • (1970) Photochem. Photobiol , vol.11 , pp. 457-475
    • Kok, B.1    Forbush, B.2    McGloin, M.3
  • 11
    • 0002232564 scopus 로고
    • Oxygen evolution in photosynthesis
    • in: Govindjee (Ed.) Academic Press, New York
    • P. Joliot, B. Kok, Oxygen evolution in photosynthesis, in: Govindjee (Ed.), Bioenergetics of Photosynthesis, Academic Press, New York, 1975, pp. 387-412.
    • (1975) Bioenergetics of Photosynthesis , pp. 387-412
    • Joliot, P.1    Kok, B.2
  • 12
    • 84884341651 scopus 로고    scopus 로고
    • Reflections on substrate water and dioxygen formation
    • N. Cox, J. Messinger, Reflections on substrate water and dioxygen formation, Biochim. Biophys. Acta 1827 (2013) 1020-1030.
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 1020-1030
    • Cox, N.1    Messinger, J.2
  • 15
    • 0028953989 scopus 로고
    • Light-responsive gene expression in cyanobacteria
    • S.S. Golden, Light-responsive gene expression in cyanobacteria, J. Bacteriol. 177 (1995) 1651-1654.
    • (1995) J. Bacteriol , vol.177 , pp. 1651-1654
    • Golden, S.S.1
  • 16
    • 0034058872 scopus 로고    scopus 로고
    • Degradation of the Photosystem II D1 and D2 proteins in different strains of the cyanobacterium Synechocystis PCC 6803 varying with respect to the type and level of psbA transcript
    • DOI 10.1023/A:1006305308196
    • J. Komenda, H. Hassan, B.A. Diner, R.J. Debus, J. Barber, P.J. Nixon, Degradation of the photosystem II D1 and D2 proteins in different strains of the cyanobacterium Synechocystis PCC 6803 varying with respect to the type and level of psbA transcript, Plant Mol. Biol. 42 (2000) 635-645. (Pubitemid 30236511)
    • (2000) Plant Molecular Biology , vol.42 , Issue.4 , pp. 635-645
    • Komenda, J.1    Hassan, H.A.G.2    Diner, B.A.3    Debus, R.J.4    Barber, J.5    Nixon, P.J.6
  • 19
    • 70749136825 scopus 로고    scopus 로고
    • Cyanobacterial psbA gene family: Optimization of oxygenic photosynthesis
    • P. Mulo, C. Sicora, E.-M. Aro, Cyanobacterial psbA gene family: optimization of oxygenic photosynthesis, Cell. Mol. Life Sci. 66 (2009) 3697-3710.
    • (2009) Cell. Mol. Life Sci , vol.66 , pp. 3697-3710
    • Mulo, P.1    Sicora, C.2    Aro, E.-M.3
  • 20
    • 58649102249 scopus 로고    scopus 로고
    • Transcription of a "silent" cyanobacterial psbA gene is induced by microaerobic conditions
    • C.I. Sicora, F.M. Ho, T. Salminen, S. Styring, E.-M. Aro, Transcription of a "silent" cyanobacterial psbA gene is induced by microaerobic conditions, Biochim. Biophys. Acta 1787 (2009) 105-112.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 105-112
    • Sicora, C.I.1    Ho, F.M.2    Salminen, T.3    Styring, S.4    Aro, E.-M.5
  • 21
    • 77953811055 scopus 로고    scopus 로고
    • Energetics in photosystem II from Thermosynechococcus elongatus with a D1 protein encoded by either the psbA1 or psbA3 gene
    • M. Sugiura, Y. Kato, R. Takahashi, H. Suzuki, T. Watanabe, T. Noguchi, F. Rappaport, A. Boussac, Energetics in photosystem II from Thermosynechococcus elongatus with a D1 protein encoded by either the psbA1 or psbA3 gene, Biochim. Biophys. Acta 1797 (2010) 1491-1499.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1491-1499
    • Sugiura, M.1    Kato, Y.2    Takahashi, R.3    Suzuki, H.4    Watanabe, T.5    Noguchi, T.6    Rappaport, F.7    Boussac, A.8
  • 22
    • 84861216966 scopus 로고    scopus 로고
    • A unique regulation of the expression of the psbA, psbD, and psbE genes, encoding the D1, D2 and cytochrome b559 subunits of the photosystem II complex in the chlorophyll d containing cyanobacterium Acaryochloris marina
    • E. Kiss, P.B. Kos, M. Chen, I. Vass, A unique regulation of the expression of the psbA, psbD, and psbE genes, encoding the D1, D2 and cytochrome b559 subunits of the photosystem II complex in the chlorophyll d containing cyanobacterium Acaryochloris marina, Biochim. Biophys. Acta 1817 (2012) 1083-1094.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1083-1094
    • Kiss, E.1    Kos, P.B.2    Chen, M.3    Vass, I.4
  • 24
    • 45749102065 scopus 로고    scopus 로고
    • Modeling of variant copies of subunit D1 in the structure of photosystem II from Thermosynechococcus elongatus
    • DOI 10.1515/BC.2008.058
    • B. Loll, M. Broser, P.B. Kós, J. Kern, J. Biesiadka, I. Vass, W. Saenger, A. Zouni, Modeling of variant copies of subunit D1 in the structure of photosystem II from Thermosynechococcus elongatus, Biol. Chem. 389 (2008) 609-617. (Pubitemid 351874192)
    • (2008) Biological Chemistry , vol.389 , Issue.5 , pp. 609-617
    • Loll, B.1    Broser, M.2    Kos, P.B.3    Kern, J.4    Biesiadka, J.5    Vass, I.6    Saenger, W.7    Zouni, A.8
  • 25
    • 77956899459 scopus 로고    scopus 로고
    • Functional characterization and quantification of the alternative PsbA copies in Thermosynechococcus elongatus and their role in photoprotection
    • J. Sander, M. Nowaczyk, J. Buchta, H. Dau, I. Vass, Z. Deak, M. Dorogi, M. Iwai, M. Rogner, Functional characterization and quantification of the alternative PsbA copies in Thermosynechococcus elongatus and their role in photoprotection, J. Biol. Chem. 285 (2010) 29851-29856.
    • (2010) J. Biol. Chem , vol.285 , pp. 29851-29856
    • Sander, J.1    Nowaczyk, M.2    Buchta, J.3    Dau, H.4    Vass, I.5    Deak, Z.6    Dorogi, M.7    Iwai, M.8    Rogner, M.9
  • 26
    • 71749108754 scopus 로고    scopus 로고
    • D1 protein variants in photosystem II from Thermosynechococcus elongatus studied by low temperature optical spectroscopy
    • J.L. Hughes, N. Nicholas, A.W. Rutherford, E. Krausz, T.-L. Lai, A. Boussac, M. Sugiura, D1 protein variants in photosystem II from Thermosynechococcus elongatus studied by low temperature optical spectroscopy, Biochim. Biophys. Acta 1797 (2010) 11-19.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 11-19
    • Hughes, J.L.1    Nicholas, N.2    Rutherford, A.W.3    Krausz, E.4    Lai, T.-L.5    Boussac, A.6    Sugiura, M.7
  • 27
    • 77956908711 scopus 로고    scopus 로고
    • Differences in the interactions between the subunits of photosystem II dependant on D1 protein variants in the thermophilic cyanobacterium Thermosynechococcus elongatus
    • M. Sugiura, E. Iwai, H. Hayashi, A. Boussac, Differences in the interactions between the subunits of photosystem II dependant on D1 protein variants in the thermophilic cyanobacterium Thermosynechococcus elongatus, J. Biol. Chem. 285 (2010) 30008-30018.
    • (2010) J. Biol. Chem , vol.285 , pp. 30008-30018
    • Sugiura, M.1    Iwai, E.2    Hayashi, H.3    Boussac, A.4
  • 28
    • 78249233837 scopus 로고    scopus 로고
    • Probing the quinone binding site of photosystem II from Thermosynechococcus elongatus containing either PsbA1 or PsbA3 as the D1 protein through the binding characteristics of herbicides
    • A. Boussac, M. Sugiura, F. Rappaport, Probing the quinone binding site of photosystem II from Thermosynechococcus elongatus containing either PsbA1 or PsbA3 as the D1 protein through the binding characteristics of herbicides, Biochim. Biophys. Acta 1807 (2010) 119-129.
    • (2010) Biochim. Biophys. Acta , vol.1807 , pp. 119-129
    • Boussac, A.1    Sugiura, M.2    Rappaport, F.3
  • 29
    • 84862236719 scopus 로고    scopus 로고
    • Deactivation processes in PsbA1-Photosystem II and PsbA3-Photosystem II under photoinhibitory conditions in the cyanobacterium Thermosynechococcus elongatus
    • S. Ogami, A. Boussac, M. Sugiura, Deactivation processes in PsbA1-Photosystem II and PsbA3-Photosystem II under photoinhibitory conditions in the cyanobacterium Thermosynechococcus elongatus, Biochim. Biophys. Acta 1817 (2012) 1322-1330.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1322-1330
    • Ogami, S.1    Boussac, A.2    Sugiura, M.3
  • 30
    • 84865682899 scopus 로고    scopus 로고
    • Influence of the PsbA1/PsbA3 and Ca2+/Sr2+ or Cl-/Br- exchanges on the redox potential of the primary quinone QA in photosystem II as revealed by spectroelectrochemistry
    • Y. Kato, T. Shibamoto, S. Yamamoto, T. Watanabe, N. Ishida, M. Sugiura, F. Rappaport, A. Boussac, Influence of the PsbA1/PsbA3 and Ca2+/Sr2+ or Cl-/Br- exchanges on the redox potential of the primary quinone QA in photosystem II as revealed by spectroelectrochemistry, Biochim. Biophys. Acta 1817 (2012) 1998-2004.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1998-2004
    • Kato, Y.1    Shibamoto, T.2    Yamamoto, S.3    Watanabe, T.4    Ishida, N.5    Sugiura, M.6    Rappaport, F.7    Boussac, A.8
  • 31
    • 84859760209 scopus 로고    scopus 로고
    • Environment of TyrZ in photosystem II from Thermosynechococcus elongatus in which PsbA2 is the D1 protein
    • M. Sugiura, S. Ogami, M. Kusumi, S. Un, F. Rappaport, A. Boussac, Environment of TyrZ in photosystem II from Thermosynechococcus elongatus in which PsbA2 is the D1 protein, J. Biol. Chem. 287 (2012) 13336-13347.
    • (2012) J. Biol. Chem , vol.287 , pp. 13336-13347
    • Sugiura, M.1    Ogami, S.2    Kusumi, M.3    Un, S.4    Rappaport, F.5    Boussac, A.6
  • 32
    • 0033401728 scopus 로고    scopus 로고
    • Highly purified thermo-stable oxygen-evolving photosystem II core complex from the thermophilic cyanobacterium Synechococcus elongatus having his-tagged CP43
    • M. Sugiura, Y. Inoue, Highly purified thermo-stable oxygen evolving photosystem II core complex from the thermophilic cyanobacterium Synechococcus elongatus having His-tagged CP43, Plant Cell Physiol. 40 (1999) 1219-1231. (Pubitemid 30031255)
    • (1999) Plant and Cell Physiology , vol.40 , Issue.12 , pp. 1219-1231
    • Sugiura, M.1    Inoue, Y.2
  • 33
    • 41249098659 scopus 로고    scopus 로고
    • Influence of histidine-198 of the D1 subunit on the properties of the primary electron donor, P680, of photosystem II in Thermosynechococcus elongates
    • M. Sugiura, A. Boussac, T. Noguchi, F. Rappaport, Influence of histidine-198 of the D1 subunit on the properties of the primary electron donor, P680, of photosystem II in Thermosynechococcus elongatus, Biochim. Biophys. Acta 1777 (2008) 331-342.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 331-342
    • Sugiura, M.1    Boussac, A.2    Noguchi, T.3    Rappaport, F.4
  • 34
    • 77953812232 scopus 로고    scopus 로고
    • Psb30 contributes to structurally stabilise the photosystem II complex in the thermophilic cyanobacterium Thermosynechococcus elongatus
    • M. Sugiura, S. Harada, T. Manabe, H. Hayashi, Y. Kashino, A. Boussac, Psb30 contributes to structurally stabilise the photosystem II complex in the thermophilic cyanobacterium Thermosynechococcus elongatus, Biochim. Biophys. Acta 1797 (2010) 1546-1554.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1546-1554
    • Sugiura, M.1    Harada, S.2    Manabe, T.3    Hayashi, H.4    Kashino, Y.5    Boussac, A.6
  • 35
    • 77957177789 scopus 로고
    • A new 4.8-kDa polypeptide intrinsic to the PS II reaction center, as revealed by modified SDS-PAGE with improved resolution of lowmolecular- weight proteins
    • M. Ikeuchi, Y. Inoue, A new 4.8-kDa polypeptide intrinsic to the PS II reaction center, as revealed by modified SDS-PAGE with improved resolution of lowmolecular- weight proteins, Plant Cell Physiol. 29 (1988) 1233-1239.
    • (1988) Plant Cell Physiol , vol.29 , pp. 1233-1239
    • Ikeuchi, M.1    Inoue, Y.2
  • 36
    • 0041696473 scopus 로고    scopus 로고
    • Structural and EPR characterization of the soluble form of cytochrome c-550 and of the psbV2 gene product from the cyanobacterium Thermosynechococcus elongatus
    • DOI 10.1093/pcp/pcg084
    • C.A. Kerfeld, M.R. Sawaya, H. Bottin, K.T. Tran, M. Sugiura, D. Cascio, A. Desbois, T.O. Yeates, D. Kirilovsky, A. Boussac, Structural and EPR characterization of the soluble form of cytochrome c-550 and of the psbV2 gene product from the cyanobacterium Thermosynechococcus elongatus, Plant Cell Physiol. 44 (2003) 697-706. (Pubitemid 36953624)
    • (2003) Plant and Cell Physiology , vol.44 , Issue.7 , pp. 697-706
    • Kerfeld, C.A.1    Sawaya, M.R.2    Bottin, H.3    Tran, K.T.4    Sugiura, M.5    Cascio, D.6    Desbois, A.7    Yeates, T.O.8    Kirilovsky, D.9    Boussac, A.10
  • 38
    • 0037172810 scopus 로고    scopus 로고
    • Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides
    • DOI 10.1021/bi026012+
    • Y. Kashino, W.M. Lauber, J.A. Carroll, Q. Wang, J. Whitmarsh, K. Satoh, H.B. Pakrasi, Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides, Biochemistry 41 (2002) 8004-8012. (Pubitemid 34655167)
    • (2002) Biochemistry , vol.41 , Issue.25 , pp. 8004-8012
    • Kashino, Y.1    Lauber, W.M.2    Carroll, J.A.3    Wang, Q.4    Whitmarsh, J.5    Satoh, K.6    Pakrasi, H.B.7
  • 39
    • 84862178390 scopus 로고    scopus 로고
    • Deletion of psbJ leads to accumulation of Psb27-Psb28 photosystem II complexes in Thermosynechococcus elongatus
    • M.M. Nowaczyk, K. Krause, M. Mieseler, A. Sczibilanski, M. Ikeuchi, M. Rögner, Deletion of psbJ leads to accumulation of Psb27-Psb28 photosystem II complexes in Thermosynechococcus elongatus, Biochim. Biophys. Acta 1817 (2012) 1339-1345.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1339-1345
    • Nowaczyk, M.M.1    Krause, K.2    Mieseler, M.3    Sczibilanski, A.4    Ikeuchi, M.5    Rögner, M.6
  • 40
    • 82755197722 scopus 로고    scopus 로고
    • Photosystem II, a growing complex: Updates on newly discovered components and low molecular mass proteins, Biochim
    • L.-X. Shi, M. Hall, C. Funk, W.P. Schröder, Photosystem II, a growing complex: updates on newly discovered components and low molecular mass proteins, Biochim. Biophys. Acta 1817 (2012) 13-25.
    • (2012) Biophys. Acta , vol.1817 , pp. 13-25
    • Shi, L.-X.1    Hall, M.2    Funk, C.3    Schröder, W.P.4
  • 42
    • 84869002016 scopus 로고    scopus 로고
    • Psb28 is involved in recovery of photosystem II at high temperature in Synechocystis sp. PCC 6803
    • S. Sakata, N. Mizusawa, H. Kubota-Kawai, I. Sakurai, H. Wada, Psb28 is involved in recovery of photosystem II at high temperature in Synechocystis sp. PCC 6803, Biochim. Biophys. Acta 1827 (2013) 50-59.
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 50-59
    • Sakata, S.1    Mizusawa, N.2    Kubota-Kawai, H.3    Sakurai, I.4    Wada, H.5
  • 43
    • 33644873592 scopus 로고    scopus 로고
    • Psb29, a conserved 22-kD protein, functions in the biogenesis of photosystem II complexes in Synechocystis and Arabidopsis
    • N. Keren, H. Ohkawa, E.A. Welsh, M. Liberton, H.B. Pakrasi, Psb29, a conserved 22-kD protein, functions in the biogenesis of photosystem II complexes in Synechocystis and Arabidopsis, Plant Cell 17 (2005) 2768-2781.
    • (2005) Plant Cell , vol.17 , pp. 2768-2781
    • Keren, N.1    Ohkawa, H.2    Welsh, E.A.3    Liberton, M.4    Pakrasi, H.B.5
  • 44
    • 53049083938 scopus 로고    scopus 로고
    • The cyanobacterial homologue of HCF136/YCF48 is a component of an early photosystem II assembly complex and is important for both the efficient assembly and repair of photosystemII in Synechocystis sp. PCC 6803
    • J. Komenda, J. Nickelsen, M. Tichy, O. Prasil, L.A. Eichacker, P.J. Nixon, The cyanobacterial homologue of HCF136/YCF48 is a component of an early photosystem II assembly complex and is important for both the efficient assembly and repair of photosystemII in Synechocystis sp. PCC 6803, J. Biol. Chem. 283 (2008) 22390-22399.
    • (2008) J. Biol. Chem , vol.283 , pp. 22390-22399
    • Komenda, J.1    Nickelsen, J.2    Tichy, M.3    Prasil, O.4    Eichacker, L.A.5    Nixon, P.J.6
  • 45
    • 84877912798 scopus 로고    scopus 로고
    • Mass spectrometrybased footprinting reveals structural dynamics of loop e of the chlorophyll-binding protein CP43 during photosystem II assembly in the cyanobacterium Synechocystis 6803
    • H. Liu, J. Chen, R.Y.-C. Huang, D. Weisz, M.L. Gross, H.B. Pakrasi, Mass spectrometrybased footprinting reveals structural dynamics of loop E of the chlorophyll-binding protein CP43 during photosystem II assembly in the cyanobacterium Synechocystis 6803, J. Biol. Chem. 288 (2013) 14212-14220.
    • (2013) J. Biol. Chem , vol.288 , pp. 14212-14220
    • Liu, H.1    Chen, J.2    Huang, R.Y.-C.3    Weisz, D.4    Gross, M.L.5    Pakrasi, H.B.6
  • 46
    • 85031139206 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, J.W. Murray, Structure of CyanoP at 2.8 angstrom: implications for the evolution and function of the PsbP subunit of photosystem II, J. Biol. Chem. 283 (2008) 22390-22399.
    • (2008) J. Biol. Chem , vol.283 , pp. 22390-22399
    • Michoux, F.1    Takasaka, K.2    Boehm, M.3    Nixon, P.J.4    Murray, J.W.5
  • 47
    • 84857239334 scopus 로고    scopus 로고
    • Crystal structure of the Psb27 assembly factor at 1.6: Implications for binding to photosystem II
    • F. Michoux, K. Takasaka, M. Boehm, J. Komenda, P.J. Nixon, J.W. Murray, Crystal structure of the Psb27 assembly factor at 1.6: implications for binding to photosystem II, Photosynth. Res. 110 (2012) 169-175.
    • (2012) Photosynth. Res , vol.110 , pp. 169-175
    • Michoux, F.1    Takasaka, K.2    Boehm, M.3    Komenda, J.4    Nixon, P.J.5    Murray, J.W.6
  • 49
    • 0034649367 scopus 로고    scopus 로고
    • EPR study of the oxygen evolving complex in His-tagged photosystem II from the cyanobacterium Synechococcus elongatus
    • A. Boussac, M. Sugiura, Y. Inoue, A.W. Rutherford, EPR study of the oxygen evolving complex in His-tagged photosystem II from the cyanobacterium Synechococcus elongatus, Biochemistry 39 (2000) 13788-13799.
    • (2000) Biochemistry , vol.39 , pp. 13788-13799
    • Boussac, A.1    Sugiura, M.2    Inoue, Y.3    Rutherford, A.W.4
  • 50
    • 0015829311 scopus 로고
    • Electron paramagnetic resonance studies of iron porphyrin and chlorin systems
    • J. Peisach, W.E. Blumberg, A. Adler, Electron paramagnetic resonance studies of iron porphyrin and chlorin systems, Ann. N. Y. Acad. Sci. 206 (1973) 310-327.
    • (1973) Ann. N. Y. Acad. Sci , vol.206 , pp. 310-327
    • Peisach, J.1    Blumberg, W.E.2    Adler, A.3
  • 51
    • 0021798004 scopus 로고
    • The electron paramagnetic resonance of metalloproteins
    • G. Palmer, The electron paramagnetic resonance of metalloproteins, Biochem. Soc. Trans. 13 (1985) 548-560. (Pubitemid 15057484)
    • (1985) Biochemical Society Transactions , vol.13 , Issue.3 , pp. 548-560
    • Palmer, G.1
  • 52
    • 0033464509 scopus 로고    scopus 로고
    • Magnetic spectroscopic (EPR, ESEEM, Mossbauer, MCD and NMR) studies of low-spin ferriheme centers and their corresponding heme proteins
    • F.A. Walker, Magnetic spectroscopic (EPR, ESEEM, Mossbauer, MCD and NMR) studies of low-spin ferriheme centers and their corresponding heme proteins, Coord. Chem. Rev. 186 (1999) 471-534.
    • (1999) Coord. Chem. Rev , vol.186 , pp. 471-534
    • Walker, F.A.1
  • 53
    • 84870509485 scopus 로고    scopus 로고
    • Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity
    • N.A. Tarboush, S. Shin, J. Geng, A. Liu, V.L. Davidson, Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity, FEBS Lett. 586 (2012) 4339-4343.
    • (2012) FEBS Lett , vol.586 , pp. 4339-4343
    • Tarboush, N.A.1    Shin, S.2    Geng, J.3    Liu, A.4    Davidson, V.L.5
  • 56
    • 1842412487 scopus 로고    scopus 로고
    • Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme
    • DOI 10.1038/38775
    • P.A. Williams, V. Fulop, E.F. Garman, N.F.W. Saunders, S.J. Ferguson, J. Hajdu, Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme, Nature 389 (1997) 406-412. (Pubitemid 27415226)
    • (1997) Nature , vol.389 , Issue.6649 , pp. 406-412
    • Williams, P.A.1    Fulop, V.2    Carman, E.F.3    Saunders, N.F.W.4    Ferguson, S.J.5    Hajdu, J.6
  • 58
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • S. Rogers, R. Wells, M. Rechsteiner, Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis, Science 234 (1986) 364-368. (Pubitemid 17181385)
    • (1986) Science , vol.234 , Issue.4774 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 59
    • 80255137210 scopus 로고    scopus 로고
    • Composition and function of cytochrome c biogenesis system II
    • J. Simon, L. Hederstedt, Composition and function of cytochrome c biogenesis system II, FEBS J. 278 (2011) 4179-4188.
    • (2011) FEBS J , vol.278 , pp. 4179-4188
    • Simon, J.1    Hederstedt, L.2
  • 60
    • 80255136293 scopus 로고    scopus 로고
    • Cytochrome c maturation system on the negative side of bioenergetic membranes: CCB or System IV
    • C. de Vitry, Cytochrome c maturation system on the negative side of bioenergetic membranes: CCB or System IV, FEBS J. 278 (2011) 4189-4197.
    • (2011) FEBS J , vol.278 , pp. 4189-4197
    • De Vitry, C.1
  • 61
    • 80255134546 scopus 로고    scopus 로고
    • Cytochrome c biogenesis in mitochondria-Systems III and v
    • J.W.A. Allen, Cytochrome c biogenesis in mitochondria-Systems III and V, FEBS J. 278 (2011) 4198-4216.
    • (2011) FEBS J , vol.278 , pp. 4198-4216
    • Allen, J.W.A.1


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