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Volumn 1797, Issue 4, 2010, Pages 451-456

Differential mechanism of light-induced and oxygen-dependent restoration of the high-potential form of cytochrome b559 in Tris-treated Photosystem II membranes

Author keywords

Cytochorome b559; Molecular oxygen; Photosystem II; Redox potential

Indexed keywords

CYTOCHROME B559; HISTIDINE; OXYGEN;

EID: 76849113966     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2009.12.023     Document Type: Article
Times cited : (10)

References (35)
  • 2
    • 33751287149 scopus 로고    scopus 로고
    • Photosystem II: an enzyme of global significance
    • Barber J. Photosystem II: an enzyme of global significance. Biochem. Soc. Trans. 2006, 34:619-631.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 619-631
    • Barber, J.1
  • 3
    • 38049011376 scopus 로고    scopus 로고
    • Primary photochemistry and energetics leading to the oxidation of the (Mn)4Ca cluster and to the evolution of molecular oxygen in Photosystem II
    • Rappaport F., Diner B.A. Primary photochemistry and energetics leading to the oxidation of the (Mn)4Ca cluster and to the evolution of molecular oxygen in Photosystem II. Coord. Chem. Rev. 2008, 252:259-272.
    • (2008) Coord. Chem. Rev. , vol.252 , pp. 259-272
    • Rappaport, F.1    Diner, B.A.2
  • 5
    • 0000337384 scopus 로고    scopus 로고
    • Form and Function of Cytochrome b-559
    • Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Whitmarsh J., Pakrasi H.B. Form and Function of Cytochrome b-559. Oxygenic Photosynthesis: The Light Reactions 1996, vol. 4:249-264. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1996) Oxygenic Photosynthesis: The Light Reactions , vol.4 , pp. 249-264
    • Whitmarsh, J.1    Pakrasi, H.B.2
  • 7
    • 0022417647 scopus 로고
    • Axial legends of chloroplast cytochrome b-559: identification and requirement for a heme-cross-linked polypeptide structure
    • Babcock G.T., Widger W.R., Cramer W.A., Oertling W.A., Metz J.G. Axial legends of chloroplast cytochrome b-559: identification and requirement for a heme-cross-linked polypeptide structure. Biochemistry 1985, 24:3638-3645.
    • (1985) Biochemistry , vol.24 , pp. 3638-3645
    • Babcock, G.T.1    Widger, W.R.2    Cramer, W.A.3    Oertling, W.A.4    Metz, J.G.5
  • 8
    • 0024298581 scopus 로고
    • Thylakoid membrane protein topography: transmembrane orientation of the chloroplast cytochrome b-559 psbE gene product
    • Tae G.-S., Black M.T., Cramer W.A., Vallon O., Bogorad L. Thylakoid membrane protein topography: transmembrane orientation of the chloroplast cytochrome b-559 psbE gene product. Biochemistry 1988, 27:9075-9080.
    • (1988) Biochemistry , vol.27 , pp. 9075-9080
    • Tae, G.-S.1    Black, M.T.2    Cramer, W.A.3    Vallon, O.4    Bogorad, L.5
  • 9
    • 0027965572 scopus 로고
    • Topography of the heme prosthetic group of cytochrome b559 in photosystem II reaction center
    • Tae G.-S., Cramer W.A. Topography of the heme prosthetic group of cytochrome b559 in photosystem II reaction center. Biochemistry 1994, 33:10060-10068.
    • (1994) Biochemistry , vol.33 , pp. 10060-10068
    • Tae, G.-S.1    Cramer, W.A.2
  • 10
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8Å resolution
    • Zouni A., Witt H.-T., Kern J., Fromme P., Krauss N., Saenger W., Orth P. Crystal structure of photosystem II from Synechococcus elongatus at 3.8Å resolution. Nature 2001, 409:739-743.
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.-T.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6    Orth, P.7
  • 11
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen evolving photosystem II from Thermosynechococcus vulcanus at 3.7Å resolution
    • Kamiya N., Shen J.R. Crystal structure of oxygen evolving photosystem II from Thermosynechococcus vulcanus at 3.7Å resolution. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:98-103.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.R.2
  • 13
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0Å resolution structure of photosystem II
    • Loll B., Kern J., Saenger W., Zouni A., Biesiadka J. Towards complete cofactor arrangement in the 3.0Å resolution structure of photosystem II. Nature 2005, 438:1040-1044.
    • (2005) Nature , vol.438 , pp. 1040-1044
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 14
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial photosystem II at 2.9-A° resolution and the role of quinones, lipids, channels and chloride
    • Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W. Cyanobacterial photosystem II at 2.9-A° resolution and the role of quinones, lipids, channels and chloride. Nat. Struc. Mol. Biol. 2009, 16:334-342.
    • (2009) Nat. Struc. 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
  • 16
    • 0023953589 scopus 로고
    • Redox acid-base characterization of cytochrome b-559 in photosystem II particles
    • Ortega J.M., Hervás M., Losada M. Redox acid-base characterization of cytochrome b-559 in photosystem II particles. Eur. J. Biochem. 1988, 171:449-455.
    • (1988) Eur. J. Biochem. , vol.171 , pp. 449-455
    • Ortega, J.M.1    Hervás, M.2    Losada, M.3
  • 17
    • 0033534159 scopus 로고    scopus 로고
    • Redox and spectral properties of cytochrome b559 in different preparations of photosystem II
    • Kaminskaya O., Kurreck J., Irrgang K.D., Renger G., Shuvalov V. Redox and spectral properties of cytochrome b559 in different preparations of photosystem II. Biochemistry 1999, 38:16223-16235.
    • (1999) Biochemistry , vol.38 , pp. 16223-16235
    • Kaminskaya, O.1    Kurreck, J.2    Irrgang, K.D.3    Renger, G.4    Shuvalov, V.5
  • 18
    • 0034786927 scopus 로고    scopus 로고
    • Factors determining the special redox properties of photosynthetic cytochrome b559
    • Roncel M., Ortega J.M., Losada M. Factors determining the special redox properties of photosynthetic cytochrome b559. Eur. J. Biochem. 2001, 268:4961-4968.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4961-4968
    • Roncel, M.1    Ortega, J.M.2    Losada, M.3
  • 19
    • 0027179104 scopus 로고
    • The redox properties of cytochromes b imposed by the membrane electrostatic environment
    • Krishtalik L.I., Tae G.-S., Cherepanov D.A., Cramer W.A. The redox properties of cytochromes b imposed by the membrane electrostatic environment. Biophys. J. 1993, 65:184-195.
    • (1993) Biophys. J. , vol.65 , pp. 184-195
    • Krishtalik, L.I.1    Tae, G.-S.2    Cherepanov, D.A.3    Cramer, W.A.4
  • 20
    • 0026454816 scopus 로고
    • Molecular changes following oxidoreduction of cytochrome b559 characterized by Fourier transform infrared difference spectroscopy and electron paramagnetic resonance: photooxidation in photosystem II and electrochemistry of isolated cytochrome b559 and iron protoporphyrin IX-bisimidazole model compounds
    • Berthomieu C., Boussac A., Mantele W., Breton J., Nabedryk E. Molecular changes following oxidoreduction of cytochrome b559 characterized by Fourier transform infrared difference spectroscopy and electron paramagnetic resonance: photooxidation in photosystem II and electrochemistry of isolated cytochrome b559 and iron protoporphyrin IX-bisimidazole model compounds. Biochemistry 1992, 31:11460-11471.
    • (1992) Biochemistry , vol.31 , pp. 11460-11471
    • Berthomieu, C.1    Boussac, A.2    Mantele, W.3    Breton, J.4    Nabedryk, E.5
  • 21
    • 34249795159 scopus 로고    scopus 로고
    • Two reaction pathways for transformation of high potential cytochrome b559 of PS II into the intermediate potential form
    • Kaminskaya O., Shuvalov V.A., Renger G. Two reaction pathways for transformation of high potential cytochrome b559 of PS II into the intermediate potential form. Biochim. Biophys. Acta 2007, 1767:550-558.
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 550-558
    • Kaminskaya, O.1    Shuvalov, V.A.2    Renger, G.3
  • 22
    • 33846617289 scopus 로고    scopus 로고
    • Evidence for a novel quinone binding site in the photosystem II complex that regulates the redox potential of cytochrome b559
    • Kaminskaya O., Shuvalov V.A., Renger G. Evidence for a novel quinone binding site in the photosystem II complex that regulates the redox potential of cytochrome b559. Biochemistry 2007, 46:1091-1105.
    • (2007) Biochemistry , vol.46 , pp. 1091-1105
    • Kaminskaya, O.1    Shuvalov, V.A.2    Renger, G.3
  • 23
    • 0001534244 scopus 로고
    • PH-dependent photoreactions of the high- and low-potential forms of cytochrome b559 in spinach PSII-enriched membranes
    • Ortega J.M., Hervás M., De la Rosa M.A., Losada M. pH-dependent photoreactions of the high- and low-potential forms of cytochrome b559 in spinach PSII-enriched membranes. Photosynth. Res. 1995, 46:185-191.
    • (1995) Photosynth. Res. , vol.46 , pp. 185-191
    • Ortega, J.M.1    Hervás, M.2    De la Rosa, M.A.3    Losada, M.4
  • 24
    • 0000485416 scopus 로고
    • PH sensitivity of the redox state of cytochrome b559 may regulate its function as a protectant against donor and acceptor side photoinhibition
    • De Las Rivas J., Klein J., Barber J. pH sensitivity of the redox state of cytochrome b559 may regulate its function as a protectant against donor and acceptor side photoinhibition. Photosynth. Res. 1995, 46:193-202.
    • (1995) Photosynth. Res. , vol.46 , pp. 193-202
    • De Las Rivas, J.1    Klein, J.2    Barber, J.3
  • 25
    • 52449100064 scopus 로고    scopus 로고
    • Heat-induced changes in the EPR signal of tyrosine D (YDOX): a possible role of cytochrome b559
    • Tiwari A., Jajoo A., Bharti S. Heat-induced changes in the EPR signal of tyrosine D (YDOX): a possible role of cytochrome b559. J. Bioenerg. Biomembr. 2008, 40:237-243.
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 237-243
    • Tiwari, A.1    Jajoo, A.2    Bharti, S.3
  • 26
    • 0028820946 scopus 로고
    • Restoration of the high potential form of cytochrome b-559 through the photoreactivation of Tris-inactivated oxygen evolving center
    • Mizusawa N., Ebina M., Yamashita T. Restoration of the high potential form of cytochrome b-559 through the photoreactivation of Tris-inactivated oxygen evolving center. Photosynth. Res. 1995, 45:71-77.
    • (1995) Photosynth. Res. , vol.45 , pp. 71-77
    • Mizusawa, N.1    Ebina, M.2    Yamashita, T.3
  • 27
    • 67649413283 scopus 로고    scopus 로고
    • Superoxide oxidase and reductase activity of cytochrome b559 in photosystem II
    • Tiwari A., Pospíšil P. Superoxide oxidase and reductase activity of cytochrome b559 in photosystem II. Biochim. Biophys. Acta 2009, 1787:985-994.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 985-994
    • Tiwari, A.1    Pospíšil, P.2
  • 28
    • 0033543222 scopus 로고    scopus 로고
    • Interconversion of low- and high-potential forms of cytochrome b559 in tris-washed photosystem II membranes under aerobic and anaerobic conditions
    • Gadjieva R., Mamedov F., Renger G., Styring S. Interconversion of low- and high-potential forms of cytochrome b559 in tris-washed photosystem II membranes under aerobic and anaerobic conditions. Biochemistry 1999, 38:10578-10589.
    • (1999) Biochemistry , vol.38 , pp. 10578-10589
    • Gadjieva, R.1    Mamedov, F.2    Renger, G.3    Styring, S.4
  • 29
    • 34547814628 scopus 로고    scopus 로고
    • Oxygen-induced changes in the redox state of the cytochrome b559 in photosystem II depend on the integrity of the Mn cluster
    • Mamedov F., Gadjieva R., Styring S. Oxygen-induced changes in the redox state of the cytochrome b559 in photosystem II depend on the integrity of the Mn cluster. Physiol. Plant. 2007, 131:41-49.
    • (2007) Physiol. Plant. , vol.131 , pp. 41-49
    • Mamedov, F.1    Gadjieva, R.2    Styring, S.3
  • 30
    • 0033005863 scopus 로고    scopus 로고
    • Restoration of the high-potential form of cytochrome b559 of photosystem II occurs via a two-step mechanism under illumination in the presence of manganese ions
    • Mizusawa N., Yamashita T., Miyao M. Restoration of the high-potential form of cytochrome b559 of photosystem II occurs via a two-step mechanism under illumination in the presence of manganese ions. Biochim. Biophys. Acta 1999, 1410:273-286.
    • (1999) Biochim. Biophys. Acta , vol.1410 , pp. 273-286
    • Mizusawa, N.1    Yamashita, T.2    Miyao, M.3
  • 31
    • 0031036838 scopus 로고    scopus 로고
    • Restoration of the high potential form of cytochrome b-559 by electron transport reactions through Photosystem II in tris-treated Photosystem II membranes
    • Mizusawa N., Miyao M., Yamashita T. Restoration of the high potential form of cytochrome b-559 by electron transport reactions through Photosystem II in tris-treated Photosystem II membranes. Biochim. Biophys. Acta 1997, 1318:145-158.
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 145-158
    • Mizusawa, N.1    Miyao, M.2    Yamashita, T.3
  • 32
    • 0000075484 scopus 로고
    • A highly resolved, oxygen-evolving photosystem II preparation from spinach thlakoid membranes. EPR and electron-transport properties
    • Berthold D.A., Babcock G.T., Yocum C.F. A highly resolved, oxygen-evolving photosystem II preparation from spinach thlakoid membranes. EPR and electron-transport properties. FEBS Lett. 1981, 134:231-234.
    • (1981) FEBS Lett. , vol.134 , pp. 231-234
    • Berthold, D.A.1    Babcock, G.T.2    Yocum, C.F.3
  • 33
    • 0001625998 scopus 로고
    • Isolation of a photosystem II preparation from higher plants with highly enriched oxygen evolution activity
    • Ford R.C., Evans M.C.W. Isolation of a photosystem II preparation from higher plants with highly enriched oxygen evolution activity. FEBS Lett. 1983, 160:159-164.
    • (1983) FEBS Lett. , vol.160 , pp. 159-164
    • Ford, R.C.1    Evans, M.C.W.2
  • 34
    • 0027144617 scopus 로고
    • Modification of histidine residues of photosystem II by diethylpyrocarbonate inhibits the electron transfer between the primary (QA) and secondary (QB) quinone acceptors
    • Hegde U., Padhye S., Kovács L., Vozár A., Demeter S. Modification of histidine residues of photosystem II by diethylpyrocarbonate inhibits the electron transfer between the primary (QA) and secondary (QB) quinone acceptors. Z. Naturforsch. 1993, 48c:896-902.
    • (1993) Z. Naturforsch. , vol.48 c , pp. 896-902
    • Hegde, U.1    Padhye, S.2    Kovács, L.3    Vozár, A.4    Demeter, S.5
  • 35
    • 42349091083 scopus 로고    scopus 로고
    • Protein surface mapping using diethylpyrocarbonate with mass spectrometric detection
    • Mendoza V.L., Vachet R.W. Protein surface mapping using diethylpyrocarbonate with mass spectrometric detection. Anal. Chem. 2008, 80:2895-2904.
    • (2008) Anal. Chem. , vol.80 , pp. 2895-2904
    • Mendoza, V.L.1    Vachet, R.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.