메뉴 건너뛰기




Volumn 113, Issue 3, 2016, Pages 620-625

Redox potential of the terminal quinone electron acceptor QB in photosystem II reveals the mechanism of electron transfer regulation

Author keywords

FTIR; Photosynthesis; Spectroelectrochemistry

Indexed keywords

MANGANESE; QUINONE DERIVATIVE; PHOTOSYSTEM II;

EID: 84955295340     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1520211113     Document Type: Article
Times cited : (64)

References (65)
  • 1
    • 57749104826 scopus 로고    scopus 로고
    • Photosynthetic energy conversion: Natural and artificial
    • Barber J (2009) Photosynthetic energy conversion: Natural and artificial. Chem Soc Rev 38(1):185-196.
    • (2009) Chem Soc Rev , vol.38 , Issue.1 , pp. 185-196
    • Barber, J.1
  • 2
    • 84859926501 scopus 로고    scopus 로고
    • Photosynthetic water splitting: Apparatus and mechanism
    • eds Eaton-Rye JJ, Tripathy BC, Sharkey TD (Springer, Dordrecht, The Netherlands)
    • Renger G (2012) Photosynthetic water splitting: Apparatus and mechanism. Photosynthesis: Plastid Biology, Energy Conversion and Carbon Assimilation, eds Eaton-Rye JJ, Tripathy BC, Sharkey TD (Springer, Dordrecht, The Netherlands), pp 359-414.
    • (2012) Photosynthesis: Plastid Biology, Energy Conversion and Carbon Assimilation , pp. 359-414
    • Renger, G.1
  • 3
    • 84859901668 scopus 로고    scopus 로고
    • 2 evolution
    • eds Wydrzynski T, Hillier W (Royal Society of Chemistry, Cambridge, UK)
    • 2 evolution. Molecular Solar Fuels, eds Wydrzynski T, Hillier W (Royal Society of Chemistry, Cambridge, UK), pp 163-207.
    • (2011) Molecular Solar Fuels , pp. 163-207
    • Messinger, J.1    Noguchi, T.2    Yano, J.3
  • 4
    • 38049011376 scopus 로고    scopus 로고
    • 4Ca cluster and to the evolution of molecular oxygen in photosystem II
    • 4Ca cluster and to the evolution of molecular oxygen in photosystem II. Coord Chem Rev 252(3-4):259-272.
    • (2008) Coord Chem Rev , vol.252 , Issue.3-4 , pp. 259-272
    • Rappaport, F.1    Diner, B.A.2
  • 5
    • 82755181814 scopus 로고    scopus 로고
    • Charge separation in photosystem II: A comparative and evolutionary overview
    • Cardona T, Sedoud A, Cox N, Rutherford AW (2012) Charge separation in photosystem II: A comparative and evolutionary overview. Biochim Biophys Acta 1817(1):26-43.
    • (2012) Biochim Biophys Acta , vol.1817 , Issue.1 , pp. 26-43
    • Cardona, T.1    Sedoud, A.2    Cox, N.3    Rutherford, A.W.4
  • 6
    • 84980182243 scopus 로고
    • Model of the System II photochemical centers
    • Joliot P, Barbieri G, Chabaud R (1969) Model of the System II photochemical centers. Photochem Photobiol 10(5):309-329.
    • (1969) Photochem Photobiol , vol.10 , Issue.5 , pp. 309-329
    • Joliot, P.1    Barbieri, G.2    Chabaud, R.3
  • 10
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial photosystem II at 2.9-Å resolution and the role of quinones, lipids, channels and chloride
    • Guskov A, et al. (2009) Cyanobacterial photosystem II at 2.9-Å resolution and the role of quinones, lipids, channels and chloride. Nat Struct Mol Biol 16(3):334-342.
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.3 , pp. 334-342
    • Guskov, A.1
  • 11
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygenevolving photosystem II at a resolution of 1.9 Å
    • Umena Y, Kawakami K, Shen J-R, Kamiya N (2011) Crystal structure of oxygenevolving photosystem II at a resolution of 1.9 Å. Nature 473(7345):55-60.
    • (2011) Nature , vol.473 , Issue.7345 , pp. 55-60
    • Umena, Y.1    Kawakami, K.2    Shen, J.-R.3    Kamiya, N.4
  • 12
    • 84872585486 scopus 로고    scopus 로고
    • Mechanism of proton-coupled quinone reduction in photosystem II
    • Saito K, Rutherford AW, Ishikita H (2013) Mechanism of proton-coupled quinone reduction in photosystem II. Proc Natl Acad Sci USA 110(3):954-959.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.3 , pp. 954-959
    • Saito, K.1    Rutherford, A.W.2    Ishikita, H.3
  • 13
    • 84901759373 scopus 로고    scopus 로고
    • Effects of hydrogen bonding interactions on the redox potential and molecular vibrations of plastoquinone as studied using density functional theory calculations
    • Ashizawa R, Noguchi T (2014) Effects of hydrogen bonding interactions on the redox potential and molecular vibrations of plastoquinone as studied using density functional theory calculations. Phys Chem Chem Phys 16(24):11864-11876.
    • (2014) Phys Chem Chem Phys , vol.16 , Issue.24 , pp. 11864-11876
    • Ashizawa, R.1    Noguchi, T.2
  • 15
    • 57849150806 scopus 로고    scopus 로고
    • Singlet oxygen production in photosystem II and related protection mechanism
    • Krieger-Liszkay A, Fufezan C, Trebst A (2008) Singlet oxygen production in photosystem II and related protection mechanism. Photosynth Res 98(1-3):551-564.
    • (2008) Photosynth Res , vol.98 , Issue.1-3 , pp. 551-564
    • Krieger-Liszkay, A.1    Fufezan, C.2    Trebst, A.3
  • 16
    • 63549106377 scopus 로고    scopus 로고
    • Janus-faced charge recombinations in photosystem II photoinhibition
    • Vass I, Cser K (2009) Janus-faced charge recombinations in photosystem II photoinhibition. Trends Plant Sci 14(4):200-205.
    • (2009) Trends Plant Sci , vol.14 , Issue.4 , pp. 200-205
    • Vass, I.1    Cser, K.2
  • 17
    • 79954575978 scopus 로고    scopus 로고
    • Role of charge recombination processes in photodamage and photoprotection of the photosystem II complex
    • Vass I (2011) Role of charge recombination processes in photodamage and photoprotection of the photosystem II complex. Physiol Plant 142(1):6-16.
    • (2011) Physiol Plant , vol.142 , Issue.1 , pp. 6-16
    • Vass, I.1
  • 18
    • 37549052159 scopus 로고    scopus 로고
    • Differential regulation of psbA and psbD gene expression, and the role of the different D1 protein copies in the cyanobacterium Thermosynechococcus elongatus BP-1
    • Kós PB, Deák Z, Cheregi O, Vass I (2008) Differential regulation of psbA and psbD gene expression, and the role of the different D1 protein copies in the cyanobacterium Thermosynechococcus elongatus BP-1. Biochim Biophys Acta 1777(1):74-83.
    • (2008) Biochim Biophys Acta , vol.1777 , Issue.1 , pp. 74-83
    • Kós, P.B.1    Deák, Z.2    Cheregi, O.3    Vass, I.4
  • 19
    • 0032534935 scopus 로고    scopus 로고
    • Modulation of quantum yield of primary radical pair formation in photosystem II by site-directed mutagenesis affecting radical cations and anions
    • Merry SA, et al. (1998) Modulation of quantum yield of primary radical pair formation in photosystem II by site-directed mutagenesis affecting radical cations and anions. Biochemistry 37(50):17439-17447.
    • (1998) Biochemistry , vol.37 , Issue.50 , pp. 17439-17447
    • Merry, S.A.1
  • 20
    • 74949118292 scopus 로고    scopus 로고
    • Hydrogen bond interactions of the pheophytin electron acceptor and its radical anion in photosystem II as revealed by Fourier transform infrared difference spectroscopy
    • Shibuya Y, et al. (2010) Hydrogen bond interactions of the pheophytin electron acceptor and its radical anion in photosystem II as revealed by Fourier transform infrared difference spectroscopy. Biochemistry 49(3):493-501.
    • (2010) Biochemistry , vol.49 , Issue.3 , pp. 493-501
    • Shibuya, Y.1
  • 21
    • 0002561024 scopus 로고
    • Energy-dependent of chlorophyll-A-fluorescence: The involvement of proton-calcium exchange at photosystem 2
    • Krieger A, Weis E (1992) Energy-dependent of chlorophyll-a-fluorescence: The involvement of proton-calcium exchange at photosystem 2. Photosynthetica 27(1-2): 89-98.
    • (1992) Photosynthetica , vol.27 , Issue.1-2 , pp. 89-98
    • Krieger, A.1    Weis, E.2
  • 24
    • 70449580488 scopus 로고    scopus 로고
    • A in photosystem II from Thermosynechococcus elongatus determined by spectroelectrochemistry
    • A in photosystem II from Thermosynechococcus elongatus determined by spectroelectrochemistry. Biochemistry 48(45):10682-10684.
    • (2009) Biochemistry , vol.48 , Issue.45 , pp. 10682-10684
    • Shibamoto, T.1    Kato, Y.2    Sugiura, M.3    Watanabe, T.4
  • 25
    • 77951298267 scopus 로고    scopus 로고
    • A in photosystem II verified by spectroelectrochemistry
    • A in photosystem II verified by spectroelectrochemistry. FEBS Lett 584(8):1526-1530.
    • (2010) FEBS Lett , vol.584 , Issue.8 , pp. 1526-1530
    • Shibamoto, T.1
  • 26
    • 79958004732 scopus 로고    scopus 로고
    • A quinone electron acceptor in photosystem II of Thermosynechococcus elongatus and spinach
    • A quinone electron acceptor in photosystem II of Thermosynechococcus elongatus and spinach. J Photochem Photobiol B 104(1-2):154-157.
    • (2011) J Photochem Photobiol B , vol.104 , Issue.1-2 , pp. 154-157
    • Ido, K.1
  • 27
    • 79956351003 scopus 로고    scopus 로고
    • - and conserved energetics of photosystem II in cyanobacteria with chlorophyll a and chlorophyll d
    • - and conserved energetics of photosystem II in cyanobacteria with chlorophyll a and chlorophyll d. Proc Natl Acad Sci USA 108(19):8054-8058.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.19 , pp. 8054-8058
    • Allakhverdiev, S.I.1
  • 28
    • 0017772395 scopus 로고
    • Dependence of the deactivation reactions of photosystem II on the redox state of plastoquinone pool A varied under anaerobic conditions; Equilibria on the acceptor side of photosystem II
    • Diner BA (1977) Dependence of the deactivation reactions of photosystem II on the redox state of plastoquinone pool A varied under anaerobic conditions; equilibria on the acceptor side of photosystem II. Biochim Biophys Acta 460(2):247-258.
    • (1977) Biochim Biophys Acta , vol.460 , Issue.2 , pp. 247-258
    • Diner, B.A.1
  • 29
    • 49049126264 scopus 로고
    • Kinetics of the oxidation-reduction reactions of the photosystem II quinone acceptor complex, and the pathway for deactivation
    • Robinson HH, Crofts AR (1983) Kinetics of the oxidation-reduction reactions of the photosystem II quinone acceptor complex, and the pathway for deactivation. FEBS Lett 153(1):221-226.
    • (1983) FEBS Lett , vol.153 , Issue.1 , pp. 221-226
    • Robinson, H.H.1    Crofts, A.R.2
  • 30
    • 48749143707 scopus 로고
    • The electrochemical domain of photosynthesis
    • Crofts AR, Wraight CA (1983) The electrochemical domain of photosynthesis. Biochim Biophys Acta 726(3):149-185.
    • (1983) Biochim Biophys Acta , vol.726 , Issue.3 , pp. 149-185
    • Crofts, A.R.1    Wraight, C.A.2
  • 31
    • 0033547703 scopus 로고    scopus 로고
    • B in photosystem II is thermodynamically perturbed in phototolerant mutants of Synechocystis sp. PCC 6803
    • B in photosystem II is thermodynamically perturbed in phototolerant mutants of Synechocystis sp. PCC 6803. Biochemistry 38(2):770-775.
    • (1999) Biochemistry , vol.38 , Issue.2 , pp. 770-775
    • Minagawa, J.1    Narusaka, Y.2    Inoue, Y.3    Satoh, K.4
  • 32
    • 57849125414 scopus 로고    scopus 로고
    • B redox potential: Analysis of thermoluminescence and fluorescence measurements
    • B redox potential: Analysis of thermoluminescence and fluorescence measurements. Photosynth Res 98(1-3):449-468.
    • (2008) Photosynth Res , vol.98 , Issue.1-3 , pp. 449-468
    • Rose, S.1
  • 33
    • 79957992189 scopus 로고    scopus 로고
    • Photosystem II fluorescence: Slow changes-scaling from the past
    • Papageorgiou GC, Govindjee (2011) Photosystem II fluorescence: Slow changes-scaling from the past. J Photochem Photobiol B 104(1-2):258-270.
    • (2011) J Photochem Photobiol B , vol.104 , Issue.1-2 , pp. 258-270
    • Papageorgiou, G.C.1    Govindjee2
  • 34
    • 0025089975 scopus 로고
    • Chlorophyll a fluorescence transient as an indicator of active and inactive photosystem II in thylakoid membranes
    • Cao J, Govindjee (1990) Chlorophyll a fluorescence transient as an indicator of active and inactive photosystem II in thylakoid membranes. Biochim Biophys Acta 1015(2): 180-188.
    • (1990) Biochim Biophys Acta , vol.1015 , Issue.2 , pp. 180-188
    • Cao, J.1    Govindjee2
  • 35
    • 0032914373 scopus 로고    scopus 로고
    • Chlorophyll a fluorescence induction
    • Lazár D (1999) Chlorophyll a fluorescence induction. Biochim Biophys Acta 1412(1): 1-28.
    • (1999) Biochim Biophys Acta , vol.1412 , Issue.1 , pp. 1-28
    • Lazár, D.1
  • 36
    • 0016158876 scopus 로고
    • Identification of the reduced primary electron acceptor of photosystem II as a bound semiquinone anion
    • van Gorkom HJ (1974) Identification of the reduced primary electron acceptor of photosystem II as a bound semiquinone anion. Biochim Biophys Acta 347(3):439-442.
    • (1974) Biochim Biophys Acta , vol.347 , Issue.3 , pp. 439-442
    • Van Gorkom, H.J.1
  • 37
    • 0017097975 scopus 로고
    • Absorbance changes due to the charge-accumulating species in system 2 of photosynthesis
    • Pulles MPJ, Van Gorkom HJ, Willemsen JG (1976) Absorbance changes due to the charge-accumulating species in system 2 of photosynthesis. Biochim Biophys Acta 449(3):536-540.
    • (1976) Biochim Biophys Acta , vol.449 , Issue.3 , pp. 536-540
    • Pulles, M.P.J.1    Van Gorkom, H.J.2    Willemsen, J.G.3
  • 38
    • 25444441462 scopus 로고    scopus 로고
    • Secondary quinone in photosystem II of Thermosynechococcus elongatus: Semiquinone-iron EPR signals and temperature dependence of electron transfer
    • Fufezan C, Zhang C, Krieger-Liszkay A, Rutherford AW (2005) Secondary quinone in photosystem II of Thermosynechococcus elongatus: Semiquinone-iron EPR signals and temperature dependence of electron transfer. Biochemistry 44(38):12780-12789.
    • (2005) Biochemistry , vol.44 , Issue.38 , pp. 12780-12789
    • Fufezan, C.1    Zhang, C.2    Krieger-Liszkay, A.3    Rutherford, A.W.4
  • 39
    • 79959990120 scopus 로고    scopus 로고
    • 2+
    • 2+. Biochemistry 50(27):6012-6021.
    • (2011) Biochemistry , vol.50 , Issue.27 , pp. 6012-6021
    • Sedoud, A.1
  • 40
    • 0027316209 scopus 로고
    • Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms
    • Mäntele W (1993) Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms. Trends Biochem Sci 18(6):197-202.
    • (1993) Trends Biochem Sci , vol.18 , Issue.6 , pp. 197-202
    • Mäntele, W.1
  • 41
    • 32344439352 scopus 로고    scopus 로고
    • Molecular analysis by vibrational spectroscopy
    • eds Wydrzynski T, Satoh K (Springer, Dordrecht, The Netherlands)
    • Noguchi T, Berthomieu C (2005) Molecular analysis by vibrational spectroscopy. Photosystem II: The Light-Driven Water:Plastoquinone Oxidoreductase, eds Wydrzynski T, Satoh K (Springer, Dordrecht, The Netherlands), pp 367-387.
    • (2005) Photosystem II: The Light-Driven Water:Plastoquinone Oxidoreductase , pp. 367-387
    • Noguchi, T.1    Berthomieu, C.2
  • 42
    • 72149119691 scopus 로고    scopus 로고
    • Fourier transform infrared (FTIR) spectroscopy
    • Berthomieu C, Hienerwadel R (2009) Fourier transform infrared (FTIR) spectroscopy. Photosynth Res 101(2-3):157-170.
    • (2009) Photosynth Res , vol.101 , Issue.2-3 , pp. 157-170
    • Berthomieu, C.1    Hienerwadel, R.2
  • 43
    • 84894245431 scopus 로고    scopus 로고
    • Fourier transform infrared difference spectroscopy for studying the molecular mechanism of photosynthetic water oxidation
    • Chu H-A (2013) Fourier transform infrared difference spectroscopy for studying the molecular mechanism of photosynthetic water oxidation. Front Plant Sci 4:146.
    • (2013) Front Plant Sci , vol.4 , pp. 146
    • Chu, H.-A.1
  • 44
    • 84911392175 scopus 로고    scopus 로고
    • 5 cluster in photosystem II
    • 5 cluster in photosystem II. Biochim Biophys Acta 1847(1):19-34.
    • (2015) Biochim Biophys Acta , vol.1847 , Issue.1 , pp. 19-34
    • Debus, R.J.1
  • 45
    • 84911386756 scopus 로고    scopus 로고
    • Fourier transform infrared difference and time-resolved infrared detection of the electron and proton transfer dynamics in photosynthetic water oxidation
    • Noguchi T (2015) Fourier transform infrared difference and time-resolved infrared detection of the electron and proton transfer dynamics in photosynthetic water oxidation. Biochim Biophys Acta 1847(1):35-45.
    • (2015) Biochim Biophys Acta , vol.1847 , Issue.1 , pp. 35-45
    • Noguchi, T.1
  • 47
    • 0018115502 scopus 로고
    • Redox potentiometry: Determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems
    • Dutton PL (1978) Redox potentiometry: Determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems. Methods Enzymol 54:411-435.
    • (1978) Methods Enzymol , vol.54 , pp. 411-435
    • Dutton, P.L.1
  • 48
    • 84881624897 scopus 로고    scopus 로고
    • Recent advances in the electrochemistry and spectroelectrochemistry of membrane proteins
    • Melin F, Hellwig P (2013) Recent advances in the electrochemistry and spectroelectrochemistry of membrane proteins. Biol Chem 394(5):593-609.
    • (2013) Biol Chem , vol.394 , Issue.5 , pp. 593-609
    • Melin, F.1    Hellwig, P.2
  • 49
    • 70350434324 scopus 로고    scopus 로고
    • Spectroelectrochemical determination of the redox potential of pheophytin a, the primary electron acceptor in photosystem II
    • Kato Y, Sugiura M, Oda A, Watanabe T (2009) Spectroelectrochemical determination of the redox potential of pheophytin a, the primary electron acceptor in photosystem II. Proc Natl Acad Sci USA 106(41):17365-17370.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.41 , pp. 17365-17370
    • Kato, Y.1    Sugiura, M.2    Oda, A.3    Watanabe, T.4
  • 50
    • 84905693401 scopus 로고    scopus 로고
    • 5 cluster and the non-heme iron center in photosystem II as revealed by FTIR spectroelectrochemistry
    • 5 cluster and the non-heme iron center in photosystem II as revealed by FTIR spectroelectrochemistry. Biochemistry 53(30):4914-4923.
    • (2014) Biochemistry , vol.53 , Issue.30 , pp. 4914-4923
    • Kato, Y.1    Noguchi, T.2
  • 51
    • 0000627943 scopus 로고
    • Infrared spectroelectrochemistry of bacteriochlorophylls and bacteriopheophytins: Implications for the binding of the pigments in the reaction center from photosynthetic bacteria
    • Mäntele WG, Wollenweber AM, Nabedryk E, Breton J (1988) Infrared spectroelectrochemistry of bacteriochlorophylls and bacteriopheophytins: Implications for the binding of the pigments in the reaction center from photosynthetic bacteria. Proc Natl Acad Sci USA 85(22):8468-8472.
    • (1988) Proc Natl Acad Sci USA , vol.85 , Issue.22 , pp. 8468-8472
    • Mäntele, W.G.1    Wollenweber, A.M.2    Nabedryk, E.3    Breton, J.4
  • 52
    • 0025054951 scopus 로고
    • Investigation of models for photosynthetic electron acceptors: Infrared spectroelectrochemistry of ubiquinone and its anions
    • Bauscher M, Nabedryk E, Bagley K, Breton J, Mäntele W (1990) Investigation of models for photosynthetic electron acceptors: Infrared spectroelectrochemistry of ubiquinone and its anions. FEBS Lett 261(1):191-195.
    • (1990) FEBS Lett , vol.261 , Issue.1 , pp. 191-195
    • Bauscher, M.1    Nabedryk, E.2    Bagley, K.3    Breton, J.4    Mäntele, W.5
  • 53
    • 0001016808 scopus 로고
    • OTTLE cell study of the UV-visible and FTIR spectroelectrochemistry of the radical anion and dianion of 1,4-benzoquinone in DMSO solutions
    • Gamage RSKA, Umapathy S, McQuillan AJ (1990) OTTLE cell study of the UV-visible and FTIR spectroelectrochemistry of the radical anion and dianion of 1,4-benzoquinone in DMSO solutions. J Electroanal Chem 284(1):229-235.
    • (1990) J Electroanal Chem , vol.284 , Issue.1 , pp. 229-235
    • Gamage, R.S.K.A.1    Umapathy, S.2    McQuillan, A.J.3
  • 54
    • 23744445165 scopus 로고    scopus 로고
    • Spectroelectrochemistry of hydrogenase enzymes and related compounds
    • Best SP (2005) Spectroelectrochemistry of hydrogenase enzymes and related compounds. Coord Chem Rev 249(15-16):1536-1554.
    • (2005) Coord Chem Rev , vol.249 , Issue.15-16 , pp. 1536-1554
    • Best, S.P.1
  • 56
    • 57849137466 scopus 로고    scopus 로고
    • A in photosystem II as studied by Fourier transform infrared spectroscopy
    • A in photosystem II as studied by Fourier transform infrared spectroscopy. Photosynth Res 98(1-3):159-167.
    • (2008) Photosynth Res , vol.98 , Issue.1-3 , pp. 159-167
    • Takano, A.1    Takahashi, R.2    Suzuki, H.3    Noguchi, T.4
  • 57
    • 0028948099 scopus 로고
    • 2+ in the photosynthetic oxygen-evolving center by means of Fourier transform infrared spectroscopy
    • 2+ in the photosynthetic oxygen-evolving center by means of Fourier transform infrared spectroscopy. Biochim Biophys Acta 1228(2-3):189-200.
    • (1995) Biochim Biophys Acta , vol.1228 , Issue.2-3 , pp. 189-200
    • Noguchi, T.1    Ono, T.2    Inoue, Y.3
  • 61
    • 0019316012 scopus 로고
    • The kinetics and thermodynamics of the reduction of cytochrome c by substituted p-benzoquinols in solution
    • Rich PR, Bendall DS (1980) The kinetics and thermodynamics of the reduction of cytochrome c by substituted p-benzoquinols in solution. Biochim Biophys Acta 592(3): 506-518.
    • (1980) Biochim Biophys Acta , vol.592 , Issue.3 , pp. 506-518
    • Rich, P.R.1    Bendall, D.S.2
  • 62
    • 0032535220 scopus 로고    scopus 로고
    • Influence of herbicide binding on the redox potential of the quinone acceptor in photosystem II: Relevance to photodamage and phytotoxicity
    • Krieger-Liszkay A, Rutherford AW (1998) Influence of herbicide binding on the redox potential of the quinone acceptor in photosystem II: Relevance to photodamage and phytotoxicity. Biochemistry 37(50):17339-17344.
    • (1998) Biochemistry , vol.37 , Issue.50 , pp. 17339-17344
    • Krieger-Liszkay, A.1    Rutherford, A.W.2
  • 63
    • 77952389013 scopus 로고    scopus 로고
    • The PsbK subunit is required for the stable assembly and stability of other small subunits in the PSII complex in the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1
    • Iwai M, et al. (2010) The PsbK subunit is required for the stable assembly and stability of other small subunits in the PSII complex in the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1. Plant Cell Physiol 51(4):554-560.
    • (2010) Plant Cell Physiol , vol.51 , Issue.4 , pp. 554-560
    • Iwai, M.1
  • 64
    • 84901030094 scopus 로고    scopus 로고
    • Z and a coupled histidine in photosystem II: Relevance to the proton transfer mechanism of water oxidation
    • Z and a coupled histidine in photosystem II: Relevance to the proton transfer mechanism of water oxidation. Biochemistry 53(19):3131-3144.
    • (2014) Biochemistry , vol.53 , Issue.19 , pp. 3131-3144
    • Nakamura, S.1    Nagao, R.2    Takahashi, R.3    Noguchi, T.4
  • 65
    • 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
    • Sugiura M, Inoue Y (1999) Highly purified thermo-stable oxygen-evolving photosystem II core complex from the thermophilic cyanobacterium Synechococcus elongatus having His-tagged CP43. Plant Cell Physiol 40(12):1219-1231.
    • (1999) Plant Cell Physiol , vol.40 , Issue.12 , pp. 1219-1231
    • Sugiura, M.1    Inoue, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.