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Volumn 51, Issue 34, 2012, Pages 6776-6785

Determination of the miss probabilities of individual s-state transitions during photosynthetic water oxidation by monitoring electron flow in photosystem II using FTIR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ANALYSIS OF VARIOUS; DIFFERENCE SPECTROSCOPY; ELECTRON ACCEPTOR; ELECTRON FLOW; FITTING PARAMETERS; FOURIER TRANSFORM INFRARED; FTIR; FTIR SPECTROSCOPY; MOLECULAR MECHANISM; OSCILLATION PATTERNS; OXIDIZING CENTERS; PHOTOSYNTHETIC WATER OXIDATION; PHOTOSYSTEM II; S STATE; S-STATE TRANSITIONS; SIGNAL AMPLITUDE; SPECTROSCOPIC DATA; STRETCHING BANDS; THERMOSYNECHOCOCCUS ELONGATUS; WATER OXIDATION;

EID: 84867507177     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300708     Document Type: Article
Times cited : (24)

References (75)
  • 1
    • 0026707522 scopus 로고
    • The manganese and calcium ions of photosynthetic oxygen evolution
    • Debus, R. J. (1992) The manganese and calcium ions of photosynthetic oxygen evolution. Biochim. Biophys. Acta 1102, 269-352.
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 269-352
    • Debus, R.J.1
  • 2
    • 33144474992 scopus 로고    scopus 로고
    • Mechanism of photosynthetic oxygen production
    • Wydrzynski, T., and Satoh, K., Eds., Springer, Dordrecht, The Netherlands
    • Hillier, W., and Messinger, J. (2005) Mechanism of photosynthetic oxygen production. In Photosystem II: The Light-Driven Water:Plastoquinone Oxidoreductase (Wydrzynski, T., and Satoh, K., Eds.) pp 567-608, Springer, Dordrecht, The Netherlands.
    • (2005) Photosystem II: The Light-Driven Water:Plastoquinone Oxidoreductase , pp. 567-608
    • Hillier, W.1    Messinger, J.2
  • 3
    • 33751424725 scopus 로고    scopus 로고
    • Water-splitting chemistry of photosystem ii
    • McEvoy, J. P., and Brudvig, G. W. (2006) Water-splitting chemistry of photosystem II. Chem. Rev. 106, 4455-4483.
    • (2006) Chem. Rev , vol.106 , pp. 4455-4483
    • McEvoy, J.P.1    Brudvig, G.W.2
  • 4
    • 84859901668 scopus 로고    scopus 로고
    • 2 evolution
    • (Wydrzynski, T., and Hillier, W., Eds.) Chapter 7, Royal Society of Chemistry, Cambridge, U.K
    • 2 Evolution. In Molecular Solar Fuels (Wydrzynski, T., and Hillier, W., Eds.) Chapter 7, pp 163-207, Royal Society of Chemistry, Cambridge, U.K.
    • (2011) Molecular Solar Fuels , pp. 163-207
    • Messinger, J.1    Noguchi, T.2    Yano, J.3
  • 5
    • 84859926501 scopus 로고    scopus 로고
    • Photosynthetic water splitting: Apparatus and mechanism
    • (Eaton-Rye, J. J., Tripathy, B. C., and Sharkey, T. D., Eds.), Springer, Dordrecht, The Netherlands
    • Renger, G. (2012) Photosynthetic water splitting: Apparatus and mechanism. In Photosynthesis: Plastid Biology, Energy Conversion and Carbon Assimilation (Eaton-Rye, J. J., Tripathy, B. C., and Sharkey, T. D., Eds.) pp 359-414, Springer, Dordrecht, The Netherlands.
    • (2012) Photosynthesis: Plastid Biology, Energy Conversion and Carbon Assimilation , pp. 359-414
    • Renger, G.1
  • 6
    • 82755197864 scopus 로고    scopus 로고
    • Structural models of the manganese complex of photosystem ii and mechanistic implications
    • Grundmeier, A., and Dau, H. (2012) Structural models of the manganese complex of photosystem II and mechanistic implications. Biochim. Biophys. Acta 1817, 88-105.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 88-105
    • Grundmeier, A.1    Dau, H.2
  • 7
    • 0036999722 scopus 로고    scopus 로고
    • Structure, dynamics, and energetics of the primary photochemistry of photosystem ii of oxygenic photosynthesis
    • Diner, B. A., and Rappaport, F. (2002) Structure, dynamics, and energetics of the primary photochemistry of photosystem II of oxygenic photosynthesis. Annu. Rev. Plant Biol. 53, 551-580.
    • (2002) Annu. Rev. Plant Biol , vol.53 , pp. 551-580
    • Diner, B.A.1    Rappaport, F.2
  • 9
    • 33846571216 scopus 로고    scopus 로고
    • The quinone iron acceptor complex
    • (Wydrzynski, T., and Satoh, K., Eds.), Springer, Dordrecht, The Netherlands
    • Petrouleas, V., and Crofts, A. R. (2005) The quinone iron acceptor complex. In Photosystem II: The Light-Driven Water:-Plastoquinone Oxidoreductase (Wydrzynski, T., and Satoh, K., Eds.) pp 177-206, Springer, Dordrecht, The Netherlands.
    • (2005) Photosystem II: The Light-Driven Water: Plastoquinone Oxidoreductase , pp. 177-206
    • Petrouleas, V.1    Crofts, A.R.2
  • 10
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the photosynthetic oxygen-evolving center
    • Ferreira, K. N., Iverson, T. M., Maghlaoui, K., Barber, J., and Iwata, S. (2004) Architecture of the photosynthetic oxygen-evolving center. Science 303, 1831-1838.
    • (2004) Science , vol.303 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 11
    • 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., and Saenger, W. (2009) Cyanobacterial photosystem II at 2.9-A; resolution and the role of quinones, lipids, channels and chloride. Nat. Struct. Mol. Biol. 16, 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
  • 12
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem ii at a resolution of 1.9 a
    • Umena, Y., Kawakami, K., Shen, J. R., and Kamiya, N. (2011) Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 A;. Nature 473, 55-60.
    • (2011) Nature , vol.473 , pp. 55-60
    • Umena, Y.1    Kawakami, K.2    Shen, J.R.3    Kamiya, N.4
  • 14
    • 84980182243 scopus 로고
    • Model of the system ii photochemical centers
    • Joliot, P., Barbieri, G., and Chabaud, R. (1969) Model of the System II photochemical centers. Photochem. Photobiol. 10, 309-329.
    • (1969) Photochem. Photobiol , vol.10 , pp. 309-329
    • Joliot, P.1    Barbieri, G.2    Chabaud, R.3
  • 16
    • 0002232564 scopus 로고
    • Oxygen evolution in photosynthesis
    • (Govindjee, Ed.), Academic Press, New York
    • Joliot, P., and Kok, B. (1975) Oxygen evolution in photosynthesis. In Bioenergetics of Photosynthesis (Govindjee, Ed.) pp 387-412, Academic Press, New York.
    • (1975) Bioenergetics of Photosynthesis , pp. 387-412
    • Joliot, P.1    Kok, B.2
  • 17
    • 84981598890 scopus 로고
    • 2 evolution. Ii. Damping of flash yield oscillation, deactivation
    • 2 evolution. II. Damping of flash yield oscillation, deactivation. Photochem. Photobiol. 14, 307-321.
    • (1971) Photochem. Photobiol , vol.14 , pp. 307-321
    • Forbush, B.1    Kok, B.2    McGloin, M.3
  • 18
    • 0000557847 scopus 로고
    • Studies on the deconvolution of flash-induced absorption changes into the difference spectra of individual redox steps within the water-oxidizing enzyme system
    • Renger, G., and Hanssum, B. (1988) Studies on the deconvolution of flash-induced absorption changes into the difference spectra of individual redox steps within the water-oxidizing enzyme system. Photosynth. Res. 16, 243-259.
    • (1988) Photosynth. Res , vol.16 , pp. 243-259
    • Renger, G.1    Hanssum, B.2
  • 19
    • 0042666844 scopus 로고    scopus 로고
    • Functional differences of photosystem ii from synechococcus elongatus and spinach characterized by flash induced oxygen evolution patterns
    • Isgandarova, S., Renger, G., and Messinger, J. (2003) Functional differences of photosystem II from Synechococcus elongatus and spinach characterized by flash induced oxygen evolution patterns. Biochemistry 42, 8929-8938.
    • (2003) Biochemistry , vol.42 , pp. 8929-8938
    • Isgandarova, S.1    Renger, G.2    Messinger, J.3
  • 20
    • 11244276886 scopus 로고    scopus 로고
    • Flash-induced oxygen evolution in photosynthesis: Simple solution for the extended s-state model that includes misses, double-hits, inactivation, and backward-Transitions
    • Shinkarev, V. P. (2005) Flash-induced oxygen evolution in photosynthesis: Simple solution for the extended S-state model that includes misses, double-hits, inactivation, and backward-Transitions. Biophys. J. 88, 412-421.
    • (2005) Biophys. J , vol.88 , pp. 412-421
    • Shinkarev, V.P.1
  • 21
    • 0019878531 scopus 로고
    • Investigation of double turnovers in photosystem ii charge separation and oxygen evolution with excitation flashes of different duration
    • Jursinic, P. (1981) Investigation of double turnovers in photosystem II charge separation and oxygen evolution with excitation flashes of different duration. Biochim. Biophys. Acta 635, 38-52.
    • (1981) Biochim. Biophys. Acta , vol.635 , pp. 38-52
    • Jursinic, P.1
  • 22
    • 84915719434 scopus 로고
    • Evidence for unequal misses in oxygen flash yield sequence in photosynthesis
    • Delrieu, M. J. (1983) Evidence for unequal misses in oxygen flash yield sequence in photosynthesis. Z. Naturforsch. C38, 247-258.
    • (1983) Z. Naturforsch. C38 , pp. 247-258
    • Delrieu, M.J.1
  • 23
    • 0027499508 scopus 로고
    • Oxygen evolution in photosynthesis: From unicycle to bicycle
    • Shinkarev, V. P., and Wraight, C. A. (1993) Oxygen evolution in photosynthesis: From unicycle to bicycle. Proc. Natl. Acad. Sci. U.S.A. 90, 1834-1838.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 1834-1838
    • Shinkarev, V.P.1    Wraight, C.A.2
  • 24
    • 0036319706 scopus 로고    scopus 로고
    • S-state dependence of the miss probability in photosystem ii
    • de Wijn, R., and van Gorkom, H. J. (2002) S-state dependence of the miss probability in Photosystem II. Photosynth. Res. 72, 217-222.
    • (2002) Photosynth. Res , vol.72 , pp. 217-222
    • De Wijn, R.1    Van Gorkom, H.J.2
  • 25
    • 84859753093 scopus 로고    scopus 로고
    • Misses during water oxidation in photosystem ii are s state-dependent
    • Han, G., Mamedov, F., and Styring, S. (2012) Misses during water oxidation in photosystem II are S state-dependent. J. Biol. Chem. 287, 13422-13429.
    • (2012) J. Biol. Chem , vol.287 , pp. 13422-13429
    • Han, G.1    Mamedov, F.2    Styring, S.3
  • 26
    • 0037085023 scopus 로고    scopus 로고
    • The rate of chargerecombination in photosystem ii
    • de Wijn, R., and van Gorkom, H. J. (2002) The rate of chargerecombination in Photosystem II. Biochim. Biophys. Acta 1553, 302-308.
    • (2002) Biochim. Biophys. Acta , vol.1553 , pp. 302-308
    • De Wijn, R.1    Van Gorkom, H.J.2
  • 27
    • 0032485936 scopus 로고    scopus 로고
    • On the origin of the '35-μs kinetics' of p680+• reduction in photosystem ii with an intact water oxidising complex
    • Christen, G., Reifarth, F., and Renger, G. (1998) On the origin of the '35-μs kinetics' of P680+• reduction in photosystem II with an intact water oxidising complex. FEBS Lett. 429, 49-52.
    • (1998) FEBS Lett , vol.429 , pp. 49-52
    • Christen, G.1    Reifarth, F.2    Renger, G.3
  • 28
    • 33847453635 scopus 로고
    • Kinetics of manganese redox transitions in the oxygen-evolving apparatus of photosynthesis
    • Dekker, J. P., Plijter, J. J., Ouwehand, L., and van Gorkom, H. J. (1984) Kinetics of manganese redox transitions in the oxygen-evolving apparatus of photosynthesis. Biochim. Biophys. Acta 767, 176-179.
    • (1984) Biochim. Biophys. Acta , vol.767 , pp. 176-179
    • Dekker, J.P.1    Plijter, J.J.2    Ouwehand, L.3    Van Gorkom, H.J.4
  • 29
    • 0342676543 scopus 로고
    • Studies on the nature of the water-oxidizing enzyme. Iii. Spectral characterization of the intermediary redox states in the water-oxidizing enzyme system y
    • Renger, G., and Weiss, W. (1986) Studies on the nature of the water-oxidizing enzyme. III. Spectral characterization of the intermediary redox states in the water-oxidizing enzyme system Y. Biochim. Biophys. Acta 850, 184-196.
    • (1986) Biochim. Biophys. Acta , vol.850 , pp. 184-196
    • Renger, G.1    Weiss, W.2
  • 30
    • 0028344645 scopus 로고
    • Kinetics of electron-Transfer and electrochromic change during the redox transitions of the photosynthetic oxygen-evolving complex
    • Rappaport, F., Blanchard-Desce, M., and Lavergne, J. (1994) Kinetics of electron-Transfer and electrochromic change during the redox transitions of the photosynthetic oxygen-evolving complex. Biochim. Biophys. Acta 1184, 178-192.
    • (1994) Biochim. Biophys. Acta , vol.1184 , pp. 178-192
    • Rappaport, F.1    Blanchard-Desce, M.2    Lavergne, J.3
  • 31
    • 0026685787 scopus 로고
    • X-ray detection of the period-four cycling of the manganese cluster in photosynthetic water oxidizing enzyme
    • Ono, T., Noguchi, T., Inoue, Y., Kusunoki, M., Matsushita, T., and Oyanagi, H. (1992) X-ray detection of the period-four cycling of the manganese cluster in photosynthetic water oxidizing enzyme. Science 258, 1335-1337.
    • (1992) Science , vol.258 , pp. 1335-1337
    • Ono, T.1    Noguchi, T.2    Inoue, Y.3    Kusunoki, M.4    Matsushita, T.5    Oyanagi, H.6
  • 33
    • 0017277681 scopus 로고
    • Reaction kinetics for positive charge accumulation on water side of chloroplast photosystem ii
    • Babcock, G. T., Blankenship, R. E., and Sauer, K. (1976) Reaction kinetics for positive charge accumulation on water side of chloroplast photosystem II. FEBS Lett. 61, 286-289.
    • (1976) FEBS Lett , vol.61 , pp. 286-289
    • Babcock, G.T.1    Blankenship, R.E.2    Sauer, K.3
  • 36
    • 0035852859 scopus 로고    scopus 로고
    • S-state dependent fourier transform infrared difference spectra for the photosystem ii oxygen evolving complex
    • Hillier, W., and Babcock, G. T. (2001) S-state dependent Fourier transform infrared difference spectra for the photosystem II oxygen evolving complex. Biochemistry 40, 1503-1509.
    • (2001) Biochemistry , vol.40 , pp. 1503-1509
    • Hillier, W.1    Babcock, G.T.2
  • 37
    • 0035852854 scopus 로고    scopus 로고
    • Flash-induced fourier transform infrared detection of the structural changes during the sstate cycle of the oxygen-evolving complex in photosystem ii
    • Noguchi, T., and Sugiura, M. (2001) Flash-induced Fourier transform infrared detection of the structural changes during the Sstate cycle of the oxygen-evolving complex in photosystem II. Biochemistry 40, 1497-1502.
    • (2001) Biochemistry , vol.40 , pp. 1497-1502
    • Noguchi, T.1    Sugiura, M.2
  • 38
    • 13444278779 scopus 로고    scopus 로고
    • No evidence from ftir difference spectroscopy that aspartate-170 of the d1 polypeptide ligates a manganese ion that undergoes oxidation during the s0 to s1, s1 to s2, or s2 to s3 transitions in photosystem ii
    • Debus, R. J., Strickler, M. A., Walker, L. M., and Hillier, W. (2005) No evidence from FTIR difference spectroscopy that aspartate-170 of the D1 polypeptide ligates a manganese ion that undergoes oxidation during the S0 to S1, S1 to S2, or S2 to S3 transitions in photosystem II. Biochemistry 44, 1367-1374.
    • (2005) Biochemistry , vol.44 , pp. 1367-1374
    • Debus, R.J.1    Strickler, M.A.2    Walker, L.M.3    Hillier, W.4
  • 39
    • 28944448293 scopus 로고    scopus 로고
    • Ftir detection of structural changes in a histidine ligand during s-state cycling of photosynthetic oxygen-evolving complex
    • Kimura, Y., Mizusawa, N., Ishii, A., and Ono, T. (2005) FTIR detection of structural changes in a histidine ligand during S-state cycling of photosynthetic oxygen-evolving complex. Biochemistry 44, 16072-16078.
    • (2005) Biochemistry , vol.44 , pp. 16072-16078
    • Kimura, Y.1    Mizusawa, N.2    Ishii, A.3    Ono, T.4
  • 40
    • 84859899002 scopus 로고    scopus 로고
    • Time-resolved infrared detection of the proton and protein dynamics during photosynthetic oxygen evolution
    • Noguchi, T., Suzuki, H., Tsuno, M., Sugiura, M., and Kato, C. (2012) Time-resolved infrared detection of the proton and protein dynamics during photosynthetic oxygen evolution. Biochemistry 51, 3205-3214.
    • (2012) Biochemistry , vol.51 , pp. 3205-3214
    • Noguchi, T.1    Suzuki, H.2    Tsuno, M.3    Sugiura, M.4    Kato, C.5
  • 41
    • 0026074911 scopus 로고
    • Improved uv-visible spectra of the stransitions in the photosynthetic oxygen-evolving system
    • Lavergne, J. (1991) Improved UV-visible spectra of the Stransitions in the photosynthetic oxygen-evolving system. Biochim. Biophys. Acta 1060, 175-188.
    • (1991) Biochim. Biophys. Acta , vol.1060 , pp. 175-188
    • Lavergne, J.1
  • 42
    • 67650517036 scopus 로고    scopus 로고
    • Monitoring proton release during photosynthetic water oxidation in photosystem ii by means of isotope-edited infrared spectroscopy
    • Suzuki, H., Sugiura, M., and Noguchi, T. (2009) Monitoring proton release during photosynthetic water oxidation in photosystem II by means of isotope-edited infrared spectroscopy. J. Am. Chem. Soc. 131, 7849-7857.
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 7849-7857
    • Suzuki, H.1    Sugiura, M.2    Noguchi, T.3
  • 43
    • 0000053790 scopus 로고
    • The influence of anions on oxygen evolution by isolated spinach chloroplasts
    • Sinclair, J. (1984) The influence of anions on oxygen evolution by isolated spinach chloroplasts. Biochim. Biophys. Acta 764, 247-252.
    • (1984) Biochim. Biophys. Acta , vol.764 , pp. 247-252
    • Sinclair, J.1
  • 44
    • 0033596856 scopus 로고    scopus 로고
    • 2-evolving complex of photosystem ii slow the kinetics of the terminal step in water oxidation and destabilize the s2 and s3 states
    • 2-evolving complex of photosystem II slow the kinetics of the terminal step in water oxidation and destabilize the S2 and S3 states. Biochemistry 38, 3719-3725.
    • (1999) Biochemistry , vol.38 , pp. 3719-3725
    • Wincencjusz, H.1    Yocum, C.F.2    Van Gorkom, H.J.3
  • 45
    • 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., and 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, 1219-1231.
    • (1999) Plant Cell Physiol , vol.40 , pp. 1219-1231
    • Sugiura, M.1    Inoue, Y.2
  • 47
    • 0000075484 scopus 로고
    • A highly resolved, oxygen-evolving photosystem ii preparation from spinach thylakoid membranes. Epr and electron-Transport properties
    • Berthold, D. A., Babcock, G. T., and Yocum, C. F. (1981) A highly resolved, oxygen-evolving photosystem II preparation from spinach thylakoid membranes. EPR and electron-Transport properties. FEBS Lett. 134, 231-234.
    • (1981) FEBS Lett , vol.134 , pp. 231-234
    • Berthold, D.A.1    Babcock, G.T.2    Yocum, C.F.3
  • 48
    • 0001544886 scopus 로고
    • Effects of removal and reconstitution of the extrinsic 33, 24 and 16 kda proteins on flash oxygen yield in photosystem ii particles
    • Ono, T., and Inoue, Y. (1986) Effects of removal and reconstitution of the extrinsic 33, 24 and 16 kDa proteins on flash oxygen yield in photosystem II particles. Biochim. Biophys. Acta 850, 380-389.
    • (1986) Biochim. Biophys. Acta , vol.850 , pp. 380-389
    • Ono, T.1    Inoue, Y.2
  • 49
    • 33947539623 scopus 로고    scopus 로고
    • Light-induced ftir difference spectroscopy as a powerful tool toward understanding the molecular mechanism of photosynthetic oxygen evolution
    • Noguchi, T. (2007) Light-induced FTIR difference spectroscopy as a powerful tool toward understanding the molecular mechanism of photosynthetic oxygen evolution. Photosynth. Res. 91, 59-69.
    • (2007) Photosynth. Res , vol.91 , pp. 59-69
    • Noguchi, T.1
  • 50
    • 0001221192 scopus 로고
    • Nature of bonding in metal cyanide complexes as related to intensity and frequency of infrared absorption spectra
    • Jones, L. H. (1963) Nature of bonding in metal cyanide complexes as related to intensity and frequency of infrared absorption spectra. Inorg. Chem. 2, 777-780.
    • (1963) Inorg. Chem , vol.2 , pp. 777-780
    • Jones, L.H.1
  • 51
    • 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, 189-200.
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 189-200
    • Noguchi, T.1    Ono, T.2    Inoue, Y.3
  • 52
    • 0038183812 scopus 로고    scopus 로고
    • Analysis of flash-induced ftir difference spectra of the s-state cycle in the photosynthetic water-oxidizing complex by uniform 15n and 13c isotope labeling
    • Noguchi, T., and Sugiura, M. (2003) Analysis of flash-induced FTIR difference spectra of the S-state cycle in the photosynthetic water-oxidizing complex by uniform 15N and 13C isotope labeling. Biochemistry 42, 6035-6042.
    • (2003) Biochemistry , vol.42 , pp. 6035-6042
    • Noguchi, T.1    Sugiura, M.2
  • 53
    • 0242569191 scopus 로고    scopus 로고
    • Changes of low-frequency vibrational modes induced by universal 15n-And 13c-isotope labeling in s2/s1 ftir difference spectrum of oxygen-evolving complex
    • Kimura, Y., Mizusawa, N., Ishii, A., Yamanari, T., and Ono, T. (2003) Changes of low-frequency vibrational modes induced by universal 15N-And 13C-isotope labeling in S2/S1 FTIR difference spectrum of oxygen-evolving complex. Biochemistry 42, 13170-13177.
    • (2003) Biochemistry , vol.42 , pp. 13170-13177
    • Kimura, Y.1    Mizusawa, N.2    Ishii, A.3    Yamanari, T.4    Ono, T.5
  • 54
    • 1542638640 scopus 로고    scopus 로고
    • Evidence that the c-Terminus of the d1 polypeptide of photosystem ii is ligated to the manganese ion that undergoes oxidation during the s1 to s2 transition: An isotope-edited ftir study
    • Chu, H.-A., Hillier, W., and Debus, R. J. (2004) Evidence that the C-Terminus of the D1 polypeptide of photosystem II is ligated to the manganese ion that undergoes oxidation during the S1 to S2 transition: An isotope-edited FTIR study. Biochemistry 43, 3152-3166.
    • (2004) Biochemistry , vol.43 , pp. 3152-3166
    • Chu, H.-A.1    Hillier, W.2    Debus, R.J.3
  • 55
    • 38049029119 scopus 로고    scopus 로고
    • Protein ligation of the photosynthetic oxygen-evolving center
    • Debus, R. J. (2008) Protein ligation of the photosynthetic oxygen-evolving center. Coord. Chem. Rev. 252, 244-258.
    • (2008) Coord. Chem. Rev , vol.252 , pp. 244-258
    • Debus, R.J.1
  • 56
    • 38049004891 scopus 로고    scopus 로고
    • Fourier transform infrared analysis of the photosynthetic oxygen-evolving center
    • Noguchi, T. (2008) Fourier transform infrared analysis of the photosynthetic oxygen-evolving center. Coord. Chem. Rev. 252, 336-346.
    • (2008) Coord. Chem. Rev , vol.252 , pp. 336-346
    • Noguchi, T.1
  • 57
    • 0033520084 scopus 로고    scopus 로고
    • Structure of a histidine ligand in the photosynthetic oxygen-evolving complex as studied by light-induced fourier transform infrared difference spectroscopy
    • Noguchi, T., Inoue, Y., and Tang, X.-S. (1999) Structure of a histidine ligand in the photosynthetic oxygen-evolving complex as studied by light-induced Fourier transform infrared difference spectroscopy. Biochemistry 38, 10187-10195.
    • (1999) Biochemistry , vol.38 , pp. 10187-10195
    • Noguchi, T.1    Inoue, Y.2    Tang, X.-S.3
  • 58
    • 79952772499 scopus 로고    scopus 로고
    • Structural coupling of an arginine side chain with the oxygen evolving mn4ca cluster in photosynstem ii as revealed by isotope-edited fourier transform infrared spectroscopy
    • Shimada, Y., Suzuki, H., Tsuchiya, T., Mimuro, M., and Noguchi, T. (2011) Structural coupling of an arginine side chain with the oxygen evolving Mn4Ca cluster in photosynstem II as revealed by isotope-edited Fourier transform infrared spectroscopy. J. Am. Chem. Soc. 133, 3808-3811.
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 3808-3811
    • Shimada, Y.1    Suzuki, H.2    Tsuchiya, T.3    Mimuro, M.4    Noguchi, T.5
  • 59
    • 0037207105 scopus 로고    scopus 로고
    • Ftir detection of water reactions during the flash-induced s-state cycle of the photosynthetic water-oxidizing complex
    • Noguchi, T., and Sugiura, M. (2002) FTIR detection of water reactions during the flash-induced S-state cycle of the photosynthetic water-oxidizing complex. Biochemistry 41, 15706-15712.
    • (2002) Biochemistry , vol.41 , pp. 15706-15712
    • Noguchi, T.1    Sugiura, M.2
  • 60
    • 0034727679 scopus 로고    scopus 로고
    • Identification of a mn-o-mn cluster vibrational mode of the oxygenevolving complex in photosystem ii by low-frequency ftir spectroscopy
    • Chu, H.-A., Sackett, H., and Babcock, G. T. (2000) Identification of a Mn-O-Mn cluster vibrational mode of the oxygenevolving complex in photosystem II by low-frequency FTIR spectroscopy. Biochemistry 39, 14371-14376.
    • (2000) Biochemistry , vol.39 , pp. 14371-14376
    • Chu, H.-A.1    Sackett, H.2    Babcock, G.T.3
  • 61
    • 19644386903 scopus 로고    scopus 로고
    • Watersensitive low-frequency vibrations of reaction intermediates during sstate cycling in photosynthetic water oxidation
    • Kimura, Y., Ishii, A., Yamanari, T., and Ono, T. (2005) Watersensitive low-frequency vibrations of reaction intermediates during Sstate cycling in photosynthetic water oxidation. Biochemistry 44, 7613-7622.
    • (2005) Biochemistry , vol.44 , pp. 7613-7622
    • Kimura, Y.1    Ishii, A.2    Yamanari, T.3    Ono, T.4
  • 62
    • 0037133143 scopus 로고    scopus 로고
    • Flash-induced ftir difference spectra of the water oxidizing complex in moderately hydrated photosystem ii core films: Effect of hydration extent on sstate transitions
    • Noguchi, T., and Sugiura, M. (2002) Flash-induced FTIR difference spectra of the water oxidizing complex in moderately hydrated photosystem II core films: Effect of hydration extent on Sstate transitions. Biochemistry 41, 2322-2330.
    • (2002) Biochemistry , vol.41 , pp. 2322-2330
    • Noguchi, T.1    Sugiura, M.2
  • 63
    • 0000948871 scopus 로고
    • Q400, the non-heme iron of the photosystem ii iron-quinone complex. A spectroscopic probe of quinone and inhibitor binding to the reaction center
    • Diner, B. A., and Petrouleas, V. (1987) Q400, the non-heme iron of the Photosystem II iron-quinone complex. A spectroscopic probe of quinone and inhibitor binding to the reaction center. Biochim. Biophys. Acta 895, 107-125.
    • (1987) Biochim. Biophys. Acta , vol.895 , pp. 107-125
    • Diner, B.A.1    Petrouleas, V.2
  • 64
    • 0027249446 scopus 로고
    • Structurefunction relations in photosystem ii. Effects of temperature andchaotropic agents on the period four oscillation of flash-induced oxygen evolution
    • Messinger, J., Schröder, W. P., and Renger, G. (1993) Structurefunction relations in photosystem II. Effects of temperature andchaotropic agents on the period four oscillation of flash-induced oxygen evolution. Biochemistry 32, 7658-7668.
    • (1993) Biochemistry , vol.32 , pp. 7658-7668
    • Messinger, J.1    Schröder, W.P.2    Renger, G.3
  • 65
    • 0026096798 scopus 로고
    • Ph-dependent charge equilibria between tyrosine-d and the s states in photosystem ii. Estimation of relative midpoint redox potentials
    • Vass, I., and Styring, S. (1991) pH-dependent charge equilibria between tyrosine-D and the S states in photosystem II. Estimation of relative midpoint redox potentials. Biochemistry 30, 830-839.
    • (1991) Biochemistry , vol.30 , pp. 830-839
    • Vass, I.1    Styring, S.2
  • 66
    • 1942440387 scopus 로고    scopus 로고
    • The stable tyrosyl radical in photosystem ii: Why d? Biochim
    • Rutherford, A. W., Boussac, A., and Faller, P. (2004) The stable tyrosyl radical in Photosystem II: Why D? Biochim. Biophys. Acta 1655, 222-230.
    • (2004) Biophys. Acta , vol.1655 , pp. 222-230
    • Rutherford, A.W.1    Boussac, A.2    Faller, P.3
  • 67
    • 0037207119 scopus 로고    scopus 로고
    • Replacement of tyrosine d with phenylalanine affects the normal proton transfer pathways for the reduction of p680+ in oxygen-evolving photosystem ii particles from chlamydomonas
    • Jeans, C., Schilstra, M. J., Ray, N., Husain, S., Minagawa, J., Nugent, J. H. A., and Klug, D. R. (2002) Replacement of tyrosine D with phenylalanine affects the normal proton transfer pathways for the reduction of P680+ in oxygen-evolving photosystem II particles from Chlamydomonas. Biochemistry 41, 15754-15761.
    • (2002) Biochemistry , vol.41 , pp. 15754-15761
    • Jeans, C.1    Schilstra, M.J.2    Ray, N.3    Husain, S.4    Minagawa, J.5    Nugent, J.H.A.6    Klug, D.R.7
  • 69
    • 32344435642 scopus 로고    scopus 로고
    • Side-path electron donors: Cytochrome b559, chlorophyll z and-carotene
    • (Wydrzynski, T., and Satoh, K., Eds.), Springer, Dordrecht, The Netherlands
    • Faller, P., Fufezan, C., and Rutherford, A. W. (2005) Side-path electron donors: Cytochrome b559, chlorophyll Z and-carotene. In Photosystem II: The Light-Driven Water:Plastoquinone Oxidoreductase (Wydrzynski, T., and Satoh, K., Eds.) pp 347-365, Springer, Dordrecht, The Netherlands.
    • (2005) Photosystem II: The Light-Driven Water:Plastoquinone Oxidoreductase , pp. 347-365
    • Faller, P.1    Fufezan, C.2    Rutherford, A.W.3
  • 70
    • 0029098147 scopus 로고
    • Molecular interactions of the redox-Active accessory chlorophyll on the electron-donor side of photosystem ii as studied by fourier transform infrared spectroscopy
    • Noguchi, T., and Inoue, Y. (1995) Molecular interactions of the redox-Active accessory chlorophyll on the electron-donor side of photosystem II as studied by Fourier transform infrared spectroscopy. FEBS Lett. 370, 241-244.
    • (1995) FEBS Lett , vol.370 , pp. 241-244
    • Noguchi, T.1    Inoue, Y.2
  • 71
    • 0028046023 scopus 로고
    • Fourier transform infrared spectrum of the radical cation of-carotene photoinduced in photosystem ii
    • Noguchi, T., Mitsuka, T., and Inoue, Y. (1994) Fourier transform infrared spectrum of the radical cation of-carotene photoinduced in photosystem II. FEBS Lett. 356, 179-182.
    • (1994) FEBS Lett , vol.356 , pp. 179-182
    • Noguchi, T.1    Mitsuka, T.2    Inoue, Y.3
  • 72
    • 0000948871 scopus 로고
    • Q400, the non-heme iron of the photosystem ii iron-quinone complex. A spectroscopic probe of quinone and inhibitor binding to the reaction center
    • Diner, B. A., and Petrouleas, V. (1987) Q400, the non-heme iron of the Photosystem II iron-quinone complex. A spectroscopic probe of quinone and inhibitor binding to the reaction center. Biochim. Biophys. Acta 895, 107-125.
    • (1987) Biochim. Biophys. Acta , vol.895 , pp. 107-125
    • Diner, B.A.1    Petrouleas, V.2
  • 73
    • 0035797872 scopus 로고    scopus 로고
    • Kinetics of electron transfer from qa to qb in photosystem ii
    • de Wijn, R., and van Gorkom, H. J. (2001) Kinetics of electron transfer from QA to QB in photosystem II. Biochemistry 40, 11912-11922.
    • (2001) Biochemistry , vol.40 , pp. 11912-11922
    • De Wijn, R.1    Van Gorkom, H.J.2
  • 74
    • 0035873926 scopus 로고    scopus 로고
    • Secondary stabilization reactions and proton-coupled electron transport in photosystem ii investigated by electroluminescence and fluorescence spectroscopy
    • de Wijn, R., Schrama, T., and van Gorkom, H. J. (2001) Secondary stabilization reactions and proton-coupled electron transport in photosystem II investigated by electroluminescence and fluorescence spectroscopy. Biochemistry 40, 5821-5834.
    • (2001) Biochemistry , vol.40 , pp. 5821-5834
    • De Wijn, R.1    Schrama, T.2    Van Gorkom, H.J.3
  • 75
    • 33751005603 scopus 로고    scopus 로고
    • 2+ exchange in the s-state cycle of photosynthetic oxygen evolution as studied by flash-induced ftir difference spectroscopy
    • 2+ exchange in the S-state cycle of photosynthetic oxygen evolution as studied by flash-induced FTIR difference spectroscopy. Biochemistry 45, 13454-13464.
    • (2006) Biochemistry , vol.45 , pp. 13454-13464
    • Suzuki, H.1    Taguchi, Y.2    Sugiura, M.3    Boussac, A.4    Noguchi, T.5


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