메뉴 건너뛰기




Volumn 50, Issue 1, 2011, Pages 63-81

Participation of glutamate-354 of the CP43 polypeptide in the ligation of manganese and the binding of substrate water in photosystem II

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE GROUPS; BRIDGING LIGANDS; C-TERMINUS; COORDINATION MODES; CYANOBACTERIUM SYNECHOCYSTIS; EPR SIGNALS; EXAFS; FTIR; HIGHER FREQUENCIES; LONG LIFETIME; OXYGEN RELEASE; PHOTOSYSTEM II; POSITIVE CHARGES; PSII CORE COMPLEX; REACTION CENTER; S STATE; SPECTROSCOPIC METHOD; SPIN STATE; STEADY STATE RATES; STRETCHING MODES; STRETCHING REGION; STRUCTURAL MODELS; THYLAKOID MEMBRANES; WATER EXCHANGE; WATER MOLECULE; WILD TYPES;

EID: 78650920475     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1015937     Document Type: Article
Times cited : (55)

References (125)
  • 1
    • 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
  • 2
    • 30744445692 scopus 로고    scopus 로고
    • Towards Complete Cofactor Arrangement in the 3.0 Å Resolution Structure of Photosystem II
    • Loll, B., Kern, J., Saenger, W., Zouni, A., and Biesiadka, J. (2005) Towards Complete Cofactor Arrangement in the 3.0 Å Resolution Structure of Photosystem II Nature 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
  • 4
    • 42149109765 scopus 로고    scopus 로고
    • Crystal Structure of the Oxygen-Evolving Complex of Photosystem II
    • Barber, J. (2008) Crystal Structure of the Oxygen-Evolving Complex of Photosystem II Inorg. Chem. 47, 1700-1710
    • (2008) Inorg. Chem. , vol.47 , pp. 1700-1710
    • Barber, J.1
  • 5
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial Photosystem II at 2.9-Å 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-Å 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
  • 7
    • 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
  • 8
    • 77955239344 scopus 로고    scopus 로고
    • Current Models and Mechanism of Water Splitting
    • (Fromme P., Ed.), Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany
    • McCarrick, R. M. and Britt, R. D. (2008) Current Models and Mechanism of Water Splitting, in Photosynthetic Protein Complexes (Fromme, P., Ed.) pp 107 - 136, Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany.
    • (2008) Photosynthetic Protein Complexes , pp. 107-136
    • McCarrick, R.M.1    Britt, R.D.2
  • 9
    • 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, 259-272
    • (2008) Coord. Chem. Rev. , vol.252 , pp. 259-272
    • Rappaport, F.1    Diner, B.A.2
  • 10
    • 57849146011 scopus 로고    scopus 로고
    • Photosystem II: The Machinery of Photosynthetic Water Splitting
    • Renger, G. and Renger, T. (2008) Photosystem II: The Machinery of Photosynthetic Water Splitting Photosynth. Res. 98, 53-80
    • (2008) Photosynth. Res. , vol.98 , pp. 53-80
    • Renger, G.1    Renger, T.2
  • 11
    • 42149154953 scopus 로고    scopus 로고
    • 4Ca Cluster from X-ray Spectroscopy
    • 4Ca Cluster from X-ray Spectroscopy Inorg. Chem. 47, 1711-1726
    • (2008) Inorg. Chem. , vol.47 , pp. 1711-1726
    • Yano, J.1    Yachandra, V.K.2
  • 13
    • 38049016877 scopus 로고    scopus 로고
    • The Manganese Complex of Photosystem II in its Reaction Cycle - Basic Framework and Possible Realization at the Atomic Level
    • Dau, H. and Haumann, M. (2008) The Manganese Complex of Photosystem II in its Reaction Cycle - Basic Framework and Possible Realization at the Atomic Level Coord. Chem. Rev. 252, 273-295
    • (2008) Coord. Chem. Rev. , vol.252 , pp. 273-295
    • Dau, H.1    Haumann, M.2
  • 14
    • 38049016880 scopus 로고    scopus 로고
    • X-ray Spectrsocopy of the Photosynthetic Oxygen-Evolving Complex
    • Sauer, K., Yano, J., and Yachandra, V. K. (2008) X-ray Spectrsocopy of the Photosynthetic Oxygen-Evolving Complex Coord. Chem. Rev. 252, 318-335
    • (2008) Coord. Chem. Rev. , vol.252 , pp. 318-335
    • Sauer, K.1    Yano, J.2    Yachandra, V.K.3
  • 16
    • 66649106614 scopus 로고    scopus 로고
    • Location of Chloride and its Possible Functions in Oxygen-Evolving Photosystem II Revealed by X-ray Crystallography
    • Kawakami, K., Umena, Y., Kamiya, N., and Shen, J.-R. (2009) Location of Chloride and its Possible Functions in Oxygen-Evolving Photosystem II Revealed by X-ray Crystallography Proc. Natl. Acad. Sci. U.S.A. 106, 8567-8572
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 8567-8572
    • Kawakami, K.1    Umena, Y.2    Kamiya, N.3    Shen, J.-R.4
  • 18
    • 33645219974 scopus 로고    scopus 로고
    • Rapid Loss of Structural Motifs in the Manganese Complex of Oxygenic Photosynthesis by X-ray Irradiation at 10-300 K
    • Grabolle, M., Haumann, M., Müller, C., Liebisch, P., and Dau, H. (2006) Rapid Loss of Structural Motifs in the Manganese Complex of Oxygenic Photosynthesis by X-ray Irradiation at 10-300 K J. Biol. Chem. 281, 4580-4588
    • (2006) J. Biol. Chem. , vol.281 , pp. 4580-4588
    • Grabolle, M.1    Haumann, M.2    Müller, C.3    Liebisch, P.4    Dau, H.5
  • 20
    • 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
  • 21
    • 34547794990 scopus 로고    scopus 로고
    • Time Resolved X-ray Spectroscopy Leads to an Extension of the Classical S-State Cycle Model of Photosynthetic Oxygen Evolution
    • Dau, H. and Haumann, M. (2007) Time Resolved X-ray Spectroscopy Leads to an Extension of the Classical S-State Cycle Model of Photosynthetic Oxygen Evolution Photosynth. Res. 92, 327-343
    • (2007) Photosynth. Res. , vol.92 , pp. 327-343
    • Dau, H.1    Haumann, M.2
  • 23
    • 0030042115 scopus 로고    scopus 로고
    • On the Functional Significance of Substrate Accessibility in the Photosynthetic Water Oxidation Mechanism
    • Wydrzynski, T., Hillier, W., and Messinger, J. (1996) On the Functional Significance of Substrate Accessibility in the Photosynthetic Water Oxidation Mechanism Physiol. Plant. 96, 342-350
    • (1996) Physiol. Plant. , vol.96 , pp. 342-350
    • Wydrzynski, T.1    Hillier, W.2    Messinger, J.3
  • 24
    • 0035846819 scopus 로고    scopus 로고
    • Does Functional Photosystem II Complex have an Oxygen Channel?
    • Anderson, J. M. (2001) Does Functional Photosystem II Complex have an Oxygen Channel? FEBS Lett. 488, 1-4
    • (2001) FEBS Lett. , vol.488 , pp. 1-4
    • Anderson, J.M.1
  • 25
    • 0036322691 scopus 로고    scopus 로고
    • The structure and function of CP47 and CP43 in Photosystem II
    • Bricker, T. M. and Frankel, L. K. (2002) The structure and function of CP47 and CP43 in Photosystem II Photosynth. Res. 72, 131-146
    • (2002) Photosynth. Res. , vol.72 , pp. 131-146
    • Bricker, T.M.1    Frankel, L.K.2
  • 26
    • 0033619712 scopus 로고    scopus 로고
    • Site-directed mutagenesis of glutamate residues in the large extrinsic loop of the photosystem II protein CP 43 affects oxygen-evolving activity and PS II assembly
    • Rosenberg, C., Christian, J., Bricker, T. M., and Putnam-Evans, C. (1999) Site-Directed Mutagenesis of Glutamate Residues in the Large Extrinsic Loop of the Photosystem II Protein CP 43 Affects Oxygen-Evolving Activity and PSII Assembly Biochemistry 38, 15994-16000 (Pubitemid 129520494)
    • (1999) Biochemistry , vol.38 , Issue.48 , pp. 15994-16000
    • Rosenberg, C.1    Christian, J.2    Bricker, T.M.3    Putnam-Evans, C.4
  • 28
    • 67650033429 scopus 로고    scopus 로고
    • Effect of a Single-Amino Acid Substitution of the 43 kDa Chlorophyll Protein on the Oxygen-Evolving Reaction of the Cyanobacterium Synechocystis sp. PCC 6803: Analysis of the Glu354Gln Mutation
    • Shimada, Y., Suzuki, H., Tsuchiya, T., Tomo, T., Noguchi, T., and Mimuro, M. (2009) Effect of a Single-Amino Acid Substitution of the 43 kDa Chlorophyll Protein on the Oxygen-Evolving Reaction of the Cyanobacterium Synechocystis sp. PCC 6803: Analysis of the Glu354Gln Mutation Biochemistry 48, 6095-6103
    • (2009) Biochemistry , vol.48 , pp. 6095-6103
    • Shimada, Y.1    Suzuki, H.2    Tsuchiya, T.3    Tomo, T.4    Noguchi, T.5    Mimuro, M.6
  • 30
    • 0035957275 scopus 로고    scopus 로고
    • Does Histidine 332 of the D1 Polypeptide Ligate the Manganese Cluster in Photosystem II? An Electron Spin Echo Envelope Modulation Study
    • Debus, R. J., Campbell, K. A., Gregor, W., Li, Z.-L., Burnap, R. L., and Britt, R. D. (2001) Does Histidine 332 of the D1 Polypeptide Ligate the Manganese Cluster in Photosystem II? An Electron Spin Echo Envelope Modulation Study Biochemistry 40, 3690-3699
    • (2001) Biochemistry , vol.40 , pp. 3690-3699
    • Debus, R.J.1    Campbell, K.A.2    Gregor, W.3    Li, Z.-L.4    Burnap, R.L.5    Britt, R.D.6
  • 32
    • 2942623788 scopus 로고    scopus 로고
    • Mid- to Low-Frequency Fourier Transform Infrared Spectra of S-State Cycle for Photosynthetic Water Oxidation in Synechocystis sp. PCC 6803
    • Yamanari, T., Kimura, Y., Mizusawa, N., Ishii, A., and Ono, T.-A. (2004) Mid- to Low-Frequency Fourier Transform Infrared Spectra of S-State Cycle for Photosynthetic Water Oxidation in Synechocystis sp. PCC 6803 Biochemistry 43, 7479-7490
    • (2004) Biochemistry , vol.43 , pp. 7479-7490
    • Yamanari, T.1    Kimura, Y.2    Mizusawa, N.3    Ishii, A.4    Ono, T.-A.5
  • 34
    • 20544470177 scopus 로고    scopus 로고
    • Evidence from Biosynthetically Incorporated Strontium and FTIR Difference Spectroscopy That the C-Terminus of the D1 Polypeptide of Photosystem II Does Not Ligate Calcium
    • Strickler, M. A., Walker, L. M., Hillier, W., and Debus, R. J. (2005) Evidence from Biosynthetically Incorporated Strontium and FTIR Difference Spectroscopy That the C-Terminus of the D1 Polypeptide of Photosystem II Does Not Ligate Calcium Biochemistry 44, 8571-8577
    • (2005) Biochemistry , vol.44 , pp. 8571-8577
    • Strickler, M.A.1    Walker, L.M.2    Hillier, W.3    Debus, R.J.4
  • 35
    • 0028303152 scopus 로고
    • Site-Directed Photosystem II Mutants with Perturbed Oxygen Evolving Properties: 1. Instability or Inefficient Assembly of the Manganese Cluster in Vivo
    • Chu, H.-A., Nguyen, A. P., and Debus, R. J. (1994) Site-Directed Photosystem II Mutants with Perturbed Oxygen Evolving Properties: 1. Instability or Inefficient Assembly of the Manganese Cluster in Vivo Biochemistry 33, 6137-6149
    • (1994) Biochemistry , vol.33 , pp. 6137-6149
    • Chu, H.-A.1    Nguyen, A.P.2    Debus, R.J.3
  • 36
    • 0028209372 scopus 로고
    • Biochemical and Spectroscopic Characterization of a New Oxygen-Evolving Photosystem II Core Complex from the Cyanobacterium Synechocystis sp. PCC 6803
    • Tang, X.-S. and Diner, B. A. (1994) Biochemical and Spectroscopic Characterization of a New Oxygen-Evolving Photosystem II Core Complex from the Cyanobacterium Synechocystis sp. PCC 6803 Biochemistry 33, 4594-4603
    • (1994) Biochemistry , vol.33 , pp. 4594-4603
    • Tang, X.-S.1    Diner, B.A.2
  • 37
  • 39
    • 0017071711 scopus 로고
    • Matrix Analysis of the Oxygen Evolving System of Photosynthesis
    • Lavorel, J. (1976) Matrix Analysis of the Oxygen Evolving System of Photosynthesis J. Theor. Biol. 57, 171-185
    • (1976) J. Theor. Biol. , vol.57 , pp. 171-185
    • Lavorel, J.1
  • 40
    • 0030028093 scopus 로고    scopus 로고
    • Improved 5-step Modeling of the Photosystem II S-state Mechanism in Cyanobacteria
    • Meunier, P. C., Burnap, R. L., and Sherman, L. A. (1996) Improved 5-step Modeling of the Photosystem II S-state Mechanism in Cyanobacteria Photosynth. Res. 47, 61-76
    • (1996) Photosynth. Res. , vol.47 , pp. 61-76
    • Meunier, P.C.1    Burnap, R.L.2    Sherman, L.A.3
  • 41
    • 0025012006 scopus 로고
    • Oxygen Release Time in Leaf Discs and Thylakoids of Peas and Photosystem II Membrane Fragments of Spinach
    • Jursinic, P. A. and Dennenberg, R. J. (1990) Oxygen Release Time in Leaf Discs and Thylakoids of Peas and Photosystem II Membrane Fragments of Spinach Biochim. Biophys. Acta 1020, 195-206
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 195-206
    • Jursinic, P.A.1    Dennenberg, R.J.2
  • 42
    • 0041317461 scopus 로고    scopus 로고
    • Does Aspartate 170 of the D1 Polypeptide Ligate the Manganese Cluster in Photosystem II? An EPR and ESEEM Study
    • Debus, R. J., Aznar, C., Campbell, K. A., Gregor, W., Diner, B. A., and Britt, R. D. (2003) Does Aspartate 170 of the D1 Polypeptide Ligate the Manganese Cluster in Photosystem II? An EPR and ESEEM Study Biochemistry 42, 10600-10608
    • (2003) Biochemistry , vol.42 , pp. 10600-10608
    • Debus, R.J.1    Aznar, C.2    Campbell, K.A.3    Gregor, W.4    Diner, B.A.5    Britt, R.D.6
  • 46
    • 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 S-state 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 S-State Transitions Biochemistry 41, 2322-2330
    • (2002) Biochemistry , vol.41 , pp. 2322-2330
    • Noguchi, T.1    Sugiura, M.2
  • 47
    • 77955262868 scopus 로고    scopus 로고
    • 4Ca Cluster of PhotosystemII Involving D1-Glu65, D2-Glu312, and D1-Glu329
    • 4Ca Cluster of PhotosystemII Involving D1-Glu65, D2-Glu312, and D1-Glu329 Biochemistry 49, 6655-6669
    • (2010) Biochemistry , vol.49 , pp. 6655-6669
    • Service, R.J.1    Hillier, W.2    Debus, R.J.3
  • 49
    • 38949105199 scopus 로고    scopus 로고
    • Investigation of Substrate Water Interactions at the High-Affinity Mn Site in the Photosystem II Oxygen-Evolving Complex
    • Singh, S., Debus, R. J., Wydrzynski, T., and Hillier, W. (2008) Investigation of Substrate Water Interactions at the High-Affinity Mn Site in the Photosystem II Oxygen-Evolving Complex Philos. Trans. R. Soc. London, Ser. B 363, 1229-1235
    • (2008) Philos. Trans. R. Soc. London, Ser. B , vol.363 , pp. 1229-1235
    • Singh, S.1    Debus, R.J.2    Wydrzynski, T.3    Hillier, W.4
  • 50
    • 8144228771 scopus 로고    scopus 로고
    • Substrate Water Interactions within the Photosystem II Oxygen Evolving Complex
    • Hillier, W. and Wydrzynski, T. (2004) Substrate Water Interactions within the Photosystem II Oxygen Evolving Complex Phys. Chem. Chem. Phys. 6, 4882-4889
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 4882-4889
    • Hillier, W.1    Wydrzynski, T.2
  • 52
    • 0032527668 scopus 로고    scopus 로고
    • 55Mn Pulsed ENDOR Demonstrates That the Photosystem II "split" EPR Signal Arises from a Magnetically-Coupled Mangano-Tyrosyl Complex
    • 55Mn Pulsed ENDOR Demonstrates That the Photosystem II "Split" EPR Signal Arises from a Magnetically-Coupled Mangano-Tyrosyl Complex J. Am. Chem. Soc. 120, 6840-6841
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6840-6841
    • Peloquin, J.M.1    Campbell, K.A.2    Britt, R.D.3
  • 53
    • 0000198823 scopus 로고    scopus 로고
    • Analysis of Dipolar and Exchange Interactions between Manganese and Tyrosine Z in the S2YZdot State of Acetate-Inhibited Photosystem II via EPR Spectral Simulations at X- and Q- bands
    • Lakshmi, K. V., Eaton, S. S., Eaton, G. R., Frank, H. A., and Brudvig, G. W. (1998) Analysis of Dipolar and Exchange Interactions between Manganese and Tyrosine Z in the S2YZdot State of Acetate-Inhibited Photosystem II via EPR Spectral Simulations at X- and Q- bands J. Phys. Chem. B 102, 8327-8335
    • (1998) J. Phys. Chem. B , vol.102 , pp. 8327-8335
    • Lakshmi, K.V.1    Eaton, S.S.2    Eaton, G.R.3    Frank, H.A.4    Brudvig, G.W.5
  • 54
    • 0001339888 scopus 로고    scopus 로고
    • Multifrequency High-Field EPR Study of the Interaction between the Tyrosyl Z Radical and the Manganese Cluster in Plant Photosystem II
    • Dorlet, P., Boussac, A., Rutherford, A. W., and Un, S. (1999) Multifrequency High-Field EPR Study of the Interaction between the Tyrosyl Z Radical and the Manganese Cluster in Plant Photosystem II J. Phys. Chem. B 103, 10945-10954
    • (1999) J. Phys. Chem. B , vol.103 , pp. 10945-10954
    • Dorlet, P.1    Boussac, A.2    Rutherford, A.W.3    Un, S.4
  • 55
    • 0035808669 scopus 로고    scopus 로고
    • Vibrational Spectroscopy of the Oxygen-Evolving Complex and of Manganese Model Compounds
    • Chu, H.-A., Hillier, W., Law, N. A., and Babcock, G. T. (2001) Vibrational Spectroscopy of the Oxygen-Evolving Complex and of Manganese Model Compounds Biochim. Biophys. Acta 1503, 69-82
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 69-82
    • Chu, H.-A.1    Hillier, W.2    Law, N.A.3    Babcock, G.T.4
  • 56
    • 32344439352 scopus 로고    scopus 로고
    • Molecular Analysis by Vibrational Spectroscopy
    • (Wydrzynski, T. and Satoh, Ki., Eds.), Springer, Dordrecht, The Netherlands
    • Noguchi, T. and Berthomieu, C. (2005) Molecular Analysis by Vibrational Spectroscopy, in Photosystem II: The Light-Driven Water:Plastoquinone Oxidoreductase (Wydrzynski, T. and Satoh, Ki., Eds.) pp 367 - 387, Springer, Dordrecht, The Netherlands.
    • (2005) Photosystem II: The Light-Driven Water:Plastoquinone Oxidoreductase , pp. 367-387
    • Noguchi, T.1    Berthomieu, C.2
  • 57
    • 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
  • 58
    • 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. 251, 336-346
    • (2008) Coord. Chem. Rev. , vol.251 , pp. 336-346
    • Noguchi, T.1
  • 59
    • 0030734034 scopus 로고    scopus 로고
    • Fourier Transform Infrared Difference Spectroscopy of Photosystem II Tyrosine D Using Site-Directed Mutagenesis and Specific Isotope Labeling
    • Hienerwadel, R., Boussac, A., Breton, J., Diner, B. A., and Berthomieu, C. (1997) Fourier Transform Infrared Difference Spectroscopy of Photosystem II Tyrosine D Using Site-Directed Mutagenesis and Specific Isotope Labeling Biochemistry 36, 14712-14723
    • (1997) Biochemistry , vol.36 , pp. 14712-14723
    • Hienerwadel, R.1    Boussac, A.2    Breton, J.3    Diner, B.A.4    Berthomieu, C.5
  • 60
    • 0030832914 scopus 로고    scopus 로고
    • Structural Coupling between the Oxygen-Evolving Mn Cluster and a Tyrosine Residue in Photosystem II As Revealed by Fourier Transform Infrared Spectroscopy
    • Noguchi, T., Inoue, Y., and Tang, X. S. (1997) Structural Coupling between the Oxygen-Evolving Mn Cluster and a Tyrosine Residue in Photosystem II As Revealed by Fourier Transform Infrared Spectroscopy Biochemistry 36, 14705-14711
    • (1997) Biochemistry , vol.36 , pp. 14705-14711
    • Noguchi, T.1    Inoue, Y.2    Tang, X.S.3
  • 61
    • 0032575361 scopus 로고    scopus 로고
    • Hydrogen-bonding of Redox-active Tyrosine Z of Photosystem II Probed by FTIR Difference Spectroscopy
    • Berthomieu, C., Hienerwadel, R., Boussac, A., Breton, J., and Diner, B. A. (1998) Hydrogen-Bonding of Redox-Active Tyrosine Z of Photosystem II Probed by FTIR Difference Spectroscopy Biochemistry 37, 10547-10554
    • (1998) Biochemistry , vol.37 , pp. 10547-10554
    • Berthomieu, C.1    Hienerwadel, R.2    Boussac, A.3    Breton, J.4    Diner, B.A.5
  • 62
    • 0035916217 scopus 로고    scopus 로고
    • D1-Asp170 Is Structurally Coupled to the Oxygen Evolving Complex in Photosystem II As Revealed by Light-Induced Fourier Transform Infrared Difference Spectroscopy
    • Chu, H.-A., Debus, R. J., and Babcock, G. T. (2001) D1-Asp170 Is Structurally Coupled to the Oxygen Evolving Complex in Photosystem II As Revealed by Light-Induced Fourier Transform Infrared Difference Spectroscopy Biochemistry 40, 2312-2316
    • (2001) Biochemistry , vol.40 , pp. 2312-2316
    • Chu, H.-A.1    Debus, R.J.2    Babcock, G.T.3
  • 63
    • 27844436623 scopus 로고    scopus 로고
    • Changes in Structural and Functional Properties of Oxygen-Evolving Complex Induced by Replacement of D1-Glutamate 189 with Glutamine in Photosystem II: Ligation of Glutamate 189 Carboxylate to the Manganese Cluster
    • Kimura, Y., Mizusawa, N., Ishii, A., Nakazawa, S., and Ono, T.-A. (2005) Changes in Structural and Functional Properties of Oxygen-Evolving Complex Induced by Replacement of D1-Glutamate 189 with Glutamine in Photosystem II: Ligation of Glutamate 189 Carboxylate to the Manganese Cluster J. Biol. Chem. 280, 37895-37900
    • (2005) J. Biol. Chem. , vol.280 , pp. 37895-37900
    • Kimura, Y.1    Mizusawa, N.2    Ishii, A.3    Nakazawa, S.4    Ono, T.-A.5
  • 64
    • 3142769223 scopus 로고    scopus 로고
    • Impact of Replacement of D1 C-terminal Alanine with Glycine on Structure and Function of Photosynthetic Oxygen-Evolving Complex
    • Mizusawa, N., Kimura, Y., Ishii, A., Yamanari, T., Nakazawa, S., Teramoto, H., and Ono, T.-A. (2004) Impact of Replacement of D1 C-terminal Alanine with Glycine on Structure and Function of Photosynthetic Oxygen-Evolving Complex J. Biol. Chem. 279, 29622-29627
    • (2004) J. Biol. Chem. , vol.279 , pp. 29622-29627
    • Mizusawa, N.1    Kimura, Y.2    Ishii, A.3    Yamanari, T.4    Nakazawa, S.5    Teramoto, H.6    Ono, T.-A.7
  • 65
    • 8744247473 scopus 로고    scopus 로고
    • Changes in the Functional and Structural Properties of the Mn Cluster Induced by Replacing the Side Group of the C-Terminus of the D1 Protein of Photosystem II
    • Mizusawa, N., Yamanari, T., Kimura, Y., Ishii, A., Nakazawa, S., and Ono, T.-A. (2004) Changes in the Functional and Structural Properties of the Mn Cluster Induced by Replacing the Side Group of the C-Terminus of the D1 Protein of Photosystem II Biochemistry 43, 14644-14652
    • (2004) Biochemistry , vol.43 , pp. 14644-14652
    • Mizusawa, N.1    Yamanari, T.2    Kimura, Y.3    Ishii, A.4    Nakazawa, S.5    Ono, T.-A.6
  • 66
    • 12544257799 scopus 로고    scopus 로고
    • Structural Changes of D1 C-terminal α-Carboxylate during S-state Cycling of Photosynthetic Oxygen Evolution
    • Kimura, Y., Mizusawa, N., Yamanari, T., Ishii, A., and Ono, T.-A. (2005) Structural Changes of D1 C-terminal α-Carboxylate during S-state Cycling of Photosynthetic Oxygen Evolution J. Biol. Chem. 280, 2078-2083
    • (2005) J. Biol. Chem. , vol.280 , pp. 2078-2083
    • Kimura, Y.1    Mizusawa, N.2    Yamanari, T.3    Ishii, A.4    Ono, T.-A.5
  • 67
    • 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.-A.2    Inoue, Y.3
  • 70
    • 1542436310 scopus 로고    scopus 로고
    • FTIR Studies on the Amino-Acid Ligands of the Photosynthetic Oxygen-Evolving Mn-Cluster
    • (Itoh, K. and Tasumi, M., Eds.), Waseda University Press, Tokyo, Japan
    • Noguchi, T., Sugiura, M., and Inoue, Y. (1999) FTIR Studies on the Amino-Acid Ligands of the Photosynthetic Oxygen-Evolving Mn-Cluster, in Fourier Transform Spectroscopy: Twelfth International Conference (Itoh, K. and Tasumi, M., Eds.) pp 459 - 460, Waseda University Press, Tokyo, Japan.
    • (1999) Fourier Transform Spectroscopy: Twelfth International Conference , pp. 459-460
    • Noguchi, T.1    Sugiura, M.2    Inoue, Y.3
  • 73
    • 0035861755 scopus 로고    scopus 로고
    • Substrate Water Exchange in Photosystem II Depends on the Peripheral Proteins
    • Hillier, W., Hendry, G., Burnap, R. L., and Wydrzynski, T. (2001) Substrate Water Exchange in Photosystem II Depends on the Peripheral Proteins J. Biol. Chem. 276, 46917-46924
    • (2001) J. Biol. Chem. , vol.276 , pp. 46917-46924
    • Hillier, W.1    Hendry, G.2    Burnap, R.L.3    Wydrzynski, T.4
  • 74
    • 44949191623 scopus 로고    scopus 로고
    • Mass Spectrometry-Based Methods for Studying Kinetics and Dynamics in Biological Systems
    • (Aartsma, T. J. and Matysik, J., Eds.), Springer, Dordrecht, The Netherlands
    • Konermann, L., Messinger, J., and Hillier, W. (2008) Mass Spectrometry-Based Methods for Studying Kinetics and Dynamics in Biological Systems, in Biophysical Techniques in Photosynthesis II (Aartsma, T. J. and Matysik, J., Eds.) pp 167 - 190, Springer, Dordrecht, The Netherlands.
    • (2008) Biophysical Techniques in Photosynthesis II , pp. 167-190
    • Konermann, L.1    Messinger, J.2    Hillier, W.3
  • 75
    • 38049079870 scopus 로고    scopus 로고
    • 18O-water Exchange in Photosystem II: Substrate Binding and Intermediates of the Water Splitting Cycle
    • 18O-water Exchange in Photosystem II: Substrate Binding and Intermediates of the Water Splitting Cycle Coord. Chem. Rev. 252, 306-317
    • (2008) Coord. Chem. Rev. , vol.252 , pp. 306-317
    • Hillier, W.1    Wydrzynski, T.2
  • 76
    • 8144230165 scopus 로고    scopus 로고
    • Structure-based Mechanism of Photosynthetic Water Oxidation
    • McEvoy, J. P. and Brudvig, G. W. (2004) Structure-Based Mechanism of Photosynthetic Water Oxidation Phys. Chem. Chem. Phys. 6, 4754-4763
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 4754-4763
    • McEvoy, J.P.1    Brudvig, G.W.2
  • 78
    • 41449116568 scopus 로고    scopus 로고
    • Quantum Mechanics/Molecular Mechanics Study of the Catalytic Cycle of Water Splitting in Photosystem II
    • Sproviero, E. M., Gascón, J. A., McEvoy, J. P., Brudvig, G. W., and Batista, V. S. (2008) Quantum Mechanics/Molecular Mechanics Study of the Catalytic Cycle of Water Splitting in Photosystem II J. Am. Chem. Soc. 130, 3428-3442
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 3428-3442
    • Sproviero, E.M.1    Gascón, J.A.2    McEvoy, J.P.3    Brudvig, G.W.4    Batista, V.S.5
  • 80
    • 0034640197 scopus 로고    scopus 로고
    • Proton and hydrogen currents in photosynthetic water oxidation
    • DOI 10.1016/S0005-2728(00)00069-4, PII S0005272800000694
    • Tommos, C. and Babcock, G. T. (2000) Proton and Hydrogen Currents in Photosynthetic Water Oxidation Biochim. Biophys. Acta 1458, 199-219 (Pubitemid 30254260)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1458 , Issue.1 , pp. 199-219
    • Tommos, C.1    Babcock, G.T.2
  • 81
    • 33144471312 scopus 로고    scopus 로고
    • Energetics of a Possible Proton Exit Pathway for Water Oxidation in Photosystem II
    • Ishikita, H., Saenger, W., Loll, B., Biesiadka, J., and Knapp, E.-W. (2006) Energetics of a Possible Proton Exit Pathway for Water Oxidation in Photosystem II Biochemistry 45, 2063-2071
    • (2006) Biochemistry , vol.45 , pp. 2063-2071
    • Ishikita, H.1    Saenger, W.2    Loll, B.3    Biesiadka, J.4    Knapp, E.-W.5
  • 82
    • 34547116864 scopus 로고    scopus 로고
    • Structural Characteristics of Channels and Pathways in Photosystem II Including the Identification of an Oxygen Channel
    • Murray, J. W. and Barber, J. (2007) Structural Characteristics of Channels and Pathways in Photosystem II Including the Identification of an Oxygen Channel J. Struct. Biol. 159, 228-237
    • (2007) J. Struct. Biol. , vol.159 , pp. 228-237
    • Murray, J.W.1    Barber, J.2
  • 83
    • 38849188029 scopus 로고    scopus 로고
    • 4 Cluster in Photosystem II based on Solvent Accessibility Simulation, with Implications for Substrate Water Access
    • 4 Cluster in Photosystem II based on Solvent Accessibility Simulation, with Implications for Substrate Water Access Biochim. Biophys. Acta 1777, 140-153
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 140-153
    • Ho, F.M.1    Styring, S.2
  • 85
    • 33749052047 scopus 로고    scopus 로고
    • Chance and Design - Proton Transfer in Water, Channels and Bioenergetic Proteins
    • Wraight, C. A. (2006) Chance and Design - Proton Transfer in Water, Channels and Bioenergetic Proteins Biochim. Biophys. Acta 1757, 886-912
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 886-912
    • Wraight, C.A.1
  • 86
    • 34548724094 scopus 로고    scopus 로고
    • Solvent-mediated Proton Transfer in Catalysis by Carbonic Anhydrase
    • Silverman, D. N. and McKenna, R. (2007) Solvent-Mediated Proton Transfer in Catalysis by Carbonic Anhydrase Acc. Chem. Res. 40, 669-675
    • (2007) Acc. Chem. Res. , vol.40 , pp. 669-675
    • Silverman, D.N.1    McKenna, R.2
  • 87
    • 74449085230 scopus 로고    scopus 로고
    • Proton Transfer in Catalysis and the Role of Proton Shuttles in Carbonic Anhydrase
    • Mikulski, R. L. and Silverman, D. N. (2010) Proton Transfer in Catalysis and the Role of Proton Shuttles in Carbonic Anhydrase Biochim. Biophys. Acta 1804, 422-426
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 422-426
    • Mikulski, R.L.1    Silverman, D.N.2
  • 89
    • 0242657390 scopus 로고    scopus 로고
    • Proton Transfer Pathways and Mechanism in Bacterial Reaction Centers
    • Paddock, M. L., Feher, G., and Okamura, M. Y. (2003) Proton Transfer Pathways and Mechanism in Bacterial Reaction Centers FEBS Lett. 555, 45-50
    • (2003) FEBS Lett. , vol.555 , pp. 45-50
    • Paddock, M.L.1    Feher, G.2    Okamura, M.Y.3
  • 90
    • 33646365537 scopus 로고    scopus 로고
    • Intraprotein Proton Transfer - Concepts and Realities from the Bacterial Photosynthetic Reaction Center
    • (Wikström M., Ed.), RSC Publishing, Cambridge, U.K
    • Wraight, C. A. (2005) Intraprotein Proton Transfer - Concepts and Realities from the Bacterial Photosynthetic Reaction Center, in Biophysical and Structural Aspects of Bioenergetics (Wikström, M., Ed.) pp 273 - 313, RSC Publishing, Cambridge, U.K.
    • (2005) Biophysical and Structural Aspects of Bioenergetics , pp. 273-313
    • Wraight, C.A.1
  • 91
    • 33746349218 scopus 로고    scopus 로고
    • Energy Transduction: Proton Transfer Through the Respiratory Complexes
    • Hosler, J. P., Ferguson-Miller, S., and Mills, D. A. (2006) Energy Transduction: Proton Transfer Through the Respiratory Complexes Annu. Rev. Biochem. 75, 165-187
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 165-187
    • Hosler, J.P.1    Ferguson-Miller, S.2    Mills, D.A.3
  • 92
    • 34848850437 scopus 로고    scopus 로고
    • Mechanism and Energetics of Proton Translocation by the Respiratory Heme-Copper Oxidases
    • Wikström, M. and Verkhovsky, M. I. (2007) Mechanism and Energetics of Proton Translocation by the Respiratory Heme-Copper Oxidases Biochim. Biophys. Acta 1767, 1200-1214
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1200-1214
    • Wikström, M.1    Verkhovsky, M.I.2
  • 93
    • 57049180108 scopus 로고    scopus 로고
    • Cytochrome c Oxidase: Exciting Progress and Remaining Mysteries
    • Brzezinski, P. and Gennis, R. B. (2008) Cytochrome c Oxidase: Exciting Progress and Remaining Mysteries J. Bioenerg. Biomembr. 40, 521-531
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 521-531
    • Brzezinski, P.1    Gennis, R.B.2
  • 95
    • 0024367788 scopus 로고
    • A Calcium-specific Site Influences the Structure and Activity of the Manganese Cluster Responsible for Photosynthetic Water Oxidation
    • Sivaraja, M., Tso, J., and Dismukes, G. C. (1989) A Calcium-Specific Site Influences the Structure and Activity of the Manganese Cluster Responsible for Photosynthetic Water Oxidation Biochemistry 28, 9459-9464
    • (1989) Biochemistry , vol.28 , pp. 9459-9464
    • Sivaraja, M.1    Tso, J.2    Dismukes, G.C.3
  • 96
    • 58149372330 scopus 로고
    • 3 Transition in Photosynthetic Oxygen Evolution System
    • 3 Transition in Photosynthetic Oxygen Evolution System Biochim. Biophys. Acta 973, 443-449
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 443-449
    • Ono, T.-A.1    Inoue, Y.2
  • 100
    • 8144226360 scopus 로고    scopus 로고
    • D1 Protein Processing and Mn Cluster Assembly in Light of the Emerging Photosystem II Structure
    • Burnap, R. L. (2004) D1 Protein Processing and Mn Cluster Assembly in Light of the Emerging Photosystem II Structure Phys. Chem. Chem. Phys. 6, 4803-4809
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 4803-4809
    • Burnap, R.L.1
  • 101
    • 38049100652 scopus 로고    scopus 로고
    • Photoassembly of the Water-Oxidizing Complex in Photosystem II
    • DasGupta, J., Ananyev, G., and Dismukes, G. C. (2008) Photoassembly of the Water-Oxidizing Complex in Photosystem II Coord. Chem. Rev. 252, 347-360
    • (2008) Coord. Chem. Rev. , vol.252 , pp. 347-360
    • Dasgupta, J.1    Ananyev, G.2    Dismukes, G.C.3
  • 109
    • 85001163723 scopus 로고
    • Relationships between the Carbon-Oxygen Stretching Frequencies of Carboxylato Complexes and the Type of Carboxylate Coordination
    • Deacon, G. B. and Phillips, R. J. (1980) Relationships between the Carbon-Oxygen Stretching Frequencies of Carboxylato Complexes and the Type of Carboxylate Coordination Coord. Chem. Rev. 33, 227-250
    • (1980) Coord. Chem. Rev. , vol.33 , pp. 227-250
    • Deacon, G.B.1    Phillips, R.J.2
  • 110
    • 0024621968 scopus 로고
    • FT-IR Characterization of Metal Acetates in Aqueous Solution
    • Tackett, J. E. (1989) FT-IR Characterization of Metal Acetates in Aqueous Solution Appl. Spectrosc. 43, 483-489
    • (1989) Appl. Spectrosc. , vol.43 , pp. 483-489
    • Tackett, J.E.1
  • 112
    • 33748386052 scopus 로고    scopus 로고
    • Correlation between the Vibrational Frequencies of the Carboxylate Group and Types of its Coordination to a Metal Ion: An ab Initio Molecular Orbital Study
    • Nara, M., Torii, H., and Tasumi, M. (1996) Correlation between the Vibrational Frequencies of the Carboxylate Group and Types of its Coordination to a Metal Ion: An ab Initio Molecular Orbital Study J. Phys. Chem. 100, 19812-19817
    • (1996) J. Phys. Chem. , vol.100 , pp. 19812-19817
    • Nara, M.1    Torii, H.2    Tasumi, M.3
  • 113
    • 0025613794 scopus 로고
    • 2O) Solutions. 1. Spectral Parameters of Amino Acid Residue Absorption Bands
    • 2O) Solutions. 1. Spectral Parameters of Amino Acid Residue Absorption Bands Biopolymers 30, 1243-1257
    • (1990) Biopolymers , vol.30 , pp. 1243-1257
    • Venyaminov, S.Yu.1    Kalnin, N.N.2
  • 114
    • 0344906170 scopus 로고    scopus 로고
    • Infrared Absorbances of Protein Side Chains
    • Rahmelow, K., Hübner, W., and Ackermann, Th. (1998) Infrared Absorbances of Protein Side Chains Anal. Biochem. 257, 1-11
    • (1998) Anal. Biochem. , vol.257 , pp. 1-11
    • Rahmelow, K.1    Hübner, W.2    Ackermann, Th.3
  • 115
    • 0034473318 scopus 로고    scopus 로고
    • The Infrared Absorption of Amino Acid Side Chains
    • Barth, A. (2000) The Infrared Absorption of Amino Acid Side Chains Prog. Biophys. Mol. Biol. 74, 141-173
    • (2000) Prog. Biophys. Mol. Biol. , vol.74 , pp. 141-173
    • Barth, A.1
  • 116
    • 0036880493 scopus 로고    scopus 로고
    • What Vibrations Tell Us about Proteins
    • Barth, A. and Zscherp, C. (2002) What Vibrations Tell Us About Proteins Q. Rev. Biophys. 35, 369-430
    • (2002) Q. Rev. Biophys. , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 118
    • 77749255459 scopus 로고    scopus 로고
    • Tracking the Flow of Water through Photosystem II Using Molecular Dynamics and Streamline Tracing
    • Vassiliev, S., Comte, P., Mahboob, A., and Bruce, D. (2010) Tracking the Flow of Water through Photosystem II Using Molecular Dynamics and Streamline Tracing Biochemistry 49, 1873-1881
    • (2010) Biochemistry , vol.49 , pp. 1873-1881
    • Vassiliev, S.1    Comte, P.2    Mahboob, A.3    Bruce, D.4
  • 119
    • 21844457647 scopus 로고    scopus 로고
    • Ligand Substitution Reactions at Inorganic Centers
    • Richens, D. T. (2005) Ligand Substitution Reactions at Inorganic Centers Chem. Rev. 105, 1961-2002
    • (2005) Chem. Rev. , vol.105 , pp. 1961-2002
    • Richens, D.T.1
  • 121
    • 0039597109 scopus 로고    scopus 로고
    • Structure of an Active Water Molecule in the Water-Oxidizing Complex of Photosystem II As Studied by FTIR Spectroscopy
    • Noguchi, T. and Sugiura, M. (2000) Structure of an Active Water Molecule in the Water-Oxidizing Complex of Photosystem II As Studied by FTIR Spectroscopy Biochemistry 39, 10943-10949
    • (2000) Biochemistry , vol.39 , pp. 10943-10949
    • Noguchi, T.1    Sugiura, M.2
  • 122
    • 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
  • 123
    • 54349117457 scopus 로고    scopus 로고
    • Monitoring Water Reactions during the S-State Cycle of the Photosynthetic Water-Oxidizing Center: Detection of the DOD Bending Vibrations by Means of Fourier Transform Infrared Spectroscopy
    • Suzuki, H., Sugiura, M., and Noguchi, T. (2008) Monitoring Water Reactions during the S-State Cycle of the Photosynthetic Water-Oxidizing Center: Detection of the DOD Bending Vibrations by Means of Fourier Transform Infrared Spectroscopy Biochemistry 47, 11024-11030
    • (2008) Biochemistry , vol.47 , pp. 11024-11030
    • Suzuki, H.1    Sugiura, M.2    Noguchi, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.