메뉴 건너뛰기




Volumn 101, Issue 2-3, 2009, Pages 157-170

Fourier transform infrared (FTIR) spectroscopy

Author keywords

Fourier transform infrared spectroscopy; Isotope edited infrared spectroscopy; Metal ligands; Water molecules

Indexed keywords

LIGAND; METAL; VEGETABLE PROTEIN;

EID: 72149119691     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-009-9439-x     Document Type: Review
Times cited : (352)

References (100)
  • 1
    • 0037094081 scopus 로고    scopus 로고
    • Spectroscopic properties of tyrosyl radicals in dipeptides
    • Ayala I, Range K, York D, Barry BA (2002) Spectroscopic properties of tyrosyl radicals in dipeptides. J Am Chem Soc 124: 5496-5505.
    • (2002) J Am Chem Soc , vol.124 , pp. 5496-5505
    • Ayala, I.1    Range, K.2    York, D.3    Barry, B.A.4
  • 2
    • 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
  • 3
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • Barth A (2007) Infrared spectroscopy of proteins. Biochim Biophys Acta 1767: 1073-1101.
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 1073-1101
    • Barth, A.1
  • 4
    • 0036840913 scopus 로고    scopus 로고
    • Characterization of a new caged proton capable of inducing large pH jumps
    • Barth A, Corrie JE (2002) Characterization of a new caged proton capable of inducing large pH jumps. Biophys J 83: 2864-2871.
    • (2002) Biophys J , vol.83 , pp. 2864-2871
    • Barth, A.1    Corrie, J.E.2
  • 5
    • 0025641033 scopus 로고
    • Molecular changes in the sarcoplasmic reticulum Ca2+ ATPase during catalytic activity: A Fourier transform infrared (FTIR) study using photolysis of caged ATP to trigger the reaction cycle
    • Barth A, Mantele W, Kreutz W (1990) Molecular changes in the sarcoplasmic reticulum Ca2+ ATPase during catalytic activity: a Fourier transform infrared (FTIR) study using photolysis of caged ATP to trigger the reaction cycle. FEBS Lett 277: 147-150.
    • (1990) FEBS Lett , vol.277 , pp. 147-150
    • Barth, A.1    Mantele, W.2    Kreutz, W.3
  • 6
    • 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: 191-195.
    • (1990) FEBS Lett , vol.261 , pp. 191-195
    • Bauscher, M.1    Nabedryk, E.2    Bagley, K.3    Breton, J.4    Mäntele, W.5
  • 7
    • 84984249419 scopus 로고
    • FTIR and EPR study of radicals of aromatic amino acids, 4-methylimidazole and phenol generated by UV-irradiation
    • Berthomieu C, Boussac A (1995) FTIR and EPR study of radicals of aromatic amino acids, 4-methylimidazole and phenol generated by UV-irradiation. Biospectroscopy 1: 187-206.
    • (1995) Biospectroscopy , vol.1 , pp. 187-206
    • Berthomieu, C.1    Boussac, A.2
  • 8
    • 0035799313 scopus 로고    scopus 로고
    • Iron coordination in photosystem II: Interaction between bicarbonate and the QB pocket studied by Fourier transform infrared spectroscopy
    • Berthomieu C, Hienerwadel R (2001) Iron coordination in photosystem II: interaction between bicarbonate and the QB pocket studied by Fourier transform infrared spectroscopy. Biochemistry 40: 4044-4052.
    • (2001) Biochemistry , vol.40 , pp. 4044-4052
    • Berthomieu, C.1    Hienerwadel, R.2
  • 9
    • 13844275382 scopus 로고    scopus 로고
    • Vibrational spectroscopy to study the properties of redox-active tyrosines in photosystem II and other proteins
    • Berthomieu C, Hienerwadel R (2005) Vibrational spectroscopy to study the properties of redox-active tyrosines in photosystem II and other proteins. Biochim Biophys Acta 1707: 51-66.
    • (2005) Biochim Biophys Acta , vol.1707 , pp. 51-66
    • Berthomieu, C.1    Hienerwadel, R.2
  • 10
    • 0026454816 scopus 로고
    • Molecular changes following oxidoreduction of cytochrome b559 characterized by Fourier transform infrared spectroscopy and electron paramagnetic resonance: Photooxidation in photosystem II and electrochemistry of isolated cytochrome b559 and iron protoporphyrin IX- bisimidazole model compounds
    • Berthomieu C, Boussac A, Mäntele W, Breton J, Nabedryk E (1992) Molecular changes following oxidoreduction of cytochrome b559 characterized by Fourier transform infrared spectroscopy and electron paramagnetic resonance: photooxidation in photosystem II and electrochemistry of isolated cytochrome b559 and iron protoporphyrin IX- bisimidazole model compounds. Biochemistry 31: 11460-11471.
    • (1992) Biochemistry , vol.31 , pp. 11460-11471
    • Berthomieu, C.1    Boussac, A.2    Mäntele, W.3    Breton, J.4    Nabedryk, E.5
  • 11
    • 0032311393 scopus 로고    scopus 로고
    • Effect of 13C, 18O, and 2H labeling on the infrared modes of UV-induced phenoxyl radicals
    • Berthomieu C, Boullais C, Neumann JM, Boussac A (1998a) Effect of 13C, 18O, and 2H labeling on the infrared modes of UV-induced phenoxyl radicals. Biochim Biophys Acta 1365: 112-116.
    • (1998) Biochim Biophys Acta , vol.1365 , pp. 112-116
    • Berthomieu, C.1    Boullais, C.2    Neumann, J.M.3    Boussac, A.4
  • 12
    • 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, Diner BA (1998b) 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
  • 13
    • 33745713079 scopus 로고    scopus 로고
    • Electrochemically-induced FTIR difference spectroscopy in the mid to far infrared (200 μm) domain: A new setup for the analysis of metal-ligands in redox-proteins
    • Berthomieu C, Marboutin L, Dupeyrat F, Bouyer P (2006) Electrochemically-induced FTIR difference spectroscopy in the mid to far infrared (200 μm) domain: a new setup for the analysis of metal-ligands in redox-proteins. Biopolymers 82: 363-367.
    • (2006) Biopolymers , vol.82 , pp. 363-367
    • Berthomieu, C.1    Marboutin, L.2    Dupeyrat, F.3    Bouyer, P.4
  • 14
    • 0035976019 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy of primary electron donors in type I photosynthetic reaction centers
    • Breton J (2001) Fourier transform infrared spectroscopy of primary electron donors in type I photosynthetic reaction centers. Biochim Biophys Acta 1507: 180-193.
    • (2001) Biochim Biophys Acta , vol.1507 , pp. 180-193
    • Breton, J.1
  • 15
    • 0028364701 scopus 로고
    • The binding sites of quinones in photosynthetic bacterial reaction centers investigated by light-induced FTIR difference spectroscopy: Assignment of the QA vibrations in Rhodobacter sphaeroides using 18O- or 13C- labeled ubiquinones and vitamin K1
    • Breton J, Burie J-R, Berthomieu C, Berger G, Nabedryk E (1994a) The binding sites of quinones in photosynthetic bacterial reaction centers investigated by light-induced FTIR difference spectroscopy: assignment of the QA vibrations in Rhodobacter sphaeroides using 18O- or 13C- labeled ubiquinones and vitamin K1. Biochemistry 33: 4953-4965.
    • (1994) Biochemistry , vol.33 , pp. 4953-4965
    • Breton, J.1    Burie, J.-R.2    Berthomieu, C.3    Berger, G.4    Nabedryk, E.5
  • 16
    • 0028557366 scopus 로고
    • Binding sites of quinones in photosynthetic bacterial reaction centers investigated by light-induced FTIR difference spectroscopy: Assignment of the interactions of each carbonyl of QA in Rhodobacter sphaeroides using site-specific 13C-labeled ubiquinone
    • Breton J, Boullais C, Burie JR, Nabedryk E, Mioskowsky C (1994b) Binding sites of quinones in photosynthetic bacterial reaction centers investigated by light-induced FTIR difference spectroscopy: assignment of the interactions of each carbonyl of QA in Rhodobacter sphaeroides using site-specific 13C-labeled ubiquinone. Biochemistry 33: 14378-14386.
    • (1994) Biochemistry , vol.33 , pp. 14378-14386
    • Breton, J.1    Boullais, C.2    Burie, J.R.3    Nabedryk, E.4    Mioskowsky, C.5
  • 17
    • 0029111537 scopus 로고
    • Binding sites of quinones in photosynthetic bacterial reaction centers investigated by light-induced FTIR difference spectroscopy: Symmetry of the carbonyl interactions and close equivalence of the QB vibrations in Rhodopseudomonas sphaeroides and Rhodobacter viridis probed by isotope labeling
    • Breton J, Boullais C, Mioskowski C, Nabedryk E (1995) Binding sites of quinones in photosynthetic bacterial reaction centers investigated by light-induced FTIR difference spectroscopy: symmetry of the carbonyl interactions and close equivalence of the QB vibrations in Rhodopseudomonas sphaeroides and Rhodobacter viridis probed by isotope labeling. Biochemistry 34: 11606-11616.
    • (1995) Biochemistry , vol.34 , pp. 11606-11616
    • Breton, J.1    Boullais, C.2    Mioskowski, C.3    Nabedryk, E.4
  • 18
    • 0037125950 scopus 로고    scopus 로고
    • The two histidine axial ligands of the primary electron donor chlorophylls (P700) in photosystem I are similarly perturbed upon P700+ formation
    • Breton J, Xu W, Diner BA, Chitnis PR (2002) The two histidine axial ligands of the primary electron donor chlorophylls (P700) in photosystem I are similarly perturbed upon P700+ formation. Biochemistry 41: 11200-11210.
    • (2002) Biochemistry , vol.41 , pp. 11200-11210
    • Breton, J.1    Xu, W.2    Diner, B.A.3    Chitnis, P.R.4
  • 19
    • 0028089816 scopus 로고
    • Asymmetric binding of the 1- and 4-C=O groups of QA in Rhodobacter sphaeroides R26 reaction centers monitored by Fourier transform infra-red spectroscopy using site-specific isotopically labelled ubiquinone-10
    • Brudler R, de Groot HJM, van Liemt WBS, Steggerda WF, Esmeijer R, Gast P, Hoff AJ, Lugtenburg J, Gerwert K (1994) Asymmetric binding of the 1- and 4-C=O groups of QA in Rhodobacter sphaeroides R26 reaction centers monitored by Fourier transform infra-red spectroscopy using site-specific isotopically labelled ubiquinone-10. EMBO J 13: 5523-5530.
    • (1994) EMBO J , vol.13 , pp. 5523-5530
    • Brudler, R.1    de Groot, H.J.M.2    van Liemt, W.B.S.3    Steggerda, W.F.4    Esmeijer, R.5    Gast, P.6    Hoff, A.J.7    Lugtenburg, J.8    Gerwert, K.9
  • 20
    • 0029084343 scopus 로고
    • FTIR spectroscopy shows weak symmetric hydrogen bonding of the QB carbonyl groups in Rhodobacter sphaeroides R26 reaction centers
    • Brudler R, de Groot HJM, van Liemt WBS, Gast R, Hoff AJ, Lugtenburg J, Gerwert K (1995) FTIR spectroscopy shows weak symmetric hydrogen bonding of the QB carbonyl groups in Rhodobacter sphaeroides R26 reaction centers. FEBS Lett 370: 88-92.
    • (1995) FEBS Lett , vol.370 , pp. 88-92
    • Brudler, R.1    de Groot, H.J.M.2    van Liemt, W.B.S.3    Gast, R.4    Hoff, A.J.5    Lugtenburg, J.6    Gerwert, K.7
  • 21
    • 0026416198 scopus 로고
    • Ca2+ release from caged-Ca2+ alters the FTIR spectrum of sarcoplasmic reticulum
    • Buchet R, Jona I, Martonosi A (1991) Ca2+ release from caged-Ca2+ alters the FTIR spectrum of sarcoplasmic reticulum. Biochim Biophys Acta 1069: 209-217.
    • (1991) Biochim Biophys Acta , vol.1069 , pp. 209-217
    • Buchet, R.1    Jona, I.2    Martonosi, A.3
  • 22
    • 0035808669 scopus 로고    scopus 로고
    • Vibrational spectroscopy of the oxygen-evolving complex and of manganese model compounds
    • Chu HA, Hillier W, Law NA, Babcock GT (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
  • 23
    • 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 HA, Hillier W, Debus RJ (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
  • 25
    • 85001163723 scopus 로고
    • Relationships between the carbon-oxygen stretching frequencies of carboxylato complexes and the type of carboxylate coordination
    • Deacon GB, Phillips RJ (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
  • 26
    • 38049029119 scopus 로고    scopus 로고
    • Protein ligation of the photosynthetic oxygen-evolving center
    • Debus RJ (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
  • 27
    • 0032824280 scopus 로고    scopus 로고
    • Raman spectroscopic studies of the structures, energetics, and bond distortions of substrates bound to enzymes
    • Deng H, Callender R (1999) Raman spectroscopic studies of the structures, energetics, and bond distortions of substrates bound to enzymes. Methods Enzymol 308: 176-201.
    • (1999) Methods Enzymol , vol.308 , pp. 176-201
    • Deng, H.1    Callender, R.2
  • 28
    • 45849117619 scopus 로고    scopus 로고
    • Primary charge separation in the photosystem II core from Synechocystis: A comparison of femtosecond visible/midinfrared pump-probe spectra of wild-type and two P680 mutants
    • Di Donato M, Cohen RO, Diner BA, Breton J, van Grondelle R, Groot ML (2008) Primary charge separation in the photosystem II core from Synechocystis: a comparison of femtosecond visible/midinfrared pump-probe spectra of wild-type and two P680 mutants. Biophys J 94: 4783-4795.
    • (2008) Biophys J , vol.94 , pp. 4783-4795
    • Di donato, M.1    Cohen, R.O.2    Diner, B.A.3    Breton, J.4    van Grondelle, R.5    Groot, M.L.6
  • 29
    • 9144235732 scopus 로고    scopus 로고
    • Long distance charge redistribution upon Cu, Zn-superoxide dismutase reduction-significance of dismutase function
    • Dupeyrat F, Vidaud C, Lorphelin A, Berthomieu C (2004) Long distance charge redistribution upon Cu, Zn-superoxide dismutase reduction-significance of dismutase function. J Biol Chem 279: 48091-48101.
    • (2004) J Biol Chem , vol.279 , pp. 48091-48101
    • Dupeyrat, F.1    Vidaud, C.2    Lorphelin, A.3    Berthomieu, C.4
  • 31
    • 20544439112 scopus 로고    scopus 로고
    • Identification of a Cd2+ and Zn2+ binding site in cytochrome c using FTIR coupled to an ATR micro-dialysis set-up and NMR spectroscopy
    • Gourion-Arsiquaud S, Chevance S, Bouyer P, Garnier L, Montillet JL, Bondon A, Berthomieu C (2005) Identification of a Cd2+ and Zn2+ binding site in cytochrome c using FTIR coupled to an ATR micro-dialysis set-up and NMR spectroscopy. Biochemistry 44: 8652-8663.
    • (2005) Biochemistry , vol.44 , pp. 8652-8663
    • Gourion-Arsiquaud, S.1    Chevance, S.2    Bouyer, P.3    Garnier, L.4    Montillet, J.L.5    Bondon, A.6    Berthomieu, C.7
  • 33
    • 0001617001 scopus 로고    scopus 로고
    • Vibrational spectra and ab initio DFT calculations of 4-methylimidazole and its different protonation forms: Infrared and Raman markers of the protonation state of a histidine side chain
    • Hasegawa K, Ono T, Noguchi T (2000) Vibrational spectra and ab initio DFT calculations of 4-methylimidazole and its different protonation forms: infrared and Raman markers of the protonation state of a histidine side chain. J Phys Chem B 104: 4253-4265.
    • (2000) J Phys Chem B , vol.104 , pp. 4253-4265
    • Hasegawa, K.1    Ono, T.2    Noguchi, T.3
  • 34
    • 0037061931 scopus 로고    scopus 로고
    • Ab initio DFT calculations and vibrational analysis of zinc-bound 4-methylimidazole as a model of a histidine ligand in metalloenzymes
    • Hasegawa K, Ono T, Noguchi T (2002) Ab initio DFT calculations and vibrational analysis of zinc-bound 4-methylimidazole as a model of a histidine ligand in metalloenzymes. J Phys Chem A 106: 3377-3390.
    • (2002) J Phys Chem A , vol.106 , pp. 3377-3390
    • Hasegawa, K.1    Ono, T.2    Noguchi, T.3
  • 35
    • 0035980251 scopus 로고    scopus 로고
    • Primary donor photo-oxidation in photosystem I: A re-evaluation of (P700(+) - P700) Fourier transform infrared difference spectra
    • Hastings G, Ramesh VM, Wang R, Sivakumar V, Webber A (2001) Primary donor photo-oxidation in photosystem I: a re-evaluation of (P700(+) - P700) Fourier transform infrared difference spectra. Biochemistry 40: 12943-12949.
    • (2001) Biochemistry , vol.40 , pp. 12943-12949
    • Hastings, G.1    Ramesh, V.M.2    Wang, R.3    Sivakumar, V.4    Webber, A.5
  • 36
    • 41449088536 scopus 로고    scopus 로고
    • Site-specific relaxation kinetics of a tryptophan zipper hairpin peptide using temperature-jump IR spectroscopy and isotopic labeling
    • Hauser K, Krejtschi C, Huang R, Wu L, Keiderling TA (2008) Site-specific relaxation kinetics of a tryptophan zipper hairpin peptide using temperature-jump IR spectroscopy and isotopic labeling. J Am Chem Soc 130: 2984-2992.
    • (2008) J Am Chem Soc , vol.130 , pp. 2984-2992
    • Hauser, K.1    Krejtschi, C.2    Huang, R.3    Wu, L.4    Keiderling, T.A.5
  • 37
    • 0029584591 scopus 로고
    • Bicarbonate binding to the non-heme iron of photosystem II investigated by Fourier transform infrared difference spectroscopy and 13C-labeled bicarbonate
    • Hienerwadel R, Berthomieu C (1995) Bicarbonate binding to the non-heme iron of photosystem II investigated by Fourier transform infrared difference spectroscopy and 13C-labeled bicarbonate. Biochemistry 34: 16288-16297.
    • (1995) Biochemistry , vol.34 , pp. 16288-16297
    • Hienerwadel, R.1    Berthomieu, C.2
  • 38
    • 0026648198 scopus 로고
    • Time-resolved infrared spectroscopy of electron transfer in bacterial photosynthetic reaction centers: Dynamics of binding and interaction upon QA and QB reduction
    • Hienerwadel R, Thibodeau D, Lenz F, Nabedryk E, Breton J, Kreutz W, Mäntele W (1990) Time-resolved infrared spectroscopy of electron transfer in bacterial photosynthetic reaction centers: dynamics of binding and interaction upon QA and QB reduction. Biochemistry 31: 5799-5808.
    • (1990) Biochemistry , vol.31 , pp. 5799-5808
    • Hienerwadel, R.1    Thibodeau, D.2    Lenz, F.3    Nabedryk, E.4    Breton, J.5    Kreutz, W.6    Mäntele, W.7
  • 39
    • 0028967120 scopus 로고
    • Protonation of Glu L212 following QB- formation in the photosynthetic reaction center of Rhodobacter sphaeroides: Evidence from time-resolved infrared spectroscopy
    • Hienerwadel R, Grzybek S, Fogel C, Kreutz W, Okamura MY, Paddock ML, Breton J, Nabedryk E, Mäntele W (1995) Protonation of Glu L212 following QB- formation in the photosynthetic reaction center of Rhodobacter sphaeroides: evidence from time-resolved infrared spectroscopy. Biochemistry 34: 2832-2843.
    • (1995) Biochemistry , vol.34 , pp. 2832-2843
    • Hienerwadel, R.1    Grzybek, S.2    Fogel, C.3    Kreutz, W.4    Okamura, M.Y.5    Paddock, M.L.6    Breton, J.7    Nabedryk, E.8    Mäntele, W.9
  • 40
    • 0029856747 scopus 로고    scopus 로고
    • Fourier transform infrared difference study of tyrosineD oxidation and plastoquinone QA reduction in photosystem II
    • Hienerwadel R, Boussac A, Breton J, Berthomieu C (1996) Fourier transform infrared difference study of tyrosineD oxidation and plastoquinone QA reduction in photosystem II. Biochemistry 35: 15447-15460.
    • (1996) Biochemistry , vol.35 , pp. 15447-15460
    • Hienerwadel, R.1    Boussac, A.2    Breton, J.3    Berthomieu, C.4
  • 41
    • 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 BA, 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
  • 42
    • 44649122732 scopus 로고    scopus 로고
    • Molecular origin of the pH dependence of tyrosine D oxidation kinetics and radical stability in photosystem II
    • Hienerwadel R, Diner BA, Berthomieu C (2008) Molecular origin of the pH dependence of tyrosine D oxidation kinetics and radical stability in photosystem II. Biochim Biophys Acta 1777: 525-531.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 525-531
    • Hienerwadel, R.1    Diner, B.A.2    Berthomieu, C.3
  • 43
    • 0035992560 scopus 로고    scopus 로고
    • Attenuated total reflection Fourier transform infrared spectroscopy of redox transitions in photosynthetic reaction centers: Comparison of perfusion- and light-induced difference spectra
    • Iwaki M, Andrianambinintsoa S, Rich P, Breton J (2002) Attenuated total reflection Fourier transform infrared spectroscopy of redox transitions in photosynthetic reaction centers: comparison of perfusion- and light-induced difference spectra. Spectrochim Acta A Mol Biomol Spectrosc 58: 1523-1533.
    • (2002) Spectrochim Acta A Mol Biomol Spectrosc , vol.58 , pp. 1523-1533
    • Iwaki, M.1    Andrianambinintsoa, S.2    Rich, P.3    Breton, J.4
  • 44
    • 0034734254 scopus 로고    scopus 로고
    • Role of internal water molecules in bacteriorhodopsin
    • Kandori H (2000) Role of internal water molecules in bacteriorhodopsin. Biochim Biophys Acta 1460: 177-191.
    • (2000) Biochim Biophys Acta , vol.1460 , pp. 177-191
    • Kandori, H.1
  • 45
    • 33846364530 scopus 로고    scopus 로고
    • FTIR studies of the redox partner interaction in cytochrome P450: The Pdx-P450cam couple
    • Karyakin A, Motiejunas D, Wade RC, Jung C (2007) FTIR studies of the redox partner interaction in cytochrome P450: the Pdx-P450cam couple. Biochim Biophys Acta 1770: 420-431.
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 420-431
    • Karyakin, A.1    Motiejunas, D.2    Wade, R.C.3    Jung, C.4
  • 46
    • 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, 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
  • 47
    • 18744379142 scopus 로고    scopus 로고
    • Proteins in action monitored by time-resolved FTIR spectroscopy
    • Kötting C, Gerwert K (2005) Proteins in action monitored by time-resolved FTIR spectroscopy. ChemPhysChem 6: 881-888.
    • (2005) ChemPhysChem , vol.6 , pp. 881-888
    • Kötting, C.1    Gerwert, K.2
  • 48
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm S, Bandekar J (1986) Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv Prot Chem 38: 181-364.
    • (1986) Adv Prot Chem , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 49
    • 0036156679 scopus 로고    scopus 로고
    • Suramin affects coupling of rhodopsin to transducin
    • Lehmann N, Aradhyam GK, Fahmy K (2002) Suramin affects coupling of rhodopsin to transducin. Biophys J 82: 793-802.
    • (2002) Biophys J , vol.82 , pp. 793-802
    • Lehmann, N.1    Aradhyam, G.K.2    Fahmy, K.3
  • 50
    • 0027216215 scopus 로고
    • Fourier transform infrared spectroscopy and electrochemistry of the primary electron donor in Rhodobacter sphaeroides and Rhodopseudomonas viridis reaction centers: Vibrational modes of the pigments in situ and evidence for protein and water modes affected by P+ formation
    • Leonhard M, Mäntele W (1993) Fourier transform infrared spectroscopy and electrochemistry of the primary electron donor in Rhodobacter sphaeroides and Rhodopseudomonas viridis reaction centers: vibrational modes of the pigments in situ and evidence for protein and water modes affected by P+ formation. Biochemistry 32: 4532-4538.
    • (1993) Biochemistry , vol.32 , pp. 4532-4538
    • Leonhard, M.1    Mäntele, W.2
  • 51
    • 21244464637 scopus 로고    scopus 로고
    • Fourier transform infrared vibrational spectroscopic imaging: Integrating microscopy and molecular recognition
    • Levin IW, Bhargava R (2005) Fourier transform infrared vibrational spectroscopic imaging: integrating microscopy and molecular recognition. Ann Rev Phys Chem 56: 429-474.
    • (2005) Ann Rev Phys Chem , vol.56 , pp. 429-474
    • Levin, I.W.1    Bhargava, R.2
  • 52
    • 41449088527 scopus 로고    scopus 로고
    • Active internal waters in the bacteriorhodopsin photocycle. A comparative study of the L and M intermediates at room and cryogenic temperatures by infrared spectroscopy
    • Lorenz-Fonfria VA, Furutani Y, Kandori H (2008) Active internal waters in the bacteriorhodopsin photocycle. A comparative study of the L and M intermediates at room and cryogenic temperatures by infrared spectroscopy. Biochemistry 47: 4071-4081.
    • (2008) Biochemistry , vol.47 , pp. 4071-4081
    • Lorenz-Fonfria, V.A.1    Furutani, Y.2    Kandori, H.3
  • 53
    • 0000627943 scopus 로고
    • Infrared spectroelectrochemistry of bacteriochlorophylls and bacteriopheophytins: Implications for the binding of the pigments in the reaction center from photosynthetic bacteria
    • USA
    • Mäntele W, Wollenweber AM, Nabedryk E, Breton J (1988a) 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: 8468-8472.
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 8468-8472
    • Mäntele, W.1    Wollenweber, A.M.2    Nabedryk, E.3    Breton, J.4
  • 55
    • 33746734322 scopus 로고    scopus 로고
    • Biologically active molecules with a "light switch"
    • Mayer G, Heckel A (2006) Biologically active molecules with a "light switch". Angew Chem 45: 4900-4921.
    • (2006) Angew Chem , vol.45 , pp. 4900-4921
    • Mayer, G.1    Heckel, A.2
  • 56
    • 0037239339 scopus 로고    scopus 로고
    • Time-resolved step-scan FTIR investigation on the primary donor of the reaction center from the green sulfur bacterium Chlorobium tepidum
    • Mezzetti A, Seo D, Leibl W, Sakurai H, Breton J (2003) Time-resolved step-scan FTIR investigation on the primary donor of the reaction center from the green sulfur bacterium Chlorobium tepidum. Photosynth Res 75: 161-169.
    • (2003) Photosynth Res , vol.75 , pp. 161-169
    • Mezzetti, A.1    Seo, D.2    Leibl, W.3    Sakurai, H.4    Breton, J.5
  • 57
    • 0025115245 scopus 로고
    • Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c
    • Moss D, Nabedryk E, Breton J, Mäntele W (1990) Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c. Eur J Biochem 187: 565-572.
    • (1990) Eur J Biochem , vol.187 , pp. 565-572
    • Moss, D.1    Nabedryk, E.2    Breton, J.3    Mäntele, W.4
  • 58
    • 49349096539 scopus 로고    scopus 로고
    • Folding kinetics of a naturally occurring helical peptide: Implication of the folding speed limit of helical proteins
    • Mukherjee S, Chowdhury P, Bunagan MR, Gai F (2008) Folding kinetics of a naturally occurring helical peptide: implication of the folding speed limit of helical proteins. J Phys Chem B 112: 9146-9150.
    • (2008) J Phys Chem B , vol.112 , pp. 9146-9150
    • Mukherjee, S.1    Chowdhury, P.2    Bunagan, M.R.3    Gai, F.4
  • 59
    • 0002859824 scopus 로고    scopus 로고
    • Light-induced Fourier transform infrared difference spectroscopy of the primary electron donor in photosynthetic reaction centers
    • H. H. Mantsch and D. Chapman (Eds.), New York: Wiley-Liss
    • Nabedryk E (1996) Light-induced Fourier transform infrared difference spectroscopy of the primary electron donor in photosynthetic reaction centers. In: Mantsch HH, Chapman D (eds) Infrared spectroscopy of biomolecules. Wiley-Liss, New York, pp 39-81.
    • (1996) Infrared Spectroscopy of Biomolecules , pp. 39-81
    • Nabedryk, E.1
  • 60
    • 52949129815 scopus 로고    scopus 로고
    • Coupling of electron transfer to proton uptake at the QB site of the bacterial reaction center: A perspective from FTIR difference spectroscopy
    • Nabedryk E, Breton J (2008) Coupling of electron transfer to proton uptake at the QB site of the bacterial reaction center: a perspective from FTIR difference spectroscopy. Biochim Biophys Acta 1777: 1229-1248.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 1229-1248
    • Nabedryk, E.1    Breton, J.2
  • 61
    • 0025305948 scopus 로고
    • Fourier transform infrared difference spectroscopy shows no evidence for an enolization of chlorophyll a upon cation formation either in vitro or during P700 photooxidation
    • Nabedryk E, Leonhardt M, Mäntele W, Breton J (1990a) Fourier transform infrared difference spectroscopy shows no evidence for an enolization of chlorophyll a upon cation formation either in vitro or during P700 photooxidation. Biochemistry 29: 3242-3247.
    • (1990) Biochemistry , vol.29 , pp. 3242-3247
    • Nabedryk, E.1    Leonhardt, M.2    Mäntele, W.3    Breton, J.4
  • 62
    • 0025292657 scopus 로고
    • A protein conformational change associated with the photoreduction of the primary and secondary quinones in the bacterial reaction center
    • Nabedryk E, Bagley KA, Thibodeau DL, Bauscher M, Mäntele W, Breton J (1990b) A protein conformational change associated with the photoreduction of the primary and secondary quinones in the bacterial reaction center. FEBS Lett 266: 59-62.
    • (1990) FEBS Lett , vol.266 , pp. 59-62
    • Nabedryk, E.1    Bagley, K.A.2    Thibodeau, D.L.3    Bauscher, M.4    Mäntele, W.5    Breton, J.6
  • 63
    • 0028973591 scopus 로고
    • Fourier transforms infrared difference spectroscopy of secondary quinone acceptor photoreduction in proton transfer mutants of Rhodobacter sphaeroides
    • Nabedryk E, Breton J, Hienerwadel R, Fogel C, Mäntele W, Paddock ML, Okamura MY (1995) Fourier transforms infrared difference spectroscopy of secondary quinone acceptor photoreduction in proton transfer mutants of Rhodobacter sphaeroides. Biochemistry 34: 14722-14732.
    • (1995) Biochemistry , vol.34 , pp. 14722-14732
    • Nabedryk, E.1    Breton, J.2    Hienerwadel, R.3    Fogel, C.4    Mäntele, W.5    Paddock, M.L.6    Okamura, M.Y.7
  • 65
    • 22144464025 scopus 로고    scopus 로고
    • A vibrational spectral marker for probing the hydrogen-bonding status of protonated Asp and Glu residues
    • Nie B, Stutzman J, Xie A (2005) A vibrational spectral marker for probing the hydrogen-bonding status of protonated Asp and Glu residues. Biophysical J 88: 2833-2847.
    • (2005) Biophysical J , vol.88 , pp. 2833-2847
    • Nie, B.1    Stutzman, J.2    Xie, A.3
  • 66
    • 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
  • 67
    • 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
  • 68
    • 32344439352 scopus 로고    scopus 로고
    • Molecular analysis by vibrational spectroscopy
    • T. Wydrzynski and K. Satoh (Eds.), Dordrecht, The Netherlands: Springer
    • Noguchi T, Berthomieu C (2005) Molecular analysis by vibrational spectroscopy. In: Wydrzynski T, Satoh K (eds) Photosystem II: the light-drivenwater/plastoquinone oxidoreductase, vol 16. Springer, Dordrecht, The Netherlands, pp 367-387.
    • (2005) Photosystem II: The Light-Drivenwater/Plastoquinone Oxidoreductase , vol.16 , pp. 367-387
    • Noguchi, T.1    Berthomieu, C.2
  • 69
    • 0039597109 scopus 로고    scopus 로고
    • Structure of an active water molecule in the water-oxidising complex of photosystem II as studied by FTIR spectroscopy
    • Noguchi T, Sugiura M (2000) Structure of an active water molecule in the water-oxidising 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
  • 70
    • 0037133143 scopus 로고    scopus 로고
    • Flash-induced FTIR difference spectroscopy of the water oxidizing complex in moderately hydrated photosystem II core films: Effect of hydration extent on S-state transitions
    • Noguchi T, Sugiura M (2002a) Flash-induced FTIR difference spectroscopy 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
  • 71
    • 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, Sugiura M (2002b) 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
  • 72
    • 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, 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
  • 73
    • 0028046023 scopus 로고
    • Fourier transform infrared spectrum of the radical cation of beta-carotene photoinduced in photosystem II
    • Noguchi T, Mitsuka T, Inoue Y (1994) Fourier transform infrared spectrum of the radical cation of beta-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
  • 74
    • 0028948099 scopus 로고
    • Direct detection of a carboxylate bridge between Mn and Ca2+ in the photosynthetic oxygen-evolving center by means of Fourier transform infrared spectroscopy
    • Noguchi T, Ono T, Inoue Y (1995) Direct detection of a carboxylate bridge between Mn and Ca2+ 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
  • 75
    • 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, 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
  • 76
    • 0032578446 scopus 로고    scopus 로고
    • Fourier transform infrared study of the cation radical of P680 in the photosystem II reaction center: Evidence for charge delocalization on the chlorophyll dimer
    • Noguchi T, Tomo T, Inoue Y (1998) Fourier transform infrared study of the cation radical of P680 in the photosystem II reaction center: evidence for charge delocalization on the chlorophyll dimer. Biochemistry 37: 13614-13625.
    • (1998) Biochemistry , vol.37 , pp. 13614-13625
    • Noguchi, T.1    Tomo, T.2    Inoue, Y.3
  • 77
    • 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, 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
  • 78
    • 0037085028 scopus 로고    scopus 로고
    • Density functional calculations modeling tyrosine oxidation in oxygenic photosynthetic electron transfer
    • O'Malley PJ (2002) Density functional calculations modeling tyrosine oxidation in oxygenic photosynthetic electron transfer. Biochim Biophys Acta 1553: 212-217.
    • (2002) Biochim Biophys Acta , vol.1553 , pp. 212-217
    • O'malley, P.J.1
  • 79
    • 3142580340 scopus 로고    scopus 로고
    • FTIR spectroscopy of Synechocystis 6803 mutants affected on the hydrogen bonds to the carbonyl groups of the PsaA chlorophyll of P700 supports an extensive delocalization of the charge in P700+
    • Pantelidou M, Chitnis PR, Breton J (2004) FTIR spectroscopy of Synechocystis 6803 mutants affected on the hydrogen bonds to the carbonyl groups of the PsaA chlorophyll of P700 supports an extensive delocalization of the charge in P700+. Biochemistry 43: 8380-8390.
    • (2004) Biochemistry , vol.43 , pp. 8380-8390
    • Pantelidou, M.1    Chitnis, P.R.2    Breton, J.3
  • 80
    • 33748571987 scopus 로고    scopus 로고
    • Chemical mapping of tumor progression by FT-IR imaging: Towards molecular histopathology
    • Petibois C, Déléris G (2006) Chemical mapping of tumor progression by FT-IR imaging: towards molecular histopathology. Trends Biotechnol 24: 455-462.
    • (2006) Trends Biotechnol , vol.24 , pp. 455-462
    • Petibois, C.1    Déléris, G.2
  • 81
    • 34249706283 scopus 로고    scopus 로고
    • Methods to probe protein transitions with ATR infrared spectroscopy
    • Rich P, Iwaki M (2007) Methods to probe protein transitions with ATR infrared spectroscopy. Mol BioSyst 3: 398-407.
    • (2007) Mol BioSyst , vol.3 , pp. 398-407
    • Rich, P.1    Iwaki, M.2
  • 82
    • 57849125414 scopus 로고    scopus 로고
    • D1-arginine mutants (R257E, K and Q) of Chlamydomonas reinhardtii have a lowered QB redox potential: Analysis of thermoluminescence and fluorescence measurements
    • Rose S, Minagawa J, Seufferheld M, Padden S, Svensson B, Kolling DRJ, Crofts AR, Govindjee (2008) D1-arginine mutants (R257E, K and Q) of Chlamydomonas reinhardtii have a lowered QB redox potential: analysis of thermoluminescence and fluorescence measurements. Photosynth Res 98: 449-468.
    • (2008) Photosynth Res , vol.98 , pp. 449-468
    • Rose, S.1    Minagawa, J.2    Seufferheld, M.3    Padden, S.4    Svensson, B.5    Kolling, D.R.J.6    Crofts, A.R.7    Govindjee8
  • 83
    • 0019891619 scopus 로고
    • Conformational changes of bacteriorhodopsin detected by Fourier transform infrared difference spectroscopy
    • Rothschild K, Zagaeski M, Cantore WA (1981) Conformational changes of bacteriorhodopsin detected by Fourier transform infrared difference spectroscopy. Biochem Biophys Res Comm 103: 483-489.
    • (1981) Biochem Biophys Res Comm , vol.103 , pp. 483-489
    • Rothschild, K.1    Zagaeski, M.2    Cantore, W.A.3
  • 85
    • 13544256286 scopus 로고    scopus 로고
    • A1 reduction in intact cyanobacterial photosystem I particles studied by time-resolved step-scan Fourier transform infrared difference spectroscopy and isotope labeling
    • Sivakumar V, Wang R, Hastings G (2005) A1 reduction in intact cyanobacterial photosystem I particles studied by time-resolved step-scan Fourier transform infrared difference spectroscopy and isotope labeling. Biochemistry 44: 1880-1893.
    • (2005) Biochemistry , vol.44 , pp. 1880-1893
    • Sivakumar, V.1    Wang, R.2    Hastings, G.3
  • 87
    • 33746303803 scopus 로고    scopus 로고
    • No evidence from FTIR difference spectroscopy that glutamate-189 of the D1 polypeptide ligates a Mn ion that undergoes oxidation during the S0 to S1, S1 to S2, or S2 to S3 transitions in photosystem II
    • Strickler MA, Hillier W, Debus J (2006) No evidence from FTIR difference spectroscopy that glutamate-189 of the D1 polypeptide ligates a Mn ion that undergoes oxidation during the S0 to S1, S1 to S2, or S2 to S3 transitions in photosystem II. Biochemistry 45: 8801-8811.
    • (2006) Biochemistry , vol.45 , pp. 8801-8811
    • Strickler, M.A.1    Hillier, W.2    Debus, J.3
  • 88
    • 33947380152 scopus 로고    scopus 로고
    • No evidence from FTIR difference spectroscopy that aspartate-342 of the D1 polypeptide ligates a Mn ion that undergoes oxidation during the S0 to S1, S1 to S2, or S2 to S3 transitions in photosystem II
    • Strickler MA, Walker LM, Hillier W, Britt RD, Debus J (2007) No evidence from FTIR difference spectroscopy that aspartate-342 of the D1 polypeptide ligates a Mn ion that undergoes oxidation during the S0 to S1, S1 to S2, or S2 to S3 transitions in photosystem II. Biochemistry 46: 3151-3160.
    • (2007) Biochemistry , vol.46 , pp. 3151-3160
    • Strickler, M.A.1    Walker, L.M.2    Hillier, W.3    Britt, R.D.4    Debus, J.5
  • 89
    • 38049169359 scopus 로고    scopus 로고
    • Criteria for determining the hydrogen-bond structures of a tyrosine side chain by Fourier transform infrared spectroscopy: Density functional theory analyses of model hydrogen-bonded complexes of p-cresol
    • Takahashi R, Noguchi T (2007) Criteria for determining the hydrogen-bond structures of a tyrosine side chain by Fourier transform infrared spectroscopy: density functional theory analyses of model hydrogen-bonded complexes of p-cresol. J Phys Chem B 111: 13833-13844.
    • (2007) J Phys Chem B , vol.111 , pp. 13833-13844
    • Takahashi, R.1    Noguchi, T.2
  • 90
    • 37049030041 scopus 로고    scopus 로고
    • Water molecules coupled to the redox-active tyrosine YD in photosystem II as detected by FTIR spectroscopy
    • Takahashi R, Sugiura M, Noguchi T (2007) Water molecules coupled to the redox-active tyrosine YD in photosystem II as detected by FTIR spectroscopy. Biochemistry 46: 14245-14249.
    • (2007) Biochemistry , vol.46 , pp. 14245-14249
    • Takahashi, R.1    Sugiura, M.2    Noguchi, T.3
  • 92
    • 0032926394 scopus 로고    scopus 로고
    • Role of bicarbonate in the photosystem II, the water-plastoquinone oxido-reductase of plant photosynthesis
    • van Rensen JJS, Xu C, Govindjee (1999) Role of bicarbonate in the photosystem II, the water-plastoquinone oxido-reductase of plant photosynthesis. Physiol Plant 105: 585-592.
    • (1999) Physiol Plant , vol.105 , pp. 585-592
    • van Rensen, J.J.S.1    Xu, C.2    Govindjee3
  • 93
    • 0025613794 scopus 로고
    • Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands
    • Venyaminov SY, Kalnin NN (1990a) Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands. Biopolymers 30: 1243-1257.
    • (1990) Biopolymers , vol.30 , pp. 1243-1257
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 94
    • 0025648652 scopus 로고
    • Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in alpha, beta-, and random coil conformations
    • Venyaminov SY, Kalnin NN (1990b) Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in alpha, beta-, and random coil conformations. Biopolymers 30: 1259-1271.
    • (1990) Biopolymers , vol.30 , pp. 1259-1271
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 96
    • 0000005909 scopus 로고
    • Time-resolved step-scan FT-IR investigations of the transition from KL to L in the bacteriorhodopsin photocycle: Identification of chromophore twists by assigning hydrogen-out-of-plane (HOOP) bending vibrations
    • Weidlich O, Siebert F (1993) Time-resolved step-scan FT-IR investigations of the transition from KL to L in the bacteriorhodopsin photocycle: identification of chromophore twists by assigning hydrogen-out-of-plane (HOOP) bending vibrations. Appl Spectrosc 47: 1394-1400.
    • (1993) Appl Spectrosc , vol.47 , pp. 1394-1400
    • Weidlich, O.1    Siebert, F.2
  • 97
    • 33744536180 scopus 로고    scopus 로고
    • Infrared spectra and molar absorption coefficients of the 20 alpha amino acids in aqueous solutions in the spectral range from 1800 to 500 cm-1
    • Wolpert M, Hellwig P (2006) Infrared spectra and molar absorption coefficients of the 20 alpha amino acids in aqueous solutions in the spectral range from 1800 to 500 cm-1. Spectrochim Acta A 64: 987-1001.
    • (2006) Spectrochim Acta A , vol.64 , pp. 987-1001
    • Wolpert, M.1    Hellwig, P.2
  • 99
    • 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, Ono T (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.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.