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Volumn 51, Issue 29, 2012, Pages 5774-5783

Fourier-transform infrared study of the photoactivation process of Xenopus (6-4) photolyase

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE I; ANION RADICALS; DNA-REPAIR ENZYMES; ELECTRON TRANSFER; FLAVIN ADENINE DINUCLEOTIDE; FT-IR SPECTRUM; FTIR; FTIR ANALYSIS; GENETIC INTEGRITY; HELICITIES; NEUTRAL RADICAL; NORMAL BASIS; ONE-ELECTRON TRANSFER; PHOTOACTIVATION; PHOTOLYASES; PHOTOPRODUCTS; PROTON DONORS; PROTONATED; REDOX STATE; SEMIQUINONES; STRETCHING VIBRATIONS; STRUCTURAL CHANGE; STRUCTURAL PERTURBATION; TWO PHOTON; UV VISIBLE SPECTROSCOPY; UV-VISIBLE; XENOPUS;

EID: 84864194063     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300530x     Document Type: Article
Times cited : (16)

References (51)
  • 1
    • 0038305458 scopus 로고    scopus 로고
    • Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors
    • Sancar, A. (2003) Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors Chem. Rev. 103, 2203-2237
    • (2003) Chem. Rev. , vol.103 , pp. 2203-2237
    • Sancar, A.1
  • 2
    • 13844256579 scopus 로고    scopus 로고
    • Light-driven enzymatic catalysis of DNA repair: A review of recent biophysical studies on photolyase
    • DOI 10.1016/j.bbabio.2004.02.010
    • Weber, S. (2005) Light-driven enzymatic catalysis of DNA repair: A review of recent biophysical studies on photolyase Biochim. Biophys. Acta 1707, 1-23 (Pubitemid 40253587)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1707 , Issue.SPEC. ISS. , pp. 1-23
    • Weber, S.1
  • 3
    • 0027439741 scopus 로고
    • A new photoreactivating enzyme that specifically repairs ultraviolet light-induced (6-4)photoproducts
    • DOI 10.1038/361371a0
    • Todo, T., Takemori, H., Ryo, H., Ihara, M., Matsunaga, T., Nikaido, O., Sato, K., and Nomura, T. (1993) A new photoreactivating enzyme that specifically repairs ultraviolet light-induced (6-4) photoproducts Nature 361, 371-374 (Pubitemid 23041633)
    • (1993) Nature , vol.361 , Issue.6410 , pp. 371-374
    • Todo, T.1    Takemori, H.2    Ryo, H.3    Ihara, M.4    Matsunaga, T.5    Nikaido, O.6    Sato, K.7    Nomura, T.8
  • 7
    • 0034214080 scopus 로고    scopus 로고
    • Intraprotein radical transfer during photoactivation of DNA photolyase
    • Aubert, C., Vos, M. H., Mathis, P., Eker, A. P., and Brettel, K. (2000) Intraprotein radical transfer during photoactivation of DNA photolyase Nature 405, 586-590
    • (2000) Nature , vol.405 , pp. 586-590
    • Aubert, C.1    Vos, M.H.2    Mathis, P.3    Eker, A.P.4    Brettel, K.5
  • 8
    • 0026503938 scopus 로고
    • The third chromophore of DNA photolyase: Trp-277 of Escherichia coli DNA photolyase repairs thymine dimers by direct electron transfer
    • Kim, S. T., Li, Y. F., and Sancar, A. (1992) The third chromophore of DNA photolyase: Trp-277 of Escherichia coli DNA photolyase repairs thymine dimers by direct electron transfer Proc. Natl. Acad. Sci. U.S.A. 89, 900-904
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 900-904
    • Kim, S.T.1    Li, Y.F.2    Sancar, A.3
  • 10
    • 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
  • 11
    • 18744379142 scopus 로고    scopus 로고
    • Proteins in action monitored by time-resolved FTIR spectroscopy
    • DOI 10.1002/cphc.200400504
    • Kötting, C. and Gerwert, K. (2005) Proteins in action monitored by time-resolved FTIR spectroscopy ChemPhysChem 6, 881-888 (Pubitemid 40669551)
    • (2005) ChemPhysChem , vol.6 , Issue.5 , pp. 881-888
    • Kotting, C.1    Gerwert, K.2
  • 12
    • 33947539623 scopus 로고    scopus 로고
    • Light-induced FTIR difference spectroscopy as a powerful tool toward understanding the molecular mechanism of photosynthetic oxygen evolution
    • DOI 10.1007/s11120-007-9137-5
    • 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 (Pubitemid 46466318)
    • (2007) Photosynthesis Research , vol.91 , Issue.1 , pp. 59-69
    • Noguchi, T.1
  • 14
    • 34250346126 scopus 로고    scopus 로고
    • A novel photoreaction mechanism for the circadian blue light photoreceptor Drosophila cryptochrome
    • DOI 10.1074/jbc.M608872200
    • Berndt, A., Kottke, T., Breitkreuz, H., Dvorsky, R., Hennig, S., Alexander, M., and Wolf, E. (2007) A novel photoreaction mechanism for the circadian blue light photoreceptor Drosophila cryptochrome J. Biol. Chem. 282, 13011-13021 (Pubitemid 47100638)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 13011-13021
    • Berndt, A.1    Kottke, T.2    Breitkreuz, H.3    Dvorsky, R.4    Hennig, S.5    Alexander, M.6    Wolf, E.7
  • 17
    • 0034660609 scopus 로고    scopus 로고
    • Bacterial cryptochrome and photolyase: Characterization of two photolyase-like genes of Synechocystis sp. PCC6803
    • Hitomi, K., Okamoto, K., Daiyasu, H., Miyashita, H., Iwai, S., Toh, H., Ishiura, M., and Todo, T. (2000) Bacterial cryptochrome and photolyase: Characterization of two photolyase-like genes of Synechocystis sp. PCC6803 Nucleic Acids Res. 28, 2353-2362 (Pubitemid 30349040)
    • (2000) Nucleic Acids Research , vol.28 , Issue.12 , pp. 2353-2362
    • Hitomi, K.1    Okamoto, K.2    Daiyasu, H.3    Miyashita, H.4    Iwai, S.5    Toh, H.6    Ishiura, M.7    Todo, T.8
  • 18
    • 77957904119 scopus 로고    scopus 로고
    • Key dynamics of conserved asparagine in a cryptochrome/photolyase family protein by Fourier transform infrared spectroscopy
    • Iwata, T., Zhang, Y., Hitomi, K., Getzoff, E. D., and Kandori, H. (2010) Key dynamics of conserved asparagine in a cryptochrome/photolyase family protein by Fourier transform infrared spectroscopy Biochemistry 49, 8882-8891
    • (2010) Biochemistry , vol.49 , pp. 8882-8891
    • Iwata, T.1    Zhang, Y.2    Hitomi, K.3    Getzoff, E.D.4    Kandori, H.5
  • 20
    • 34250191465 scopus 로고    scopus 로고
    • Hydration and temperature similarly affect light-induced protein structural changes in the chromophoric domain of phototropin
    • DOI 10.1021/bi7003087
    • Iwata, T., Yamamoto, A., Tokutomi, S., and Kandori, H. (2007) Hydration and temperature similarly affects light-induced protein structural changes in the chromophore domain of phototropin Biochemistry 46, 7016-7021 (Pubitemid 46906430)
    • (2007) Biochemistry , vol.46 , Issue.23 , pp. 7016-7021
    • Iwata, T.1    Yamamoto, A.2    Tokutomi, S.3    Kandori, H.4
  • 21
    • 38349119939 scopus 로고    scopus 로고
    • Role of Phe1010 in light-induced structural changes of the neo1-LOV2 domain of Adiantum
    • Yamamoto, A., Iwata, T., Tokutomi, S., and Kandori, H. (2008) Role of Phe1010 in light-induced structural changes of the neo1-LOV2 domain of Adiantum Biochemistry 47, 922-928
    • (2008) Biochemistry , vol.47 , pp. 922-928
    • Yamamoto, A.1    Iwata, T.2    Tokutomi, S.3    Kandori, H.4
  • 22
    • 33947528119 scopus 로고    scopus 로고
    • Electron nuclear double resonance differentiates complementary roles for active site histidines in (6-4) photolyase
    • DOI 10.1074/jbc.M604734200
    • Schleicher, E., Hitomi, K., Kay, C. W. M., Getzoff, E. D., Todo, T., and Weber, S. (2007) Electron nuclear double resonance differentiates complementary roles for active site histidines in (6-4) photolyase J. Biol. Chem. 282, 4738-4747 (Pubitemid 47100916)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.7 , pp. 4738-4747
    • Schleicher, E.1    Hitomi, K.2    Kay, C.W.M.3    Getzoff, E.D.4    Todo, T.5    Weber, S.6
  • 23
    • 70349914561 scopus 로고    scopus 로고
    • Microsecond light-induced proton transfer to flavin in the blue light sensor plant cryptochrome
    • Langenbacher, T., Immeln, D., Dick, B., and Kottke, T. (2009) Microsecond light-induced proton transfer to flavin in the blue light sensor plant cryptochrome J. Am. Chem. Soc. 131, 14274-14280
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 14274-14280
    • Langenbacher, T.1    Immeln, D.2    Dick, B.3    Kottke, T.4
  • 26
    • 0345733997 scopus 로고    scopus 로고
    • Redox-Triggered FTIR Difference Spectra of FAD in Aqueous Solution and Bound to Flavoproteins
    • DOI 10.1021/bi035219f
    • Wille, G., Ritter, M., Friedemann, R., Möntele, W., and Hübner, G. (2003) Redox-triggered FTIR difference spectra of FAD in aqueous solution and bound to flavoproteins Biochemistry 42, 14814-14821 (Pubitemid 37553509)
    • (2003) Biochemistry , vol.42 , Issue.50 , pp. 14814-14821
    • Wille, G.1    Ritter, M.2    Friedemann, R.3    Mantele, W.4    Hubner, G.5
  • 27
    • 0019889065 scopus 로고
    • Normal mode analysis of lumiflavin and interpretation of resonance Raman spectra of flavoproteins
    • Bowman, W. D. and Spiro, T. G. (1981) Normal mode analysis of lumiflavin and interpretation of resonance Raman spectra of flavoproteins Biochemistry 20, 3313-3318
    • (1981) Biochemistry , vol.20 , pp. 3313-3318
    • Bowman, W.D.1    Spiro, T.G.2
  • 28
    • 0021094373 scopus 로고
    • Assignment and the effect of hydrogen bonding on the vibrational normal modes of flavins and flavoproteins
    • Schmidt, J., Coudron, P., Thompson, A. W., Watters, K. L., and McFarland, J. T. (1983) Assignment and the effect of hydrogen bonding on the vibrational normal modes of flavins and flavoproteins Biochemistry 22, 76-84
    • (1983) Biochemistry , vol.22 , pp. 76-84
    • Schmidt, J.1    Coudron, P.2    Thompson, A.W.3    Watters, K.L.4    McFarland, J.T.5
  • 29
    • 0001411522 scopus 로고
    • Vibrational analysis of flavin derivatives: Normal coordinate treatments of lumiflavin
    • Abe, M. and Kyogoku, Y. (1987) Vibrational analysis of flavin derivatives: Normal coordinate treatments of lumiflavin Spectrochim. Acta 43A, 1027-1038
    • (1987) Spectrochim. Acta , vol.43 , pp. 1027-1038
    • Abe, M.1    Kyogoku, Y.2
  • 30
    • 0001027209 scopus 로고
    • Assignment and the effect of hydrogen bonding on the vibrational normal modes of flavins and flavoproteins
    • Livery, C. R. and McFarland, J. T. (1990) Assignment and the effect of hydrogen bonding on the vibrational normal modes of flavins and flavoproteins J. Phys. Chem. 94, 3980-3994
    • (1990) J. Phys. Chem. , vol.94 , pp. 3980-3994
    • Livery, C.R.1    McFarland, J.T.2
  • 31
    • 0001049969 scopus 로고
    • Time-resolved SERS study of direct photochemical charge transfer between FMN and a Ag electrode
    • Zhang, W., Vivoni, A., Lombard, J. R., and Birke, R. L. (1995) Time-resolved SERS study of direct photochemical charge transfer between FMN and a Ag electrode J. Phys. Chem. 99, 12846-12857
    • (1995) J. Phys. Chem. , vol.99 , pp. 12846-12857
    • Zhang, W.1    Vivoni, A.2    Lombard, J.R.3    Birke, R.L.4
  • 32
    • 79952269602 scopus 로고    scopus 로고
    • IR spectra of flavins in solution: DFT/MM description of redox effects
    • Rieff, B., Bauer, S., Mathias, G., and Tavan, P. (2011) IR spectra of flavins in solution: DFT/MM description of redox effects J. Phys. Chem. B 115, 2117-2123
    • (2011) J. Phys. Chem. B , vol.115 , pp. 2117-2123
    • Rieff, B.1    Bauer, S.2    Mathias, G.3    Tavan, P.4
  • 33
    • 33748564613 scopus 로고    scopus 로고
    • Characteristic structure and environment in FAD cofactor of (6-4) photolyase along function revealed by resonance Raman spectroscopy
    • DOI 10.1021/jp062998b
    • Li, J., Uchida, T., Ohta, T., Todo, T., and Kitagawa, T. (2006) Characteristic structure and environment in FAD cofactor of (6-4) photolyase along function revealed by resonance Raman spectroscopy J. Phys. Chem. B 110, 16724-16732 (Pubitemid 44373402)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.33 , pp. 16724-16732
    • Li, J.1    Uchida, T.2    Ohta, T.3    Todo, T.4    Kitagawa, T.5
  • 34
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • DOI 10.1016/S0079-6107(00)00021-3, PII S0079610700000213
    • Barth, A. (2000) The infrared absorption of amino acid side chains Prog. Biophys. Mol. Biol. 74, 141-173 (Pubitemid 32168153)
    • (2000) Progress in Biophysics and Molecular Biology , vol.74 , Issue.3-5 , pp. 141-173
    • Barth, A.1
  • 35
    • 33644553813 scopus 로고    scopus 로고
    • Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy
    • Kottke, T., Batschauer, A., Ahmad, M., and Heberle, J. (2006) Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy Biochemistry 45, 2472-2479
    • (2006) Biochemistry , vol.45 , pp. 2472-2479
    • Kottke, T.1    Batschauer, A.2    Ahmad, M.3    Heberle, J.4
  • 37
    • 0000216262 scopus 로고    scopus 로고
    • Structural and vibrational analysis of indolyl radical and indolyl radical cation from density functional methods
    • Walden, S. E. and Wheeler, R. A. (1996) Structural and vibrational analysis of indolyl radical and indolyl radical cation from density functional methods J. Chem. Soc., Perkin Trans. 2, 2663-2672 (Pubitemid 126436984)
    • (1996) Journal of the Chemical Society. Perkin Transactions 2 , vol.1996 , Issue.12 , pp. 2663-2672
    • Walden, S.E.1    Wheeler, R.A.2
  • 38
    • 34249887915 scopus 로고    scopus 로고
    • FTIR study on the hydrogen bond structure of a key tyrosine residue in the flavin-binding blue light sensor TePixD from Thermosynechococcus elongatus
    • DOI 10.1021/bi7004653
    • Takahashi, R., Okajima, K., Suzuki, H., Nakamura, H., Ikeuchi, M., and Noguchi, T. (2007) FTIR study on the hydrogen bond structure of a key tyrosine residue in the flavin-binding blue light sensor TePixD from Thermosynechococcus elongates Biochemistry 46, 6459-6467 (Pubitemid 46870113)
    • (2007) Biochemistry , vol.46 , Issue.22 , pp. 6459-6467
    • Takahashi, R.1    Okajima, K.2    Suzuki, H.3    Nakamura, H.4    Ikeuchi, M.5    Noguchi, T.6
  • 39
    • 84984249419 scopus 로고
    • FTIR and EPR study of radical of aromatic amino acids 4-methylimidazole and phenol generated by UV irradiation
    • Berthomieu, C. and Boussac, A. (1995) FTIR and EPR study of radical 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
  • 40
    • 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
    • DOI 10.1021/bi971760y
    • 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 (Pubitemid 27524391)
    • (1997) Biochemistry , vol.36 , Issue.48 , pp. 14705-14711
    • Noguchi, T.1    Inoue, Y.2    Tang, X.-S.3
  • 41
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm, S. and Bandekar, J. (1986) Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins Adv. Protein Chem. 38, 181-364
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 42
    • 17444409955 scopus 로고    scopus 로고
    • Light-induced reactions of Escherichia coli DNA photolyase monitored by Fourier transform infrared spectroscopy
    • DOI 10.1111/j.1742-4658.2005.04617.x
    • Schleicher, E., Hessling, B., Illarionova, V., Bacher, A., Weber, S., Richter, G., and Gerwert, K. (2005) Light-induced reactions of Escherichia coli DNA photolyase monitored by Fourier transform infrared spectroscopy FEBS J. 272, 1855-1866 (Pubitemid 40547244)
    • (2005) FEBS Journal , vol.272 , Issue.8 , pp. 1855-1866
    • Schleicher, E.1    Hessling, B.2    Illarionova, V.3    Bacher, A.4    Weber, S.5    Richter, G.6    Gerwert, K.7
  • 45
    • 3242722151 scopus 로고    scopus 로고
    • Altered hydrogen bonding of Arg82 during the proton pump cycle of bacteriorhodopsin: A low-temperature polarized FTIR spectroscopic study
    • DOI 10.1021/bi049368p
    • Tanimoto, T., Shibata, M., Belenky, M., Herzfeld, J., and Kandori, H. (2004) Altered hydrogen bonding of Arg82 during the proton pump cycle of bacteriorhodopsin: A low-temperature polarized FTIR spectroscopic study Biochemistry 43, 9439-9447 (Pubitemid 38955476)
    • (2004) Biochemistry , vol.43 , Issue.29 , pp. 9439-9447
    • Tanimoto, T.1    Shibata, M.2    Belenky, M.3    Herzfeld, J.4    Kandori, H.5
  • 47
    • 68849111523 scopus 로고    scopus 로고
    • Different role of the Ja helix in the light-induced activation of the LOV2 domains in various phototropins
    • Koyama, T., Iwata, T., Yamamoto, A., Sato, Y., Matsuoka, D., Tokutomi, S., and Kandori, H. (2009) Different role of the Ja helix in the light-induced activation of the LOV2 domains in various phototropins Biochemistry 48, 7621-7628
    • (2009) Biochemistry , vol.48 , pp. 7621-7628
    • Koyama, T.1    Iwata, T.2    Yamamoto, A.3    Sato, Y.4    Matsuoka, D.5    Tokutomi, S.6    Kandori, H.7
  • 48
    • 0028909764 scopus 로고
    • Infrared spectroscopy applied to biochemical and biological problems
    • Siebert, F. (1995) Infrared spectroscopy applied to biochemical and biological problems Methods Enzymol. 246, 501-526
    • (1995) Methods Enzymol. , vol.246 , pp. 501-526
    • Siebert, F.1
  • 49
    • 33745727013 scopus 로고    scopus 로고
    • The photochemistry of the light-, oxygen-, and voltage-sensitive domains in the algal blue light receptor phot
    • DOI 10.1002/bip.20510
    • Kottke, T., Hegemann, P., Dick, B., and Heberle, J. (2006) The photochemistry of the light-, oxygen-, and voltage-sensitive domains in the algal blue light receptor phot Biopolymers 82, 373-378 (Pubitemid 44000907)
    • (2006) Biopolymers , vol.82 , Issue.4 , pp. 373-378
    • Kottke, T.1    Hegemann, P.2    Dick, B.3    Heberle, J.4
  • 50
    • 83455194627 scopus 로고    scopus 로고
    • Light-induced structural changes of the LOV2 domains in various phototropins revealed by FTIR spectroscopy
    • Iwata, T., Tokutomi, S., and Kandori, H. (2011) Light-induced structural changes of the LOV2 domains in various phototropins revealed by FTIR spectroscopy Biophysics 7, 89-98
    • (2011) Biophysics , vol.7 , pp. 89-98
    • Iwata, T.1    Tokutomi, S.2    Kandori, H.3


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