메뉴 건너뛰기




Volumn 96, Issue 1, 2009, Pages 38-48

Spectroscopic characterization of a (6-4) photolyase from the green alga Ostreococcus tauri

Author keywords

(6 4) photolyase; Flavin adenine dinucleotide (FAD); Ostreococcus tauri; Photoinduced oxidation; Photoreduction; Steady state spectroscopy

Indexed keywords

DEOXYRIBODIPYRIMIDINE PHOTOLYASE; FLAVINE ADENINE NUCLEOTIDE;

EID: 67349227758     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2009.04.003     Document Type: Article
Times cited : (18)

References (62)
  • 1
    • 0027439741 scopus 로고
    • A new photoreactivating enzyme that specifically repairs ultraviolet light-induced (6-4) photoproducts
    • Todo T., Takemori H., Ryo H., Ihara M., Matsunaga T., Nikaido O., Sato K., and Nomura T. A new photoreactivating enzyme that specifically repairs ultraviolet light-induced (6-4) photoproducts. Nature 361 (1993) 371-374
    • (1993) Nature , vol.361 , 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
  • 2
    • 0038305458 scopus 로고    scopus 로고
    • Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors
    • Sancar A. Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors. Chem. Rev. 103 (2003) 2203-2237
    • (2003) Chem. Rev. , vol.103 , pp. 2203-2237
    • Sancar, A.1
  • 3
    • 0028117141 scopus 로고
    • Structure and function of DNA photolyase
    • Sancar A. Structure and function of DNA photolyase. Biochemistry 33 (1994) 2-9
    • (1994) Biochemistry , vol.33 , pp. 2-9
    • Sancar, A.1
  • 4
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T. Instability and decay of the primary structure of DNA. Nature 362 (1993) 709-715
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 5
    • 0033617475 scopus 로고    scopus 로고
    • Cryptochromes: blue light receptors for plants and animals
    • Cashmore A.R., Jarillo J.A., Wu Y.J., and Liu D.M. Cryptochromes: blue light receptors for plants and animals. Science 284 (1999) 760-765
    • (1999) Science , vol.284 , pp. 760-765
    • Cashmore, A.R.1    Jarillo, J.A.2    Wu, Y.J.3    Liu, D.M.4
  • 7
    • 0032997614 scopus 로고    scopus 로고
    • Functional diversity of the DNA photolyase blue light receptor family
    • Todo T. Functional diversity of the DNA photolyase blue light receptor family. Mutat. Res.-DNA Repair 434 (1999) 89-97
    • (1999) Mutat. Res.-DNA Repair , vol.434 , pp. 89-97
    • Todo, T.1
  • 8
    • 0028812143 scopus 로고
    • Crystal structure of DNA photolyase from Escherichia coli
    • Park H.-W., Kim S.-T., Sancar A., and Deisenhofer J. Crystal structure of DNA photolyase from Escherichia coli. Science 268 (1995) 1866-1872
    • (1995) Science , vol.268 , pp. 1866-1872
    • Park, H.-W.1    Kim, S.-T.2    Sancar, A.3    Deisenhofer, J.4
  • 11
    • 33748564613 scopus 로고    scopus 로고
    • Characteristic structure and environment in FAD cofactor of (6-4) photolyase along function revealed by resonance Raman spectroscopy
    • Li J., Uchida T., Ohta T., Todo T., and Kitagawa T. Characteristic structure and environment in FAD cofactor of (6-4) photolyase along function revealed by resonance Raman spectroscopy. J. Phys. Chem. B 110 (2006) 16724-16732
    • (2006) J. Phys. Chem. B , vol.110 , pp. 16724-16732
    • Li, J.1    Uchida, T.2    Ohta, T.3    Todo, T.4    Kitagawa, T.5
  • 12
    • 0029914630 scopus 로고    scopus 로고
    • Similarity among the Drosophila (6-4) photolyase, a human photolyase homolog and the DNA photolyase blue-light photoreceptor family
    • Todo T., Ryo H., Yamamoto K., Toh H., Inui T., Ayaki H., Nomura T., and Ikenaga M. Similarity among the Drosophila (6-4) photolyase, a human photolyase homolog and the DNA photolyase blue-light photoreceptor family. Science 272 (1996) 109-112
    • (1996) Science , vol.272 , pp. 109-112
    • Todo, T.1    Ryo, H.2    Yamamoto, K.3    Toh, H.4    Inui, T.5    Ayaki, H.6    Nomura, T.7    Ikenaga, M.8
  • 14
    • 10044280323 scopus 로고    scopus 로고
    • Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair
    • Mees A., Klar T., Gnau P., Hennecke U., Eker A.P.M., Carell T., and Essen L.-O. Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair. Science 306 (2004) 1789-1793
    • (2004) Science , vol.306 , pp. 1789-1793
    • Mees, A.1    Klar, T.2    Gnau, P.3    Hennecke, U.4    Eker, A.P.M.5    Carell, T.6    Essen, L.-O.7
  • 17
    • 33748756801 scopus 로고    scopus 로고
    • Similarities and differences between cyclobutane pyrimidine dimer photolyase and (6-4) photolyase as revealed by resonance Raman spectroscopy - electron transfer from the FAD cofactor to ultraviolet-damaged DNA
    • Li J., Uchida T., Todo T., and Kitagawa T. Similarities and differences between cyclobutane pyrimidine dimer photolyase and (6-4) photolyase as revealed by resonance Raman spectroscopy - electron transfer from the FAD cofactor to ultraviolet-damaged DNA. J. Biol. Chem. 281 (2006) 25551-25559
    • (2006) J. Biol. Chem. , vol.281 , pp. 25551-25559
    • Li, J.1    Uchida, T.2    Todo, T.3    Kitagawa, T.4
  • 19
    • 0023114231 scopus 로고
    • Action mechanism of Escherichia coli DNA photolyase. III. Photolysis of the enzyme-substrate complex and the absolute action spectrum
    • Sancar G.B., Jorns M.S., Payne G., Fluke D.J., Rupert C.S., and Sancar A. Action mechanism of Escherichia coli DNA photolyase. III. Photolysis of the enzyme-substrate complex and the absolute action spectrum. J. Biol. Chem. 262 (1987) 492-498
    • (1987) J. Biol. Chem. , vol.262 , pp. 492-498
    • Sancar, G.B.1    Jorns, M.S.2    Payne, G.3    Fluke, D.J.4    Rupert, C.S.5    Sancar, A.6
  • 20
    • 0029118241 scopus 로고
    • Kim S.T., Heelis P.F., and Sancar A. (Eds), Academic Press Inc., San Diego
    • In: Kim S.T., Heelis P.F., and Sancar A. (Eds). Redox-active Amino Acids in Biology (1995), Academic Press Inc., San Diego 319-343
    • (1995) Redox-active Amino Acids in Biology , pp. 319-343
  • 21
    • 0025100995 scopus 로고
    • Chromophore function and interaction in Escherichia coli DNA photolyase: reconstruction of the apoenzyme with pterin and/or flavin derivatives
    • Jorns M.S., Wang B., Jordan S.P., and Chanderkar L.P. Chromophore function and interaction in Escherichia coli DNA photolyase: reconstruction of the apoenzyme with pterin and/or flavin derivatives. Biochemistry 29 (1990) 551-561
    • (1990) Biochemistry , vol.29 , pp. 551-561
    • Jorns, M.S.1    Wang, B.2    Jordan, S.P.3    Chanderkar, L.P.4
  • 22
    • 0033851115 scopus 로고    scopus 로고
    • The chemical and biological versatility of riboflavin
    • Massey V. The chemical and biological versatility of riboflavin. Biochem. Soc. Trans. 28 (2000) 283-296
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 283-296
    • Massey, V.1
  • 23
    • 33947528119 scopus 로고    scopus 로고
    • Electron nuclear double resonance differentiates complementary roles for active site histidines in (6-4) photolyase
    • Schleicher E., Hitomi K., Kay C.W.M., Getzoff E.D., Todo T., and Weber S. Electron nuclear double resonance differentiates complementary roles for active site histidines in (6-4) photolyase. J. Biol. Chem. 282 (2007) 4738-4747
    • (2007) J. Biol. Chem. , vol.282 , pp. 4738-4747
    • Schleicher, E.1    Hitomi, K.2    Kay, C.W.M.3    Getzoff, E.D.4    Todo, T.5    Weber, S.6
  • 25
    • 0026495678 scopus 로고
    • Energy transfer (deazaflavin FADH2) and electron transfer (FADH2 T<>T) kinetics in Anacystis nidulans photolyase
    • Kim S.-T., Heelis P.F., and Sancar A. Energy transfer (deazaflavin FADH2) and electron transfer (FADH2 T<>T) kinetics in Anacystis nidulans photolyase. Biochemistry 31 (1992) 11244-11248
    • (1992) Biochemistry , vol.31 , pp. 11244-11248
    • Kim, S.-T.1    Heelis, P.F.2    Sancar, A.3
  • 26
    • 9944229136 scopus 로고    scopus 로고
    • Femtosecond dynamics of DNA photolyase: energy transfer of antenna initiation and electron transfer of cofactor reduction
    • Saxena C., Sancar A., and Zhong D. Femtosecond dynamics of DNA photolyase: energy transfer of antenna initiation and electron transfer of cofactor reduction. J. Phys. Chem. B 108 (2004) 18026-18033
    • (2004) J. Phys. Chem. B , vol.108 , pp. 18026-18033
    • Saxena, C.1    Sancar, A.2    Zhong, D.3
  • 27
    • 20444366979 scopus 로고    scopus 로고
    • Ultrafast dynamics of resonance energy transfer in cryptochrome
    • Saxena C., Wang H., Kavakli I.H., Sancar A., and Zhong D. Ultrafast dynamics of resonance energy transfer in cryptochrome. J. Am. Chem. Soc. 127 (2005) 7984-7985
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 7984-7985
    • Saxena, C.1    Wang, H.2    Kavakli, I.H.3    Sancar, A.4    Zhong, D.5
  • 28
    • 0024121590 scopus 로고
    • Identification of the second chromophore of Escherichia coli and yeast DNA photolyases as 5,10-methenyltetrahydrofolate
    • Johnson J.L., Hamm-Alvarez S., Payne G., Sancar G.B., Rajagopalan K.V., and Sancar A. Identification of the second chromophore of Escherichia coli and yeast DNA photolyases as 5,10-methenyltetrahydrofolate. Proc. Natl. Acad. Sci. USA 85 (1988) 2046-2050
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2046-2050
    • Johnson, J.L.1    Hamm-Alvarez, S.2    Payne, G.3    Sancar, G.B.4    Rajagopalan, K.V.5    Sancar, A.6
  • 29
    • 0025272139 scopus 로고
    • DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans
    • Eker A.P.M., Kooiman P., Hessels J.K.C., and Yasui A. DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans. J. Biol. Chem. 265 (1990) 8009-8015
    • (1990) J. Biol. Chem. , vol.265 , pp. 8009-8015
    • Eker, A.P.M.1    Kooiman, P.2    Hessels, J.K.C.3    Yasui, A.4
  • 31
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace C.N., Vajdos F., Fee L., Grimsley G., and Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4 (1995) 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 32
    • 0015881843 scopus 로고
    • A rapid micromethod for determination of FMN and FAD in mixtures
    • Faeder E.J., and Siegel L.M. A rapid micromethod for determination of FMN and FAD in mixtures. Anal. Biochem. 53 (1973) 332-336
    • (1973) Anal. Biochem. , vol.53 , pp. 332-336
    • Faeder, E.J.1    Siegel, L.M.2
  • 34
    • 0035909815 scopus 로고    scopus 로고
    • Evidence of powerful substrate electric fields in DNA photolyase: implications for thymidine dimer repair
    • MacFarlane IV A.W., and Stanley R.J. Evidence of powerful substrate electric fields in DNA photolyase: implications for thymidine dimer repair. Biochemistry 40 (2001) 15203-15214
    • (2001) Biochemistry , vol.40 , pp. 15203-15214
    • MacFarlane IV, A.W.1    Stanley, R.J.2
  • 35
    • 0027990435 scopus 로고
    • Characterization of a medium wavelength type DNA photolyase: purification and properties of photolyase from Bacillus firmus
    • Malhotra K., Kim S.-T., and Sancar A. Characterization of a medium wavelength type DNA photolyase: purification and properties of photolyase from Bacillus firmus. Biochemistry 33 (1994) 8712-8718
    • (1994) Biochemistry , vol.33 , pp. 8712-8718
    • Malhotra, K.1    Kim, S.-T.2    Sancar, A.3
  • 36
    • 0141531996 scopus 로고    scopus 로고
    • Purification and characterization of three members of the photolyase/cryptochrome family blue-light photoreceptors from Vibrio cholerae
    • Worthington E.N., Kavakli I.H., Berrocal-Tito G., Bondo B.E., and Sancar A. Purification and characterization of three members of the photolyase/cryptochrome family blue-light photoreceptors from Vibrio cholerae. J. Biol. Chem. 278 (2003) 39143-39154
    • (2003) J. Biol. Chem. , vol.278 , pp. 39143-39154
    • Worthington, E.N.1    Kavakli, I.H.2    Berrocal-Tito, G.3    Bondo, B.E.4    Sancar, A.5
  • 37
    • 0023661050 scopus 로고
    • DNA repair catalyzed by Escherichia coli DNA photolyase containing only reduced flavin: elimination of the enzyme's second chromophore by reduction with sodium borohydride
    • Jorns M.S., Wang B., and Jordan S.P. DNA repair catalyzed by Escherichia coli DNA photolyase containing only reduced flavin: elimination of the enzyme's second chromophore by reduction with sodium borohydride. Biochemistry 26 (1987) 6810-6816
    • (1987) Biochemistry , vol.26 , pp. 6810-6816
    • Jorns, M.S.1    Wang, B.2    Jordan, S.P.3
  • 38
    • 0024364027 scopus 로고
    • Role of enzyme-bound 5, 10-methenyltetrahydropteroylpolyglutamate in catalysis by Escherichia coli DNA photolyase
    • Hamm-Alvarez S., Sancar A., and Rajagopalan K.V. Role of enzyme-bound 5, 10-methenyltetrahydropteroylpolyglutamate in catalysis by Escherichia coli DNA photolyase. J. Biol. Chem. 264 (1989) 9649-9656
    • (1989) J. Biol. Chem. , vol.264 , pp. 9649-9656
    • Hamm-Alvarez, S.1    Sancar, A.2    Rajagopalan, K.V.3
  • 39
    • 34250346126 scopus 로고    scopus 로고
    • A novel photoreaction mechanism for the circadian blue light photoreceptor Drosophila cryptochrome
    • Berndt A., Kottke T., Breitkreuz H., Dvorsky R., Hennig S., Alexander M., and Wolf E. A novel photoreaction mechanism for the circadian blue light photoreceptor Drosophila cryptochrome. J. Biol. Chem. 282 (2007) 13011-13021
    • (2007) J. Biol. Chem. , vol.282 , pp. 13011-13021
    • Berndt, A.1    Kottke, T.2    Breitkreuz, H.3    Dvorsky, R.4    Hennig, S.5    Alexander, M.6    Wolf, E.7
  • 40
    • 50149098153 scopus 로고    scopus 로고
    • Absorption and fluorescence spectroscopic characterisation of the circadian blue-light photoreceptor cryptochrome from Drosophila melanogaster (dCry)
    • Shirdel J., Zirak P., Penzkofer A., Breitkreuz H., and Wolf E. Absorption and fluorescence spectroscopic characterisation of the circadian blue-light photoreceptor cryptochrome from Drosophila melanogaster (dCry). Chem. Phys. 352 (2008) 35-47
    • (2008) Chem. Phys. , vol.352 , pp. 35-47
    • Shirdel, J.1    Zirak, P.2    Penzkofer, A.3    Breitkreuz, H.4    Wolf, E.5
  • 41
    • 0015951494 scopus 로고
    • Fluorescence and optical characteristics of reduced flavines and flavoproteins
    • Ghisla S., Massey V., Lhoste J.-M., and Mayhew S.G. Fluorescence and optical characteristics of reduced flavines and flavoproteins. Biochemistry 13 (1974) 589-597
    • (1974) Biochemistry , vol.13 , pp. 589-597
    • Ghisla, S.1    Massey, V.2    Lhoste, J.-M.3    Mayhew, S.G.4
  • 43
    • 0023643412 scopus 로고
    • The active form of Escherichia coli DNA photolyase contains a fully reduced flavin and not a flavin radical, both in vivo and in vitro
    • Payne G., Heelis P.F., Rohrs B.R., and Sancar A. The active form of Escherichia coli DNA photolyase contains a fully reduced flavin and not a flavin radical, both in vivo and in vitro. Biochemistry 26 (1987) 7121-7127
    • (1987) Biochemistry , vol.26 , pp. 7121-7127
    • Payne, G.1    Heelis, P.F.2    Rohrs, B.R.3    Sancar, A.4
  • 44
    • 33846596542 scopus 로고    scopus 로고
    • Cryptochrome 3 from Arabidopsis thaliana: structural and functional analysis of its complex with a folate light antenna
    • Klar T., Pokorny R., Moldt J., Batschauer A., and Essen L.-O. Cryptochrome 3 from Arabidopsis thaliana: structural and functional analysis of its complex with a folate light antenna. J. Mol. Biol. 366 (2007) 954-964
    • (2007) J. Mol. Biol. , vol.366 , pp. 954-964
    • Klar, T.1    Pokorny, R.2    Moldt, J.3    Batschauer, A.4    Essen, L.-O.5
  • 45
    • 0015497790 scopus 로고
    • Molecular luminescence studies of flavins. I. Excited states of flavins
    • Sun M., Song P.S., and Moore T.A. Molecular luminescence studies of flavins. I. Excited states of flavins. J. Am. Chem. Soc. 94 (1972) 1730-1740
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 1730-1740
    • Sun, M.1    Song, P.S.2    Moore, T.A.3
  • 46
    • 0015862373 scopus 로고
    • On the effect of temperature on the absorption spectra of free and protein-bound flavines
    • Mueller F., Mayhew S.G., and Massey V. On the effect of temperature on the absorption spectra of free and protein-bound flavines. Biochemistry 12 (1973) 4654-4662
    • (1973) Biochemistry , vol.12 , pp. 4654-4662
    • Mueller, F.1    Mayhew, S.G.2    Massey, V.3
  • 47
    • 0018855280 scopus 로고
    • Effect of hydrogen bonding on electronic spectra and reactivity of flavins
    • Yagi K., Ohishi N., Nishimoto K., Choi J.D., and Song P.-S. Effect of hydrogen bonding on electronic spectra and reactivity of flavins. Biochemistry 19 (1980) 1553-1557
    • (1980) Biochemistry , vol.19 , pp. 1553-1557
    • Yagi, K.1    Ohishi, N.2    Nishimoto, K.3    Choi, J.D.4    Song, P.-S.5
  • 48
    • 0033545878 scopus 로고    scopus 로고
    • Intraprotein electron transfer between tyrosine and tryptophan in DNA photolyase from Anacystis nidulans
    • Aubert C., Mathis P., Eker A.P.M., and Brettel K. Intraprotein electron transfer between tyrosine and tryptophan in DNA photolyase from Anacystis nidulans. Proc. Natl. Acad. Sci. USA 96 (1999) 5423-5427
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5423-5427
    • Aubert, C.1    Mathis, P.2    Eker, A.P.M.3    Brettel, K.4
  • 49
    • 0034214080 scopus 로고    scopus 로고
    • Intraprotein radical transfer during photoactivation of DNA photolyase
    • Aubert C., Vos M.H., Mathis P., Eker A.P.M., and Brettel K. Intraprotein radical transfer during photoactivation of DNA photolyase. Nature 405 (2000) 586-590
    • (2000) Nature , vol.405 , pp. 586-590
    • Aubert, C.1    Vos, M.H.2    Mathis, P.3    Eker, A.P.M.4    Brettel, K.5
  • 50
    • 0038024617 scopus 로고    scopus 로고
    • Light-induced electron transfer in a cryptochrome blue-light photoreceptor
    • Giovani B., Byrdin M., Ahmad M., and Brettel K. Light-induced electron transfer in a cryptochrome blue-light photoreceptor. Nat. Struct. Biol. 10 (2003) 489-490
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 489-490
    • Giovani, B.1    Byrdin, M.2    Ahmad, M.3    Brettel, K.4
  • 51
    • 1942536615 scopus 로고    scopus 로고
    • Intraprotein electron transfer and proton dynamics during photoactivation of DNA photolyase from E. coli: review and new insight from an "inverse" deuterium isotope effect
    • Byrdin M., Sartor V., Eker A.P.M., Vos M.H., Aubert C., Brettel K., and Mathis P. Intraprotein electron transfer and proton dynamics during photoactivation of DNA photolyase from E. coli: review and new insight from an "inverse" deuterium isotope effect. Biochim. Biophys. Acta 1655 (2004) 64-70
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 64-70
    • Byrdin, M.1    Sartor, V.2    Eker, A.P.M.3    Vos, M.H.4    Aubert, C.5    Brettel, K.6    Mathis, P.7
  • 52
    • 21244502156 scopus 로고    scopus 로고
    • Light-induced electron transfer in Arabidopsis cryptochrome-1 correlates with in vivo function
    • Zeugner A., Byrdin M., Bouly J.-P., Bakrim N., Giovani B., Brettel K., and Ahmad M. Light-induced electron transfer in Arabidopsis cryptochrome-1 correlates with in vivo function. J. Biol. Chem. 280 (2005) 19437-19440
    • (2005) J. Biol. Chem. , vol.280 , pp. 19437-19440
    • Zeugner, A.1    Byrdin, M.2    Bouly, J.-P.3    Bakrim, N.4    Giovani, B.5    Brettel, K.6    Ahmad, M.7
  • 53
    • 33748526475 scopus 로고    scopus 로고
    • Role of the middle residue in the triple tryptophan electron transfer chain of DNA photolyase: ultrafast spectroscopy of a Trp → Phe mutant
    • Lukacs A., Eker A.P.M., Byrdin M., Villette S., Pan J., Brettel K., and Vos M.H. Role of the middle residue in the triple tryptophan electron transfer chain of DNA photolyase: ultrafast spectroscopy of a Trp → Phe mutant. J. Phys. Chem. B 110 (2006) 15654-15658
    • (2006) J. Phys. Chem. B , vol.110 , pp. 15654-15658
    • Lukacs, A.1    Eker, A.P.M.2    Byrdin, M.3    Villette, S.4    Pan, J.5    Brettel, K.6    Vos, M.H.7
  • 54
    • 34548505502 scopus 로고    scopus 로고
    • Observation of an intermediate tryptophanyl radical in W306F mutant DNA photolyase from Escherichia coli supports electron hopping along the triple tryptophan chain
    • Byrdin M., Villette S., Eker A.P.M., and Brettel K. Observation of an intermediate tryptophanyl radical in W306F mutant DNA photolyase from Escherichia coli supports electron hopping along the triple tryptophan chain. Biochemistry 46 (2007) 10072-10077
    • (2007) Biochemistry , vol.46 , pp. 10072-10077
    • Byrdin, M.1    Villette, S.2    Eker, A.P.M.3    Brettel, K.4
  • 55
    • 55549100984 scopus 로고    scopus 로고
    • Electron hopping through the 15 Angström triple tryptophan molecular wire in DNA photolyase occurs within 30 ps
    • Lukacs A., Eker A.P.M., Byrdin M., Brettel K., and Vos M.H. Electron hopping through the 15 Angström triple tryptophan molecular wire in DNA photolyase occurs within 30 ps. J. Am. Chem. Soc. 130 (2008) 14394-14395
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14394-14395
    • Lukacs, A.1    Eker, A.P.M.2    Byrdin, M.3    Brettel, K.4    Vos, M.H.5
  • 56
    • 0023666973 scopus 로고
    • Photochemical properties of Escherichia coli DNA photolyase - selective photodecomposition of the 2nd chromophore
    • Heelis P.F., Payne G., and Sancar A. Photochemical properties of Escherichia coli DNA photolyase - selective photodecomposition of the 2nd chromophore. Biochemistry 26 (1987) 4634-4640
    • (1987) Biochemistry , vol.26 , pp. 4634-4640
    • Heelis, P.F.1    Payne, G.2    Sancar, A.3
  • 58
    • 52149085899 scopus 로고    scopus 로고
    • Involvement of electron transfer in the photoreaction of zebrafish cryptochrome-DASH
    • Zikihara K., Ishikawa T., Todo T., and Tokutomi S. Involvement of electron transfer in the photoreaction of zebrafish cryptochrome-DASH. Photochem. Photobiol. 84 (2008) 1016-1023
    • (2008) Photochem. Photobiol. , vol.84 , pp. 1016-1023
    • Zikihara, K.1    Ishikawa, T.2    Todo, T.3    Tokutomi, S.4
  • 60
  • 61
    • 41249100106 scopus 로고    scopus 로고
    • Animal type 1 cryptochromes - analysis of the redox state of the flavin cofactor by site-directed mutagenesis
    • Ozturk N., Song S.-H., Selby C.P., and Sancar A. Animal type 1 cryptochromes - analysis of the redox state of the flavin cofactor by site-directed mutagenesis. J. Biol. Chem. 283 (2008) 3256-3263
    • (2008) J. Biol. Chem. , vol.283 , pp. 3256-3263
    • Ozturk, N.1    Song, S.-H.2    Selby, C.P.3    Sancar, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.