메뉴 건너뛰기




Volumn 97, Issue 2, 2009, Pages 94-108

Photocycle dynamics of the E149A mutant of cryptochrome 3 from Arabidopsis thaliana

Author keywords

Arabidopsis thaliana; Blue light photoreceptor; Cryptochrome cry3; Cryptochrome mutant; DNA photolyase, flavin adenine dinucleotide (FAD); FAD reduction and oxidation; Photo induced charge transfer; Photocycle dynamics

Indexed keywords

CRYPTOCHROME; CRYPTOCHROME 3; FLAVINE ADENINE NUCLEOTIDE; METHYLENETETRAHYDROFOLIC ACID; UNCLASSIFIED DRUG;

EID: 71749093646     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2009.08.005     Document Type: Article
Times cited : (14)

References (76)
  • 2
    • 84889429084 scopus 로고    scopus 로고
    • Briggs W.R., and Spudich J.L. (Eds), Wiley-VCH, Weinheim, Germany
    • In: Briggs W.R., and Spudich J.L. (Eds). Handbook of Photosensory Receptors (2005), Wiley-VCH, Weinheim, Germany
    • (2005) Handbook of Photosensory Receptors
  • 3
    • 84920143748 scopus 로고    scopus 로고
    • Schäfer E., and Nagy F. (Eds), Springer, Dordrecht, The Netherlands
    • In: Schäfer E., and Nagy F. (Eds). Photomorphogenesis in Plants and Bacteria. third ed. (2006), Springer, Dordrecht, The Netherlands
    • (2006) Photomorphogenesis in Plants and Bacteria. third ed.
  • 5
    • 32344444896 scopus 로고    scopus 로고
    • Photolyases and cryptochromes: common mechanisms of DNA repair and light-driven signalling?
    • Essen L.-O. Photolyases and cryptochromes: common mechanisms of DNA repair and light-driven signalling?. Curr. Opinion Struct. Biol. 16 (2006) 51-59
    • (2006) Curr. Opinion Struct. Biol. , vol.16 , pp. 51-59
    • Essen, L.-O.1
  • 6
    • 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. 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.4
  • 7
    • 34047220139 scopus 로고    scopus 로고
    • Insect cryptochromes: gene duplication and loss define diverse ways to construct insect circadian clocks
    • Yuan Q., Metterville D., Briscoe A.D., and Reppert S.M. Insect cryptochromes: gene duplication and loss define diverse ways to construct insect circadian clocks. Mol. Biol. Evol. 24 (2007) 948-955
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 948-955
    • Yuan, Q.1    Metterville, D.2    Briscoe, A.D.3    Reppert, S.M.4
  • 8
    • 0027493250 scopus 로고
    • HY4 gene of A. thaliana encodes a protein with characteristics of a blue-light photoreceptor
    • Ahmad M., and Cashmore A.R. HY4 gene of A. thaliana encodes a protein with characteristics of a blue-light photoreceptor. Nature 366 (1993) 162-166
    • (1993) Nature , vol.366 , pp. 162-166
    • Ahmad, M.1    Cashmore, A.R.2
  • 9
    • 0032570771 scopus 로고    scopus 로고
    • Regulation of flowering time by Arabidopsis photoreceptors
    • Guo H., Yang H., and Mockler T.C. Regulation of flowering time by Arabidopsis photoreceptors. C. Lin, Science 279 (1998) 1360-1363
    • (1998) C. Lin, Science , vol.279 , pp. 1360-1363
    • Guo, H.1    Yang, H.2    Mockler, T.C.3
  • 10
    • 0037452591 scopus 로고    scopus 로고
    • Regulation of photoperiodic flowering by Arabidopsis photoreceptors
    • Mockler T., Yang H., Yu X., Parikh D., Cheng Y.C., Dolan S., and Lin C. Regulation of photoperiodic flowering by Arabidopsis photoreceptors. PNAS 100 (2003) 2140-2145
    • (2003) PNAS , vol.100 , pp. 2140-2145
    • Mockler, T.1    Yang, H.2    Yu, X.3    Parikh, D.4    Cheng, Y.C.5    Dolan, S.6    Lin, C.7
  • 11
    • 0037629260 scopus 로고    scopus 로고
    • An Arabidopsis protein closely related to Synechocystis cryptochrome is targeted to organelles
    • Kleine T., Lockhart P., and Batschauer A. An Arabidopsis protein closely related to Synechocystis cryptochrome is targeted to organelles. Plant J. 35 (2003) 93-103
    • (2003) Plant J. , vol.35 , pp. 93-103
    • Kleine, T.1    Lockhart, P.2    Batschauer, A.3
  • 13
    • 0141531996 scopus 로고    scopus 로고
    • Purification and characterizationof 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 characterizationof three members of the photolyase/cryptochrome family blue-light photoreceptors from Vibrio cholerae. J. Biol. Chem. 278 (2003) 39143
    • (2003) J. Biol. Chem. , vol.278 , pp. 39143
    • Worthington, E.N.1    Kavakli, I.H.2    Berrocal-Tito, G.3    Bondo, B.E.4    Sancar, A.5
  • 15
    • 33750713440 scopus 로고    scopus 로고
    • A cryptochrome/photolyase class of enzymes with single-stranded DNA-specific photolyase activity
    • Selby C.P., and Sancar A. A cryptochrome/photolyase class of enzymes with single-stranded DNA-specific photolyase activity. PNAS 103 (2006) 17696-17700
    • (2006) PNAS , vol.103 , pp. 17696-17700
    • Selby, C.P.1    Sancar, A.2
  • 16
    • 58549111388 scopus 로고    scopus 로고
    • Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome
    • Pokorny R., Klar T., Hennecke U., Carell T., Batschauer A., and Essen L.-O. Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome. PNAS 105 (2008) 21023-21027
    • (2008) PNAS , vol.105 , pp. 21023-21027
    • Pokorny, R.1    Klar, T.2    Hennecke, U.3    Carell, T.4    Batschauer, A.5    Essen, L.-O.6
  • 17
    • 0034038064 scopus 로고    scopus 로고
    • A model for photoreceptor-based magnetoreception in birds
    • Ritz T., Adem S., and Schulten K. A model for photoreceptor-based magnetoreception in birds. Biophys. J. 78 (2000) 707-718
    • (2000) Biophys. J. , vol.78 , pp. 707-718
    • Ritz, T.1    Adem, S.2    Schulten, K.3
  • 18
    • 34147174257 scopus 로고    scopus 로고
    • Magnetic field effects in Arabidopsis thaliana cryptochrome-1
    • Solo'yov I.A., Chandler D.E., and Schulten K. Magnetic field effects in Arabidopsis thaliana cryptochrome-1. Biophys. J. 92 (2007) 2711-2726
    • (2007) Biophys. J. , vol.92 , pp. 2711-2726
    • Solo'yov, I.A.1    Chandler, D.E.2    Schulten, K.3
  • 19
    • 33846821969 scopus 로고    scopus 로고
    • Magnetic intensity affects cryptochrome-dependent responses in Arabidopsis thaliana
    • Ahmad M., Galland P., Ritz T., Wiltschko R., and Wiltschko W. Magnetic intensity affects cryptochrome-dependent responses in Arabidopsis thaliana. Planta 225 (2006) 615-624
    • (2006) Planta , vol.225 , pp. 615-624
    • Ahmad, M.1    Galland, P.2    Ritz, T.3    Wiltschko, R.4    Wiltschko, W.5
  • 20
    • 50049118298 scopus 로고    scopus 로고
    • Cryptochrome mediates light-dependent magnetosensitivity in Drosophila
    • Gegear R.J., Casselman A., Waddell S., and Reppert S.M. Cryptochrome mediates light-dependent magnetosensitivity in Drosophila. Nature 454 (2008) 1014-1019
    • (2008) Nature , vol.454 , pp. 1014-1019
    • Gegear, R.J.1    Casselman, A.2    Waddell, S.3    Reppert, S.M.4
  • 22
    • 0029857950 scopus 로고    scopus 로고
    • At-PHH1, a novel gene from Arabidopsis thaliana related to microbial photolyases and plant blue light photoreceptors
    • Hoffman P.D., Batschauer A., and Hays J.B. At-PHH1, a novel gene from Arabidopsis thaliana related to microbial photolyases and plant blue light photoreceptors. Mol. Gen. Genet. 253 (1996) 259-265
    • (1996) Mol. Gen. Genet. , vol.253 , pp. 259-265
    • Hoffman, P.D.1    Batschauer, A.2    Hays, J.B.3
  • 23
    • 0036275942 scopus 로고    scopus 로고
    • Blue light receptors and signal transduction
    • Lin C. Blue light receptors and signal transduction. Plant Cell 14 Suppl. (2002) S207-S225
    • (2002) Plant Cell , vol.14 , Issue.SUPPL
    • Lin, C.1
  • 24
    • 0032570771 scopus 로고    scopus 로고
    • Regulation of flowering time by Arabidopsis photoreceptors
    • Guo H., Yang H., Mockler T.C., and Lin C. Regulation of flowering time by Arabidopsis photoreceptors. Science 279 (1998) 1360-1363
    • (1998) Science , vol.279 , pp. 1360-1363
    • Guo, H.1    Yang, H.2    Mockler, T.C.3    Lin, C.4
  • 25
    • 32344435000 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of cryptochrome 3 from Arabidopsis thaliana
    • Pokorny R., Klar T., Essen L.-O., and Batschauer A. Crystallization and preliminary X-ray analysis of cryptochrome 3 from Arabidopsis thaliana. Acta Crystallogr. F 61 (2005) 935-938
    • (2005) Acta Crystallogr. F , vol.61 , pp. 935-938
    • Pokorny, R.1    Klar, T.2    Essen, L.-O.3    Batschauer, A.4
  • 26
    • 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
  • 27
    • 33845189961 scopus 로고    scopus 로고
    • Crystal structure of cryptochrome 3 from Arabidopsis thaliana and its implications for photolyase activity
    • Huang Y., Baxter R., Smith B.S., Partch C.L., Colbert C.L., and Deisenhofer J. Crystal structure of cryptochrome 3 from Arabidopsis thaliana and its implications for photolyase activity. PNAS 103 (2006) 17701-17706
    • (2006) PNAS , vol.103 , pp. 17701-17706
    • Huang, Y.1    Baxter, R.2    Smith, B.S.3    Partch, C.L.4    Colbert, C.L.5    Deisenhofer, J.6
  • 28
    • 4544302622 scopus 로고    scopus 로고
    • Preliminary characterization of light harvesting in E. coli DNA photolyase
    • Henry A.A., Jimenez R., Hanway D., and Romesberg F.E. Preliminary characterization of light harvesting in E. coli DNA photolyase. ChemBioChem. 5 (2004) 1088-1094
    • (2004) ChemBioChem. , vol.5 , pp. 1088-1094
    • Henry, A.A.1    Jimenez, R.2    Hanway, D.3    Romesberg, F.E.4
  • 30
    • 0023342489 scopus 로고
    • Fluorescence behaviour of highly concentrated rhodamine 6G solutions
    • Penzkofer A., and Leupacher W. Fluorescence behaviour of highly concentrated rhodamine 6G solutions. J. Luminesc. 37 (1987) 61-72
    • (1987) J. Luminesc. , vol.37 , pp. 61-72
    • Penzkofer, A.1    Leupacher, W.2
  • 31
    • 0033442448 scopus 로고    scopus 로고
    • Fluorescence spectroscopic behaviour of neat and blended conjugated polymer thin films
    • Holzer W., Pichlmaier M., Penzkofer A., Bradley D.D.C., and Blau W.J. Fluorescence spectroscopic behaviour of neat and blended conjugated polymer thin films. Chem. Phys. 246 (1999) 445-462
    • (1999) Chem. Phys. , vol.246 , pp. 445-462
    • Holzer, W.1    Pichlmaier, M.2    Penzkofer, A.3    Bradley, D.D.C.4    Blau, W.J.5
  • 34
    • 0025555047 scopus 로고
    • Compression of picosecond light pulses of a hybridly mode-locked pulsed Nd:glass laser
    • Scheidler W., and Penzkofer A. Compression of picosecond light pulses of a hybridly mode-locked pulsed Nd:glass laser. Opt. Commun. 80 (1990) 127-132
    • (1990) Opt. Commun. , vol.80 , pp. 127-132
    • Scheidler, W.1    Penzkofer, A.2
  • 36
    • 62149101427 scopus 로고    scopus 로고
    • Photo-dynamics of roseoflavin and riboflavin in aqueous and organic solvents
    • Zirak P., Penzkofer A., Mathes T., and Hegemann P. Photo-dynamics of roseoflavin and riboflavin in aqueous and organic solvents. Chem. Phys. 358 (2009) 111-122
    • (2009) Chem. Phys. , vol.358 , pp. 111-122
    • Zirak, P.1    Penzkofer, A.2    Mathes, T.3    Hegemann, P.4
  • 37
    • 36349010704 scopus 로고    scopus 로고
    • Protein aggregation studied by forward light scattering and light transmission analysis
    • Penzkofer A., Shirdel J., Zirak P., Breitkreuz H., and Wolf E. Protein aggregation studied by forward light scattering and light transmission analysis. Chem. Phys. 342 (2007) 55-63
    • (2007) Chem. Phys. , vol.342 , pp. 55-63
    • Penzkofer, A.1    Shirdel, J.2    Zirak, P.3    Breitkreuz, H.4    Wolf, E.5
  • 38
    • 1042267420 scopus 로고    scopus 로고
    • Fluorescence quenching of flavin adenine dinucleotide in aqueous solution by pH dependent isomerisation and photo-induced electron transfer
    • Islam Sh.D.M., Susdorf T., Penzkofer A., and Hegemann P. Fluorescence quenching of flavin adenine dinucleotide in aqueous solution by pH dependent isomerisation and photo-induced electron transfer. Chem. Phys. 295 (2003) 139-151
    • (2003) Chem. Phys. , vol.295 , pp. 139-151
    • Islam, Sh.D.M.1    Susdorf, T.2    Penzkofer, A.3    Hegemann, P.4
  • 41
    • 0000986142 scopus 로고
    • Fluorescence of riboflavin, flavin adenine dinucleotide
    • Weber G. Fluorescence of riboflavin, flavin adenine dinucleotide. J. Biochem. 47 (1950) 114-121
    • (1950) J. Biochem. , vol.47 , pp. 114-121
    • Weber, G.1
  • 42
    • 0016286777 scopus 로고
    • Time-resolved fluorescence of flavin adenine dinucleotide
    • Wahl Ph., Auchet J.C., Visser A.J.W.G., and Müller F. Time-resolved fluorescence of flavin adenine dinucleotide. FEBS Lett. 44 (1974) 67-70
    • (1974) FEBS Lett. , vol.44 , pp. 67-70
    • Wahl, Ph.1    Auchet, J.C.2    Visser, A.J.W.G.3    Müller, F.4
  • 43
    • 0021668461 scopus 로고
    • Kinetics of stacking interactions in flavin adenine dinucleotide from time-resolved flavin fluorescence
    • Visser A.J.W.G. Kinetics of stacking interactions in flavin adenine dinucleotide from time-resolved flavin fluorescence. Photochem. Photobiol. 40 (1984) 703-706
    • (1984) Photochem. Photobiol. , vol.40 , pp. 703-706
    • Visser, A.J.W.G.1
  • 44
    • 0037194931 scopus 로고    scopus 로고
    • Dynamic conformations of flavin adenine dinucleotide: simulated molecular dynamics of the flavin cofactor related to the time-resolved fluorescence characteristics
    • van den Berg P.A.W., Feenstra K.A., Mark A.E., Berendsen H.J.C., and Visser A.J.W.G. Dynamic conformations of flavin adenine dinucleotide: simulated molecular dynamics of the flavin cofactor related to the time-resolved fluorescence characteristics. J. Phys. Chem. B 106 (2002) 8858-8869
    • (2002) J. Phys. Chem. B , vol.106 , pp. 8858-8869
    • van den Berg, P.A.W.1    Feenstra, K.A.2    Mark, A.E.3    Berendsen, H.J.C.4    Visser, A.J.W.G.5
  • 45
    • 0037106098 scopus 로고    scopus 로고
    • pH dependence of the absorption and emission behaviour of riboflavin in aqueous solution
    • Drössler P., Holzer W., Penzkofer A., and Hegemann P. pH dependence of the absorption and emission behaviour of riboflavin in aqueous solution. Chem. Phys. 282 (2002) 429-439
    • (2002) Chem. Phys. , vol.282 , pp. 429-439
    • Drössler, P.1    Holzer, W.2    Penzkofer, A.3    Hegemann, P.4
  • 46
    • 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
  • 48
    • 0141993723 scopus 로고    scopus 로고
    • The motions of an enzyme soloist
    • Orrit M. The motions of an enzyme soloist. Science 302 (2003) 239-240
    • (2003) Science , vol.302 , pp. 239-240
    • Orrit, M.1
  • 49
    • 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
  • 50
    • 55549100984 scopus 로고    scopus 로고
    • Electron hopping through the 15 Å 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 Å 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
  • 51
    • 34250864953 scopus 로고    scopus 로고
    • Absorption and fluorescence spectroscopic characterisation of a phenothiazine-flavin dyad
    • Shirdel J., Penzkofer A., Procházka R., Shen Z., and Daub J. Absorption and fluorescence spectroscopic characterisation of a phenothiazine-flavin dyad. Chem. Phys. 336 (2007) 1-13
    • (2007) Chem. Phys. , vol.336 , pp. 1-13
    • Shirdel, J.1    Penzkofer, A.2    Procházka, R.3    Shen, Z.4    Daub, J.5
  • 52
    • 0034245626 scopus 로고    scopus 로고
    • Ultrafast excited state dynamics of oxidized flavins: direct obervations of quenching by purines
    • Stanley R.J., and Macfarlane IV A.W. Ultrafast excited state dynamics of oxidized flavins: direct obervations of quenching by purines. J. Phys. Chem. A 104 (2000) 6899-6906
    • (2000) J. Phys. Chem. A , vol.104 , pp. 6899-6906
    • Stanley, R.J.1    Macfarlane IV, A.W.2
  • 54
    • 0006579490 scopus 로고
    • Ionization potentials and donor properties of nucleic acid bases and related compounds
    • Hush N.S., and Cheung A.S. Ionization potentials and donor properties of nucleic acid bases and related compounds. Chem. Phys. Lett. 34 (1975) 11
    • (1975) Chem. Phys. Lett. , vol.34 , pp. 11
    • Hush, N.S.1    Cheung, A.S.2
  • 55
    • 0016998170 scopus 로고
    • Ultraviolet photoelectron studies of biological purines: the valence electronic structure of adenine
    • Peng S., Padva A., and Le Breton P.R. Ultraviolet photoelectron studies of biological purines: the valence electronic structure of adenine. PNAS 73 (1976) 2966
    • (1976) PNAS , vol.73 , pp. 2966
    • Peng, S.1    Padva, A.2    Le Breton, P.R.3
  • 56
    • 84987154502 scopus 로고
    • Ab initio study of a purine nucleoside-adenosine
    • Kwiatkowski J.S., and Pullman B. Ab initio study of a purine nucleoside-adenosine. Int. J. Quant. Chem. 15 (1979) 499-510
    • (1979) Int. J. Quant. Chem. , vol.15 , pp. 499-510
    • Kwiatkowski, J.S.1    Pullman, B.2
  • 58
    • 84961985239 scopus 로고    scopus 로고
    • Ab initio study on electron excitation and electron transfer in tryptophan-tyrosine system
    • Tong J., and Li X.-Y. Ab initio study on electron excitation and electron transfer in tryptophan-tyrosine system. Chem. Phys. 284 (2002) 543-554
    • (2002) Chem. Phys. , vol.284 , pp. 543-554
    • Tong, J.1    Li, X.-Y.2
  • 59
    • 84995072709 scopus 로고
    • On the photoionization energy threshold of tryptophan in aqueous solutions
    • Amouyal E., Bernas A., and Grand G. On the photoionization energy threshold of tryptophan in aqueous solutions. Photochem. Photobiol. 29 (1979) 1071-1077
    • (1979) Photochem. Photobiol. , vol.29 , pp. 1071-1077
    • Amouyal, E.1    Bernas, A.2    Grand, G.3
  • 60
    • 0014743497 scopus 로고
    • Excitation of tryptophan in solution during irradiation with X-rays and UV light between 77 K and 300 K
    • Steen H.B. Excitation of tryptophan in solution during irradiation with X-rays and UV light between 77 K and 300 K. Radiation Research 41 (1970) 268-287
    • (1970) Radiation Research , vol.41 , pp. 268-287
    • Steen, H.B.1
  • 61
    • 0001762121 scopus 로고
    • Photo-oxidation of tryptophan sensitized by methylene blue
    • Smith G.J. Photo-oxidation of tryptophan sensitized by methylene blue. J. Chem. Soc. Faraday Trans. II 74 (1978) 1350-1354
    • (1978) J. Chem. Soc. Faraday Trans. II , vol.74 , pp. 1350-1354
    • Smith, G.J.1
  • 63
    • 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. Blue-light-induced changes in Arabidopsis cryptochrome 1 probed by FTIR difference spectroscopy. Biochem. 45 (2006) 2472-2479
    • (2006) Biochem. , vol.45 , pp. 2472-2479
    • Kottke, T.1    Batschauer, A.2    Ahmad, M.3    Heberle, J.4
  • 67
    • 34547592093 scopus 로고    scopus 로고
    • Blue light induces radical formation and autophosphorylation in the light-sensitive domain of Chlamydomonas cryptochrome
    • Immeln D., Schlesinger R., Heberle J., and Kottke T. Blue light induces radical formation and autophosphorylation in the light-sensitive domain of Chlamydomonas cryptochrome. J. Biol. Chem. 282 (2007) 21720-21728
    • (2007) J. Biol. Chem. , vol.282 , pp. 21720-21728
    • Immeln, D.1    Schlesinger, R.2    Heberle, J.3    Kottke, T.4
  • 68
    • 71749088032 scopus 로고    scopus 로고
    • private communication
    • T, Kottke, private communication.
    • Kottke, T.1
  • 69
    • 20444366979 scopus 로고    scopus 로고
    • Ultrafast dynamics of resonance energy transfer in cryptochrome
    • Saxena C., Wang H., Kavakli 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, H.3    Sancar, A.4    Zhong, D.5
  • 70
    • 45249083827 scopus 로고    scopus 로고
    • Ultrafast dynamics and anionic active states of the flavin cofactor in cryptochrome and photolyase
    • Kao Y.-T., Tan C., Song S.-H., Öztürk N., Li J., Wang L., Sancar A., and Zhong D. Ultrafast dynamics and anionic active states of the flavin cofactor in cryptochrome and photolyase. J. Am. Chem. Soc. 130 (2008) 7695-7701
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 7695-7701
    • Kao, Y.-T.1    Tan, C.2    Song, S.-H.3    Öztürk, N.4    Li, J.5    Wang, L.6    Sancar, A.7    Zhong, D.8
  • 71
    • 41249100106 scopus 로고    scopus 로고
    • Animal type 1 cryptochromes. Analysis of the redox state of the flavin cofactor by site directed mutagenesis
    • Öztürk 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
    • Öztürk, N.1    Song, S.-H.2    Selby, C.P.3    Sancar, A.4
  • 73
    • 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. Biochem. 26 (1987) 6810-6816
    • (1987) Biochem. , vol.26 , pp. 6810-6816
    • Jorns, M.S.1    Wang, B.2    Jordan, S.P.3
  • 74
    • 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
  • 75
    • 33847360030 scopus 로고    scopus 로고
    • Photo-reduction of flavin mononucleotide to semiquinone form in LOV domain mutants of blue-light receptor phot from Chlamydomonas reinhardtii
    • Song S.-H., Dick B., Penzkofer A., and Hegemann P. Photo-reduction of flavin mononucleotide to semiquinone form in LOV domain mutants of blue-light receptor phot from Chlamydomonas reinhardtii. J. Photochem. Photobiol. 87 (2007) 37-48
    • (2007) J. Photochem. Photobiol. , vol.87 , pp. 37-48
    • Song, S.-H.1    Dick, B.2    Penzkofer, A.3    Hegemann, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.