메뉴 건너뛰기




Volumn 48, Issue 48, 2009, Pages 11399-11411

Kinetic stability of the flavin semiquinone in photolyase and cryptochrome-DASH

Author keywords

[No Author keywords available]

Indexed keywords

BINDING POCKETS; CELLULAR PROCESS; CIRCADIAN RHYTHMS; COFACTORS; CRYPTOCHROMES; CYCLOBUTANE PYRIMIDINE DIMERS; ELECTRON TRANSFER; FUNCTIONAL DIVERSITY; HUMAN HEALTH; KINETIC MECHANISM; KINETIC STABILITY; PHOTO-INDUCED ELECTRON TRANSFER; PHOTOLYASES; PLANT GROWTH; RATE LIMITING; REDOX PROPERTY; SEMIQUINONES; SYNECHOCYSTIS;

EID: 73149114186     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901371s     Document Type: Article
Times cited : (20)

References (64)
  • 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
    • 33744587947 scopus 로고    scopus 로고
    • The cryptochromes
    • Lin, C., and Todo, T. (2005) The cryptochromes. Genome Biol. 6, 220-229.
    • (2005) Genome Biol , vol.6 , pp. 220-229
    • Lin, C.1    Todo, T.2
  • 3
    • 0032493753 scopus 로고    scopus 로고
    • Evidence for Dinucleotide Flipping by DNA Photolyase
    • Vande Berg, B. J., and Sancar, G. B. (1998) Evidence for Dinucleotide Flipping by DNA Photolyase. J. Biol. Chem. 273, 20276-20284.
    • (1998) J. Biol. Chem , vol.273 , pp. 20276-20284
    • Vande Berg, B.J.1    Sancar, G.B.2
  • 4
    • 0037064082 scopus 로고    scopus 로고
    • Cyclobutylpyrimidine Dimer Base Flipping by DNA Photolyase
    • Christine, K. S., MacFarlane, A. W.IV, Yang, K., and Stanley, R. J. (2002) Cyclobutylpyrimidine Dimer Base Flipping by DNA Photolyase. J. Biol. Chem. 277, 38339-38344.
    • (2002) J. Biol. Chem , vol.277 , pp. 38339-38344
    • Christine, K.S.1    MacFarlane, A.W.I.2    Yang, K.3    Stanley, R.J.4
  • 5
    • 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. (2004) Crystal Structure of a Photolyase Bound to a CPD-Like DNA Lesion After in Situ Repair. Science 306, 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
  • 7
    • 0029061519 scopus 로고
    • Putative Blue-Light Photoreceptors from Arabidopsis thaliana and Sinapis alba with a High Degree of Sequence Homology to DNA Photolyase Contain the Two Photolyase Cofactors but Lack DNA Repair Activity
    • Malhotra, K., Kim, S.-T., Batschauer, A., Dawut, L., and Sancar, A. (1995) Putative Blue-Light Photoreceptors from Arabidopsis thaliana and Sinapis alba with a High Degree of Sequence Homology to DNA Photolyase Contain the Two Photolyase Cofactors but Lack DNA Repair Activity. Biochemistry 34, 6892-6899.
    • (1995) Biochemistry , vol.34 , pp. 6892-6899
    • Malhotra, K.1    Kim, S.-T.2    Batschauer, A.3    Dawut, L.4    Sancar, A.5
  • 8
    • 33750713440 scopus 로고    scopus 로고
    • A cryptochrome/photolyase class of enzymes with single-stranded DNA-specific photolyase activity
    • Selby, C. P., and Sancar, A. (2006) A cryptochrome/photolyase class of enzymes with single-stranded DNA-specific photolyase activity. Proc. Natl. Acad. Sci. U.S.A. 103, 17696-17700.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 17696-17700
    • Selby, C.P.1    Sancar, A.2
  • 10
    • 0141762747 scopus 로고    scopus 로고
    • Cryptochromes: Enabling Plants and Animals to Determine Circadian Time
    • Cashmore, A. R. (2003) Cryptochromes: Enabling Plants and Animals to Determine Circadian Time. Cell 114, 537-543.
    • (2003) Cell , vol.114 , pp. 537-543
    • Cashmore, A.R.1
  • 11
    • 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. (2007) Insect Cryptochromes: Gene Duplication and Loss Define Diverse Ways to Construct Insect Circadian Clocks. Mol. Biol. Evol. 24, 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
  • 12
    • 4544221643 scopus 로고    scopus 로고
    • Regulation of the Mammalian Circadian Clock by Cryptochrome
    • Sancar, A. (2004) Regulation of the Mammalian Circadian Clock by Cryptochrome. J. Biol. Chem. 279, 34079-34082.
    • (2004) J. Biol. Chem , vol.279 , pp. 34079-34082
    • Sancar, A.1
  • 13
    • 50049118298 scopus 로고    scopus 로고
    • Cryptochrome mediates light-dependent magnetosensitivity in Drosophila
    • Gegear, R. J., Casselman, A., Waddell, S., and Reppert, S. M. (2008) Cryptochrome mediates light-dependent magnetosensitivity in Drosophila. Nature 454, 1014-1018.
    • (2008) Nature , vol.454 , pp. 1014-1018
    • Gegear, R.J.1    Casselman, A.2    Waddell, S.3    Reppert, S.M.4
  • 15
    • 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.
    • (2000) Nucleic Acids Res , vol.28 , 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
  • 16
    • 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, Ì. H., Berrocal-Tito, G., Bondo, B. E., and Sancar, A. (2003) Purification and Characterization of Three Members of the Photolyase/Cryptochrome Family Blue-light Photoreceptors from Vibrio cholerae. J. Biol. Chem. 278, 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
  • 17
    • 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. (2008) Involvement of Electron Transfer in the Photoreaction of Zebrafish Cryptochrome-DASH. Photochem. Photobiol. 84, 1016-1023.
    • (2008) Photochem. Photobiol , vol.84 , pp. 1016-1023
    • Zikihara, K.1    Ishikawa, T.2    Todo, T.3    Tokutomi, S.4
  • 19
    • 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. (2007) Cryptochrome 3 from Arabidopsis thaliana: Structural and Functional Analysis of its Complex with a Folate Light Antenna. J. Mol. Biol. 366, 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
  • 20
    • 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. (2006) Crystal structure of cryptochrome 3 from Arabidopsis thaliana and its implications for photolyase activity. Proc. Natl. Acad. Sci. U.S.A. 103, 17701-17706.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , 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
  • 21
    • 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, T., and Essen, L.-O. (2008) Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome. Proc. Natl. Acad. Sci. U.S.A. 105, 21023-21027.
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 21023-21027
    • Pokorny, R.1    Klar, T.2    Hennecke, U.3    Carell, T.4    Batschauer, T.5    Essen, L.-O.6
  • 22
    • 0021755617 scopus 로고
    • Identification of a Neutral Flavin Radical and Characterization of a Second Chromophore in Escherichia coli DNA Photolyase
    • Jorns, M. S., Sancar, G. B., and Sancar, A. (1984) Identification of a Neutral Flavin Radical and Characterization of a Second Chromophore in Escherichia coli DNA Photolyase. Biochemistry 23, 2673-2679.
    • (1984) Biochemistry , vol.23 , pp. 2673-2679
    • Jorns, M.S.1    Sancar, G.B.2    Sancar, A.3
  • 23
    • 0027381537 scopus 로고
    • Crystallization and Preliminary X-ray Diffraction Studies of Photolyase (Photoreactivating Enzyme) from the Cyanobacterium Anacystis nidulans
    • Miki, K., Tamada, T., Nishida, H., Inaka, K., Yasui, Q., de Ruiter, P. E., and Eker, A. P. M. (1993) Crystallization and Preliminary X-ray Diffraction Studies of Photolyase (Photoreactivating Enzyme) from the Cyanobacterium Anacystis nidulans. J. Mol. Biol. 233, 167-169.
    • (1993) J. Mol. Biol , vol.233 , pp. 167-169
    • Miki, K.1    Tamada, T.2    Nishida, H.3    Inaka, K.4    Yasui, Q.5    de Ruiter, P.E.6    Eker, A.P.M.7
  • 25
    • 0023643412 scopus 로고
    • The Active Form of Escherichia 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. (1987) The Active Form of Escherichia DNA Photolyase Contains a Fully Reduced Flavin and Not a Flavin Radical, both in Vivo and in Vitro. Biochemistry 26, 7121-7127.
    • (1987) Biochemistry , vol.26 , pp. 7121-7127
    • Payne, G.1    Heelis, P.F.2    Rohrs, B.R.3    Sancar, A.4
  • 26
    • 0033570113 scopus 로고    scopus 로고
    • The effects of pH and semiquinone formation on the oxidation-reduction potentials of flavin mononucleotide
    • Mayhew, S. G. (1999) The effects of pH and semiquinone formation on the oxidation-reduction potentials of flavin mononucleotide. Eur. J. Biochem. 265, 698-702.
    • (1999) Eur. J. Biochem , vol.265 , pp. 698-702
    • Mayhew, S.G.1
  • 27
    • 23044508423 scopus 로고    scopus 로고
    • Substrate Binding Modulates the Reduction Potential of DNA Photolyase
    • Gindt, Y. M., Schelvis, J. P. M., Thoren, K. L., and Huang, T. H. (2005) Substrate Binding Modulates the Reduction Potential of DNA Photolyase. J. Am. Chem. Soc. 127, 10472-10473.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 10472-10473
    • Gindt, Y.M.1    Schelvis, J.P.M.2    Thoren, K.L.3    Huang, T.H.4
  • 28
    • 62849120822 scopus 로고    scopus 로고
    • What Makes the Difference between a Cryptochrome and DNA Photolyase? A Spectroelectrochemical Comparison of the Flavin Redox Transitions
    • Balland, V., Byrdin, M., Eker, A. P. M., Ahmad, M., and Brettel, K. (2009) What Makes the Difference between a Cryptochrome and DNA Photolyase? A Spectroelectrochemical Comparison of the Flavin Redox Transitions. J. Am. Chem. Soc. 131, 426-427.
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 426-427
    • Balland, V.1    Byrdin, M.2    Eker, A.P.M.3    Ahmad, M.4    Brettel, K.5
  • 29
    • 0026755198 scopus 로고
    • Roles of FAD and 8-Hydroxy-5-deazaflavin Chromophores in Photoreactivation by Anacystis nidulans DNA Photolyase
    • Malholtra, K., Kim, S.-T., Walsh, C., and Sancar, A. (1992) Roles of FAD and 8-Hydroxy-5-deazaflavin Chromophores in Photoreactivation by Anacystis nidulans DNA Photolyase. J. Biol. Chem. 267, 15406-15411.
    • (1992) J. Biol. Chem , vol.267 , pp. 15406-15411
    • Malholtra, K.1    Kim, S.-T.2    Walsh, C.3    Sancar, A.4
  • 30
    • 0023129084 scopus 로고
    • Action Mechanism of Escherichia coli DNA Photolyase
    • Jorns, M. S., Baldwin, E. T., Sancar, G. B., and Sancar, A. (1987) Action Mechanism of Escherichia coli DNA Photolyase. J. Biol. Chem. 262, 486-491.
    • (1987) J. Biol. Chem , vol.262 , pp. 486-491
    • Jorns, M.S.1    Baldwin, E.T.2    Sancar, G.B.3    Sancar, A.4
  • 32
    • 49749112845 scopus 로고    scopus 로고
    • Active Site of Escherichia coli DNA Pohtolyase: Asn378 Is Crucial both for Stabilizing the Neutral Flavin Radical Cofactor and for DNA Repair
    • Xu, L., Mu, W., Ding, Y., Luo, Z., Han, Q., Bi, F., Wang, Y., and Song, Q. (2008) Active Site of Escherichia coli DNA Pohtolyase: Asn378 Is Crucial both for Stabilizing the Neutral Flavin Radical Cofactor and for DNA Repair. Biochemistry 47, 8736-8743.
    • (2008) Biochemistry , vol.47 , pp. 8736-8743
    • Xu, L.1    Mu, W.2    Ding, Y.3    Luo, Z.4    Han, Q.5    Bi, F.6    Wang, Y.7    Song, Q.8
  • 33
    • 0031024423 scopus 로고    scopus 로고
    • Control of Oxidation-Reduction Potentials in Flavodoxin from Clostridium beijerinckii: The Role of Conformation Changes
    • Ludwig, M. L., Pattridge, K. A., Metzger, A. L., and Dixon, M. M. (1997) Control of Oxidation-Reduction Potentials in Flavodoxin from Clostridium beijerinckii: The Role of Conformation Changes. Biochemistry 36, 1259-1280.
    • (1997) Biochemistry , vol.36 , pp. 1259-1280
    • Ludwig, M.L.1    Pattridge, K.A.2    Metzger, A.L.3    Dixon, M.M.4
  • 34
    • 0032499631 scopus 로고    scopus 로고
    • Modulation of the Redox Potentials of FMN in Desulfovibrio vulgaris Flavodoxin: Thermodynamic Properties and Crystal Structures of Glycine-61 Mutants
    • O'Farrell, P. A., Walsh, M. A., McCarthy, A. A., Higgins, T. M., Voordouw, G., and Mayhew, S. G. (1998) Modulation of the Redox Potentials of FMN in Desulfovibrio vulgaris Flavodoxin: Thermodynamic Properties and Crystal Structures of Glycine-61 Mutants. Biochemistry 37, 8405-8416.
    • (1998) Biochemistry , vol.37 , pp. 8405-8416
    • O'Farrell, P.A.1    Walsh, M.A.2    McCarthy, A.A.3    Higgins, T.M.4    Voordouw, G.5    Mayhew, S.G.6
  • 35
    • 3042690022 scopus 로고    scopus 로고
    • Proton-Coupled Electron Transfer of Flavodoxin Immobilized on Nanostructured Tin Dioxide Electrodes: Thermodynamics versus Kinetics Control of Protein Redox Function
    • Astuti, Y., Topoglidis, E., Briscoe, P. B., Fantuzzi, A., Gilardi, G., and Durrant, J. R. (2004) Proton-Coupled Electron Transfer of Flavodoxin Immobilized on Nanostructured Tin Dioxide Electrodes: Thermodynamics versus Kinetics Control of Protein Redox Function. J. Am. Chem. Soc. 126, 8001-8009.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 8001-8009
    • Astuti, Y.1    Topoglidis, E.2    Briscoe, P.B.3    Fantuzzi, A.4    Gilardi, G.5    Durrant, J.R.6
  • 36
    • 0035916295 scopus 로고    scopus 로고
    • Determination of the Redox Properties of Human NADPH-Cytochrome P450 Reductase
    • Munro, A. W., Noble, M. A., Robledo, L., Daff, S. N., and Chapman, S. K. (2001) Determination of the Redox Properties of Human NADPH-Cytochrome P450 Reductase. Biochemistry 40, 1956-1963.
    • (2001) Biochemistry , vol.40 , pp. 1956-1963
    • Munro, A.W.1    Noble, M.A.2    Robledo, L.3    Daff, S.N.4    Chapman, S.K.5
  • 37
    • 4644273566 scopus 로고    scopus 로고
    • Redox Properties of the Isolated Flavin Mononucleotide- and Flavin Adenine Dinucleotide-Binding Domains of Neuronal Nitric Oxide Synthase
    • Garnaud, P. E., Koetsier, M., Ost, T. W. B., and Daff, S. (2004) Redox Properties of the Isolated Flavin Mononucleotide- and Flavin Adenine Dinucleotide-Binding Domains of Neuronal Nitric Oxide Synthase. Biochemistry 43, 11035-11044.
    • (2004) Biochemistry , vol.43 , pp. 11035-11044
    • Garnaud, P.E.1    Koetsier, M.2    Ost, T.W.B.3    Daff, S.4
  • 39
    • 8844239344 scopus 로고    scopus 로고
    • The unusual properties of flavocytochrome P450 BM3 flavodoxin domain
    • Hanley, S. C., Ost, T. W. B., and Daff, S. (2004) The unusual properties of flavocytochrome P450 BM3 flavodoxin domain. Biochem. Biophys. Res. Commun. 325, 1418-1423.
    • (2004) Biochem. Biophys. Res. Commun , vol.325 , pp. 1418-1423
    • Hanley, S.C.1    Ost, T.W.B.2    Daff, S.3
  • 40
    • 0024973032 scopus 로고
    • Unusual Redox Properties of Electron-Transfer Flavoprotein from Methylophilus methylotrophus
    • Byron, C. M., Stankovich, M. T., Husain, M., and Davidson, V. L. (1989) Unusual Redox Properties of Electron-Transfer Flavoprotein from Methylophilus methylotrophus. Biochemistry 28, 8582-8587.
    • (1989) Biochemistry , vol.28 , pp. 8582-8587
    • Byron, C.M.1    Stankovich, M.T.2    Husain, M.3    Davidson, V.L.4
  • 41
    • 0035827531 scopus 로고    scopus 로고
    • αArg-237 in Methylophilus methylotrophus (sp. W3A1) Electron-transferring Flavoprotein Affords ∼200-Millivolt Stabilization of the FAD Anionic Semiquinone and a Kinetic Block of Full Reduction to the Dihydroquinone
    • Talfournier, F., Munro, A. W., Basran, J., Sutcliffe, M. J., Daff, S., Chapman, S. K., and Scrutton, N. S. (2001) αArg-237 in Methylophilus methylotrophus (sp. W3A1) Electron-transferring Flavoprotein Affords ∼200-Millivolt Stabilization of the FAD Anionic Semiquinone and a Kinetic Block of Full Reduction to the Dihydroquinone. J. Biol. Chem. 276, 20190-20196.
    • (2001) J. Biol. Chem , vol.276 , pp. 20190-20196
    • Talfournier, F.1    Munro, A.W.2    Basran, J.3    Sutcliffe, M.J.4    Daff, S.5    Chapman, S.K.6    Scrutton, N.S.7
  • 42
    • 0028108347 scopus 로고
    • Activation of Molecular Oxygen by Flavins and Flavoproteins
    • Massey, V. (1994) Activation of Molecular Oxygen by Flavins and Flavoproteins. J. Biol. Chem. 269, 22459-22462.
    • (1994) J. Biol. Chem , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 43
    • 33646348711 scopus 로고    scopus 로고
    • To be or not to be an oxidase: Challenging the oxygen reactivity of flavoenzymes
    • Mattevi, A. (2006) To be or not to be an oxidase: Challenging the oxygen reactivity of flavoenzymes. Trends Biochem. Sci. 31, 276-283.
    • (2006) Trends Biochem. Sci , vol.31 , pp. 276-283
    • Mattevi, A.1
  • 45
    • 44049088217 scopus 로고    scopus 로고
    • Discrimination of Class I Cyclobutane Pyrimidine Dimer Photolyase from Blue Light Photoreceptors by Single Methionine Residue
    • Miyazawa, Y., Nishioka, H., Yura, K., and Yamoto, T. (2008) Discrimination of Class I Cyclobutane Pyrimidine Dimer Photolyase from Blue Light Photoreceptors by Single Methionine Residue. Biophys. J. 94, 2194-2203.
    • (2008) Biophys. J , vol.94 , pp. 2194-2203
    • Miyazawa, Y.1    Nishioka, H.2    Yura, K.3    Yamoto, T.4
  • 46
    • 0024500294 scopus 로고
    • Reconstitution of Escherichia coli DNA Photolyase with Various Folate Derivatives
    • Wang, B., and Jorns, M. S. (1989) Reconstitution of Escherichia coli DNA Photolyase with Various Folate Derivatives. Biochemistry 28, 1148-1152.
    • (1989) Biochemistry , vol.28 , pp. 1148-1152
    • Wang, B.1    Jorns, M.S.2
  • 47
    • 0025100995 scopus 로고
    • Chromophore Function and Interaction in Escherichia coli DNA Photolyase: Reconstitution of the Apoenzyme with Pterin and/or Flavin Derivatives
    • Jorns, M. S., Wang, B., Jordan, S. P., and Chanderkar, L. P. (1990) Chromophore Function and Interaction in Escherichia coli DNA Photolyase: Reconstitution of the Apoenzyme with Pterin and/or Flavin Derivatives. Biochemistry 29, 552-561.
    • (1990) Biochemistry , vol.29 , pp. 552-561
    • Jorns, M.S.1    Wang, B.2    Jordan, S.P.3    Chanderkar, L.P.4
  • 48
    • 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. (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.
    • (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
  • 49
    • 0017716367 scopus 로고
    • A Photochemical Procedure for Reduction of Oxidation- Reduction Proteins Employing Deazariboflavin as Catalyst
    • Massey, V., and Hemmerich, P. (1977) A Photochemical Procedure for Reduction of Oxidation- Reduction Proteins Employing Deazariboflavin as Catalyst. J. Biol. Chem. 252, 5612-5614.
    • (1977) J. Biol. Chem , vol.252 , pp. 5612-5614
    • Massey, V.1    Hemmerich, P.2
  • 50
    • 52749089381 scopus 로고    scopus 로고
    • Spectroscopic investigation of flavoproteins: Mechanistic differences between (electro)chemical and photochemical reduction and oxidation
    • N€oll, G. (2008) Spectroscopic investigation of flavoproteins: Mechanistic differences between (electro)chemical and photochemical reduction and oxidation. J. Photochem. Photobiol., A 200, 34-38.
    • (2008) J. Photochem. Photobiol., A , vol.200 , pp. 34-38
    • N€oll, G.1
  • 54
    • 41249100106 scopus 로고    scopus 로고
    • Animal Type 1 Cryptochromes: Analysis of the Redox State of the FAD Cofactor by Site-Directed Mutagenesis
    • Öztürk, N., Song, S.-H., Selby, C., and Sancar, A. (2008) Animal Type 1 Cryptochromes: Analysis of the Redox State of the FAD Cofactor by Site-Directed Mutagenesis. J. Biol. Chem. 283, 3256-3263.
    • (2008) J. Biol. Chem , vol.283 , pp. 3256-3263
    • Öztürk, N.1    Song, S.-H.2    Selby, C.3    Sancar, A.4
  • 55
    • 33748502081 scopus 로고    scopus 로고
    • Reversible resolution of flavin and pterin cofactors of His-tagged Escherichia coli DNA photolyase
    • Xu, L., Zhang, D., Mu, W., van Berkel, W. J. H., and Luo, Z. (2006) Reversible resolution of flavin and pterin cofactors of His-tagged Escherichia coli DNA photolyase. Biochim. Biophys. Acta 1764, 1454-1461.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1454-1461
    • Xu, L.1    Zhang, D.2    Mu, W.3    van Berkel, W.J.H.4    Luo, Z.5
  • 56
    • 35348833510 scopus 로고    scopus 로고
    • Binding Isotope Effects: Boon and Bane
    • Schramm, V. L. (2007) Binding Isotope Effects: Boon and Bane. Curr. Opin. Chem. Biol. 11, 529-536.
    • (2007) Curr. Opin. Chem. Biol , vol.11 , pp. 529-536
    • Schramm, V.L.1
  • 57
    • 0342327312 scopus 로고    scopus 로고
    • Differential Stabilization of the Three FMN Redox Forms by Tyrosine 94 and Tryptophan 57 in Flavodoxin from Anabena and Its Influence on the Redox Potential
    • Lostao, A., Gómez-Moreno, C., Mayhew, S. G., and Sancho, J. (1997) Differential Stabilization of the Three FMN Redox Forms by Tyrosine 94 and Tryptophan 57 in Flavodoxin from Anabena and Its Influence on the Redox Potential. Biochemistry 36, 14334-14344.
    • (1997) Biochemistry , vol.36 , pp. 14334-14344
    • Lostao, A.1    Gómez-Moreno, C.2    Mayhew, S.G.3    Sancho, J.4
  • 58
    • 0025357978 scopus 로고    scopus 로고
    • Payne, G., Wills, M., Walsh, C., and Sancar, A. (1990) Reconstitution of Escherichia coli Photolyase with Flavins and Flavin Analogues. Biochemistry 29, 5706-5711.
    • Payne, G., Wills, M., Walsh, C., and Sancar, A. (1990) Reconstitution of Escherichia coli Photolyase with Flavins and Flavin Analogues. Biochemistry 29, 5706-5711.
  • 59
    • 33748638376 scopus 로고    scopus 로고
    • The equilibrium between the oxidation of hydrogen peroxide by oxygen and the dismutation of peroxyl or superoxide radicals in aqueous solutions in contact with oxygen
    • Petlicki, J., and van de Ven, T. G. M. (1998) The equilibrium between the oxidation of hydrogen peroxide by oxygen and the dismutation of peroxyl or superoxide radicals in aqueous solutions in contact with oxygen. J. Chem. Soc., Faraday Trans. 94, 2763-2767.
    • (1998) J. Chem. Soc., Faraday Trans , vol.94 , pp. 2763-2767
    • Petlicki, J.1    van de Ven, T.G.M.2
  • 60
    • 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. (2007) Electron Nuclear Double Resonance Differentiates Complementary Roles for Active Site Histidines in (6-4) Photolyase. J. Biol. Chem. 282, 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
  • 61
    • 0034829412 scopus 로고    scopus 로고
    • The Electronic Structure of the Flavin Cofactor in DNA Photolyase
    • Weber, S., M€obius, G., Richter, G., and Kay, C. W. M. (2001) The Electronic Structure of the Flavin Cofactor in DNA Photolyase. J. Am. Chem. Soc. 123, 3790-3798.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 3790-3798
    • Weber, S.1    M€obius, G.2    Richter, G.3    Kay, C.W.M.4
  • 62
    • 0025868148 scopus 로고
    • Active Site of DNA Photolyase: Tryptophan-206 Is the Intrinsic Hydrogen Atom Donor Essential for Flavin Radical Photoreduction and DNA Repair in Vitro
    • Li, Y. F., Heelis, P. F., and Sancar, A. (1991) Active Site of DNA Photolyase: Tryptophan-206 Is the Intrinsic Hydrogen Atom Donor Essential for Flavin Radical Photoreduction and DNA Repair in Vitro. Biochemistry 30, 6322-6329.
    • (1991) Biochemistry , vol.30 , pp. 6322-6329
    • Li, Y.F.1    Heelis, P.F.2    Sancar, A.3
  • 64
    • 0023656687 scopus 로고
    • Purification of the Yeast PHR1 Photolyase from an Escherichia coli Overproducing Strain and Characterization of the Intrinsic Chromophores of the Enzyme
    • Sancar, G. B., Smith, F. W., and Heelis, P. F. (1987) Purification of the Yeast PHR1 Photolyase from an Escherichia coli Overproducing Strain and Characterization of the Intrinsic Chromophores of the Enzyme. J. Biol. Chem. 262, 15457-15465.
    • (1987) J. Biol. Chem , vol.262 , pp. 15457-15465
    • Sancar, G.B.1    Smith, F.W.2    Heelis, P.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.