메뉴 건너뛰기




Volumn 1655, Issue 1-3, 2004, Pages 64-70

Intraprotein electron transfer and proton dynamics during photoactivation of DNA photolyase from E. coli: Review and new insights from an "inverse" deuterium isotope effect

Author keywords

Deuterium isotope effect; Electron transfer; Photolyase; Proton transfer; Transient absorption spectroscopy; Tryptophan radical

Indexed keywords

BACTERIAL ENZYME; DEOXYRIBODIPYRIMIDINE PHOTOLYASE; DEUTERIUM; TRYPTOPHAN;

EID: 1942536615     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.07.001     Document Type: Review
Times cited : (78)

References (24)
  • 1
    • 0003115680 scopus 로고    scopus 로고
    • DNA photolyases in DNA damage and repair
    • J.A. Nickoloff, Hoekstra M.F. Totowa: Humana Press Inc.
    • Yasui A., Eker A.P.M. DNA photolyases in DNA damage and repair. Nickoloff J.A., Hoekstra M.F. DNA Repair in Higher Eukaryotes. vol. 2:1998;9-32 Humana Press Inc. Totowa.
    • (1998) DNA Repair in Higher Eukaryotes , vol.2 , pp. 9-32
    • Yasui, A.1    Eker, A.P.M.2
  • 2
    • 0034733494 scopus 로고    scopus 로고
    • Enzymatic photoreactivation: 50 years and counting
    • Sancar G.B. Enzymatic photoreactivation: 50 years and counting. Mutat. Res. 451:2000;25-37.
    • (2000) Mutat. Res. , vol.451 , pp. 25-37
    • Sancar, G.B.1
  • 4
    • 0025868148 scopus 로고
    • Active site of DNA photolyase: Tryptophan-306 is the intrinsic hydrogen atom donor essential for flavin radical photoreduction and DNA repair in vitro
    • Li Y.F., Heelis P.F., Sancar A. Active site of DNA photolyase: tryptophan-306 is the intrinsic hydrogen atom donor essential for flavin radical photoreduction and DNA repair in vitro. Biochemistry. 30:1991;6322-6329.
    • (1991) Biochemistry , vol.30 , pp. 6322-6329
    • Li, Y.F.1    Heelis, P.F.2    Sancar, A.3
  • 5
    • 0028812143 scopus 로고
    • Crystal structure of DNA photolyase from Escherichia coli
    • Park H.W., Kim S.T., Sancar A., 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
  • 8
    • 0034214080 scopus 로고    scopus 로고
    • Intraprotein radical transfer during photoactivation of DNA photolyase
    • Aubert C., Vos M.H., Mathis P., Eker A.P.M., 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
  • 9
    • 1942507666 scopus 로고    scopus 로고
    • Ultrafast spectroscopy of the excited flavin radical and its primary photoproduct in DNA photolyase from E. coli
    • S. Chapman, R. Perham, & N. Scrutton. Berlin: Rudolph Weber, Agency for Scientific Publications
    • Byrdin M., Brettel K., Aubert C., Eker A.P.M., Vos M.H. Ultrafast spectroscopy of the excited flavin radical and its primary photoproduct in DNA photolyase from E. coli. Chapman S., Perham R., Scrutton N. Flavins and Flavoproteins 2002. 2002;701-706 Rudolph Weber, Agency for Scientific Publications, Berlin.
    • (2002) Flavins and Flavoproteins 2002 , pp. 701-706
    • Byrdin, M.1    Brettel, K.2    Aubert, C.3    Eker, A.P.M.4    Vos, M.H.5
  • 10
    • 0041806654 scopus 로고    scopus 로고
    • Dissection of the triple tryptophan electron transfer chain in E. coli DNA Photolyase: Trp382 is the primary donor in photoactivation
    • Byrdin M., Eker A.P.M., Vos M.H., Brettel K. Dissection of the triple tryptophan electron transfer chain in E. coli DNA Photolyase: Trp382 is the primary donor in photoactivation. Proc. Natl. Acad. Sci. U. S. A. 100:2003;8676-8681.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 8676-8681
    • Byrdin, M.1    Eker, A.P.M.2    Vos, M.H.3    Brettel, K.4
  • 12
    • 0001430553 scopus 로고
    • Doublet-quartet intersystem crossing of flavin radical in DNA photolyase
    • Okamura T., Sancar A., Heelis P.F., Hirata Y., Mataga N. Doublet-quartet intersystem crossing of flavin radical in DNA photolyase. J. Am. Chem. Soc. 111:1989;5967-5969.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 5967-5969
    • Okamura, T.1    Sancar, A.2    Heelis, P.F.3    Hirata, Y.4    Mataga, N.5
  • 13
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page C.C., Moser C.C., Chen X., Dutton P.L. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature. 402:1999;47-52.
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 18
    • 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., Brettel K. Intraprotein electron transfer between tyrosine and tryptophan in DNA photolyase from Anacystis nidulans. Proc. Natl. Acad. Sci. U. S. A. 96:1999;5423-5427.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5423-5427
    • Aubert, C.1    Mathis, P.2    Eker, A.P.M.3    Brettel, K.4
  • 19
    • 0002379632 scopus 로고
    • Theoretical basis and mechanistic utility of solvent isotope effects
    • P.F. Cook. Boca Raton: CRC Press
    • Quinn D.M., Sutton L.D. Theoretical basis and mechanistic utility of solvent isotope effects. Cook P.F. Enzyme Mechanism from Isotope Effects. 1991;73-126 CRC Press, Boca Raton.
    • (1991) Enzyme Mechanism from Isotope Effects , pp. 73-126
    • Quinn, D.M.1    Sutton, L.D.2
  • 20
    • 0026763765 scopus 로고
    • Engineering protein structure for electron transfer function in photosynthesic reaction centers
    • Moser C.C., Dutton P.L. Engineering protein structure for electron transfer function in photosynthesic reaction centers. Biochim. Biophys. Acta. 1101:1992;171-176.
    • (1992) Biochim. Biophys. Acta , vol.1101 , pp. 171-176
    • Moser, C.C.1    Dutton, P.L.2
  • 21
    • 0000660599 scopus 로고    scopus 로고
    • Hydrogen atom transfer in ribonucleotide reductase (RNR)
    • Siegbahn P.E.M., Eriksson L., Himo F., Pavlov M. Hydrogen atom transfer in ribonucleotide reductase (RNR). J. Phys. Chem. 102:1998;10622-10629.
    • (1998) J. Phys. Chem. , vol.102 , pp. 10622-10629
    • Siegbahn, P.E.M.1    Eriksson, L.2    Himo, F.3    Pavlov, M.4
  • 22
    • 0038024617 scopus 로고    scopus 로고
    • Light-induced electron transfer in a cryptochrome blue-light photoreceptor
    • Giovani B., Byrdin M., Ahmad M., 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
  • 24
    • 0033595465 scopus 로고    scopus 로고
    • EPR detection of the transient tyrosyl radical in DNA photolyase from Anacystis nidulans
    • Aubert C., Brettel K., Mathis P., Eker A.P.M., Boussac A. EPR detection of the transient tyrosyl radical in DNA photolyase from Anacystis nidulans. J. Am. Chem. Soc. 121:1999;8659-8660.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8659-8660
    • Aubert, C.1    Brettel, K.2    Mathis, P.3    Eker, A.P.M.4    Boussac, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.