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Volumn 189, Issue 1, 2007, Pages 39-45

Luminescence and Raman spectroscopic studies on the damage of tryptophan, histidine and carnosine by singlet oxygen

Author keywords

Amino acids; Carnosine; Singlet oxygen; Spectroscopy

Indexed keywords


EID: 34248340542     PISSN: 10106030     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jphotochem.2007.01.005     Document Type: Article
Times cited : (31)

References (44)
  • 1
    • 0038322621 scopus 로고    scopus 로고
    • Physical mechanisms of generation and deactivation of singlet oxygen
    • Schweitzer C., and Schmidt R. Physical mechanisms of generation and deactivation of singlet oxygen. Chem. Rev. 103 (2003) 1685-1757
    • (2003) Chem. Rev. , vol.103 , pp. 1685-1757
    • Schweitzer, C.1    Schmidt, R.2
  • 2
    • 0037564169 scopus 로고    scopus 로고
    • Singlet oxygen-mediated damage to proteins and its consequences
    • Davies M.J. Singlet oxygen-mediated damage to proteins and its consequences. Biochem. Biophys. Res. Commun. 305 (2003) 761-770
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 761-770
    • Davies, M.J.1
  • 4
    • 0035472975 scopus 로고    scopus 로고
    • Effect of visible light on selected enzymes, vitamins and amino acids
    • Edwards A.M., and Silva E. Effect of visible light on selected enzymes, vitamins and amino acids. J. Photochem. Photobiol. B: Biol. 63 (2001) 126-131
    • (2001) J. Photochem. Photobiol. B: Biol. , vol.63 , pp. 126-131
    • Edwards, A.M.1    Silva, E.2
  • 5
    • 84889533712 scopus 로고
    • Rate constants for the decay and reactions of the lowest electronically excited state of molecular oxygen in solution. An expanded and revised compilation
    • Wilkinson F., Helman W.P., and Ross A.B. Rate constants for the decay and reactions of the lowest electronically excited state of molecular oxygen in solution. An expanded and revised compilation. J. Phys. Chem. Ref. Data 24 (1995) 663-1021
    • (1995) J. Phys. Chem. Ref. Data , vol.24 , pp. 663-1021
    • Wilkinson, F.1    Helman, W.P.2    Ross, A.B.3
  • 6
    • 3042688696 scopus 로고    scopus 로고
    • Reactive species formed on proteins exposed to singlet oxygen
    • Davies M.J. Reactive species formed on proteins exposed to singlet oxygen. Photochem. Photobiol. Sci. 3 (2004) 17-25
    • (2004) Photochem. Photobiol. Sci. , vol.3 , pp. 17-25
    • Davies, M.J.1
  • 7
    • 24944444794 scopus 로고    scopus 로고
    • Oxidative DNA strand scission induced by peptides
    • Prestwich E.G., Marc D.R., Rego J., and Kelley S.O. Oxidative DNA strand scission induced by peptides. Chem. Biol. 12 (2005) 695-701
    • (2005) Chem. Biol. , vol.12 , pp. 695-701
    • Prestwich, E.G.1    Marc, D.R.2    Rego, J.3    Kelley, S.O.4
  • 9
    • 0344158770 scopus 로고
    • Antioxidant activity of carnosine, homocarnosine, and anserine present in muscle and brain
    • Kohen R., Yamamoto Y., Cundy K.C., and Ames B.N. Antioxidant activity of carnosine, homocarnosine, and anserine present in muscle and brain. Proc. Natl. Acad. Sci. U.S.A. 85 (1988) 3175-3179
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 3175-3179
    • Kohen, R.1    Yamamoto, Y.2    Cundy, K.C.3    Ames, B.N.4
  • 11
    • 0027185676 scopus 로고
    • Extracellular production of singlet oxygen by stimulated macrophages quantified using 9,l0-diphenylanthracene and perylene in a polystyrene film
    • Steinbeck M.J., Khan A.U., and Karnovsky M.J. Extracellular production of singlet oxygen by stimulated macrophages quantified using 9,l0-diphenylanthracene and perylene in a polystyrene film. J. Biol. Chem. 268 (1993) 15649-15654
    • (1993) J. Biol. Chem. , vol.268 , pp. 15649-15654
    • Steinbeck, M.J.1    Khan, A.U.2    Karnovsky, M.J.3
  • 12
    • 28144437214 scopus 로고    scopus 로고
    • Synthesis and time-resolved fluorimentric application of a europium chelate-based phosphorescence probe specific for singlet oxygen
    • Song B., Wang G., Tan M., and Yuan J. Synthesis and time-resolved fluorimentric application of a europium chelate-based phosphorescence probe specific for singlet oxygen. New J. Chem. 29 (2005) 1431-1438
    • (2005) New J. Chem. , vol.29 , pp. 1431-1438
    • Song, B.1    Wang, G.2    Tan, M.3    Yuan, J.4
  • 13
    • 28144465655 scopus 로고    scopus 로고
    • A new europium chelate-based phosphorescence probe specific for singlet oxygen
    • Song B., Wang G., Tan M., and Yuan J. A new europium chelate-based phosphorescence probe specific for singlet oxygen. Chem. Commun. (2005) 3553-3555
    • (2005) Chem. Commun. , pp. 3553-3555
    • Song, B.1    Wang, G.2    Tan, M.3    Yuan, J.4
  • 14
    • 33646493036 scopus 로고    scopus 로고
    • A new terbium (III) chelate as an efficient singlet oxygen fluorescence probe
    • Wang G., Tan M., and Yuan J. A new terbium (III) chelate as an efficient singlet oxygen fluorescence probe. Free Radic. Biol. Med. 40 (2006) 1644-1653
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 1644-1653
    • Wang, G.1    Tan, M.2    Yuan, J.3
  • 15
    • 0031988467 scopus 로고    scopus 로고
    • Mercapto-substituted perylenequinonoid pigments. A new type of singlet oxygen sensitizer
    • Weng M., Zhuang M.-H., and Shen T. Mercapto-substituted perylenequinonoid pigments. A new type of singlet oxygen sensitizer. Dyes Pigments 36 (1998) 93-102
    • (1998) Dyes Pigments , vol.36 , pp. 93-102
    • Weng, M.1    Zhuang, M.-H.2    Shen, T.3
  • 16
    • 0032104360 scopus 로고    scopus 로고
    • Antioxidant characteristics of l-histidine
    • Wade A.M., and Tucker H.N. Antioxidant characteristics of l-histidine. J. Nutr. Biochem. 9 (1998) 308-315
    • (1998) J. Nutr. Biochem. , vol.9 , pp. 308-315
    • Wade, A.M.1    Tucker, H.N.2
  • 17
    • 3042592136 scopus 로고    scopus 로고
    • Anti-crosslinking properties of carnosine: significance of histidine
    • Hobart L.J., Seibel I., Yeargans G.S., and Seidler N.W. Anti-crosslinking properties of carnosine: significance of histidine. Life Sci. 75 (2004) 1379-1389
    • (2004) Life Sci. , vol.75 , pp. 1379-1389
    • Hobart, L.J.1    Seibel, I.2    Yeargans, G.S.3    Seidler, N.W.4
  • 18
    • 0000562315 scopus 로고    scopus 로고
    • Quenching of singlet oxygen by trolox C, ascorbate, and amino acids: effects of pH and temperature
    • Bisby R.H., Morgan C.G., Hamblett I., and Gorman A.A. Quenching of singlet oxygen by trolox C, ascorbate, and amino acids: effects of pH and temperature. J. Phys. Chem. A 103 (1999) 7454-7459
    • (1999) J. Phys. Chem. A , vol.103 , pp. 7454-7459
    • Bisby, R.H.1    Morgan, C.G.2    Hamblett, I.3    Gorman, A.A.4
  • 19
    • 33750063177 scopus 로고    scopus 로고
    • A europium (III) complex as an efficient singlet oxygen luminescence probe
    • Song B., Wang G., Tan M., and Yuan J. A europium (III) complex as an efficient singlet oxygen luminescence probe. J. Am. Chem. Soc. 128 (2006) 13442-13450
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 13442-13450
    • Song, B.1    Wang, G.2    Tan, M.3    Yuan, J.4
  • 20
  • 21
    • 12744271798 scopus 로고
    • Chemistry of singlet oxygen. VII. Quenching by β-carotene
    • Foote C.S., and Denny R.W. Chemistry of singlet oxygen. VII. Quenching by β-carotene. J. Am. Chem. Soc. 90 (1968) 6233-6235
    • (1968) J. Am. Chem. Soc. , vol.90 , pp. 6233-6235
    • Foote, C.S.1    Denny, R.W.2
  • 22
    • 84995036150 scopus 로고
    • Chemical reaction rates of amino acids with singlet oxygen
    • Matheson I.B.C., and Lee J. Chemical reaction rates of amino acids with singlet oxygen. Photochem. Photobiol. 29 (1979) 279-881
    • (1979) Photochem. Photobiol. , vol.29 , pp. 279-881
    • Matheson, I.B.C.1    Lee, J.2
  • 23
    • 0032987671 scopus 로고    scopus 로고
    • Improved functional recovery of ischemic rat hearts due to singlet oxygen scavengers histidine and carnosine
    • Lee J.W., Miyawaki H., Bobst E.V., Hester J.D., Ashraf M., and Bobst A.M. Improved functional recovery of ischemic rat hearts due to singlet oxygen scavengers histidine and carnosine. J. Mol. Cell Cardiol. 31 (1999) 113-121
    • (1999) J. Mol. Cell Cardiol. , vol.31 , pp. 113-121
    • Lee, J.W.1    Miyawaki, H.2    Bobst, E.V.3    Hester, J.D.4    Ashraf, M.5    Bobst, A.M.6
  • 24
    • 84986793568 scopus 로고
    • Resonance Raman spectra of poly (l-lysine), aromatic amino acids, l-histidine and native and thermally unfolded ribonuclease A
    • Chinsky L., Jolles B., Laigle A., and Turpin P.Y. Resonance Raman spectra of poly (l-lysine), aromatic amino acids, l-histidine and native and thermally unfolded ribonuclease A. J. Raman Spectrosc. 16 (1985) 235-240
    • (1985) J. Raman Spectrosc. , vol.16 , pp. 235-240
    • Chinsky, L.1    Jolles, B.2    Laigle, A.3    Turpin, P.Y.4
  • 25
    • 2542544330 scopus 로고    scopus 로고
    • UV resonance Raman spectroscopy of DNA and protein constituents of viruses: assignments and cross sections for excitations at 257, 244, 238, and 229 nm
    • Wen Z.Q., and Thomas Jr. G.J. UV resonance Raman spectroscopy of DNA and protein constituents of viruses: assignments and cross sections for excitations at 257, 244, 238, and 229 nm. Biopolymers 45 (1997) 247-256
    • (1997) Biopolymers , vol.45 , pp. 247-256
    • Wen, Z.Q.1    Thomas Jr., G.J.2
  • 26
    • 30544439249 scopus 로고    scopus 로고
    • Structural changes during the photocycle of photoactive yellow protein monitored by ultraviolet resonance Raman spectra of tyrosine and tryptophan
    • El-Mashtoly S.F., Yamauchi S., Kumauchi M., Hamada N., Tokunaga F., and Unno M. Structural changes during the photocycle of photoactive yellow protein monitored by ultraviolet resonance Raman spectra of tyrosine and tryptophan. J. Phys. Chem B 109 (2005) 23666-23673
    • (2005) J. Phys. Chem B , vol.109 , pp. 23666-23673
    • El-Mashtoly, S.F.1    Yamauchi, S.2    Kumauchi, M.3    Hamada, N.4    Tokunaga, F.5    Unno, M.6
  • 27
    • 0036160618 scopus 로고    scopus 로고
    • Characterization of deoxygenated cobalt (II)-carnosine complexes by Raman and IR spectroscopy
    • Torreggiani A., Taddei P., and Fini G. Characterization of deoxygenated cobalt (II)-carnosine complexes by Raman and IR spectroscopy. Biopolymers 67 (2002) 70-81
    • (2002) Biopolymers , vol.67 , pp. 70-81
    • Torreggiani, A.1    Taddei, P.2    Fini, G.3
  • 28
    • 0034323107 scopus 로고    scopus 로고
    • A new measurement system for UV resonance Raman spectra of large proteins and its application to cytochrome c oxidase
    • Aki M., Ogura T., Shinzawa-Itoh K., Yoshikawa S., and Kitagawa T. A new measurement system for UV resonance Raman spectra of large proteins and its application to cytochrome c oxidase. J. Phys. Chem. B 104 (2000) 10765-10774
    • (2000) J. Phys. Chem. B , vol.104 , pp. 10765-10774
    • Aki, M.1    Ogura, T.2    Shinzawa-Itoh, K.3    Yoshikawa, S.4    Kitagawa, T.5
  • 29
    • 0042737808 scopus 로고    scopus 로고
    • Raman structural markers of tryptophan and histidine side chains in proteins
    • Takeuchi H. Raman structural markers of tryptophan and histidine side chains in proteins. Biopolymers (Biospectroscopy) 72 (2003) 305-317
    • (2003) Biopolymers (Biospectroscopy) , vol.72 , pp. 305-317
    • Takeuchi, H.1
  • 30
    • 0024284778 scopus 로고
    • Characterization of individual tryptophan side chains in proteins using Raman spectroscopy and hydrogen-deuterium exchange kinetics
    • Miura T., Takeuchi H., and Harada I. Characterization of individual tryptophan side chains in proteins using Raman spectroscopy and hydrogen-deuterium exchange kinetics. Biochemistry 27 (1988) 88-94
    • (1988) Biochemistry , vol.27 , pp. 88-94
    • Miura, T.1    Takeuchi, H.2    Harada, I.3
  • 31
    • 84988213609 scopus 로고
    • Theoretical analysis of the resonance Raman spectrum of tryptophan
    • Marconi G. Theoretical analysis of the resonance Raman spectrum of tryptophan. J. Raman Spectrosc. 22 (1991) 361-365
    • (1991) J. Raman Spectrosc. , vol.22 , pp. 361-365
    • Marconi, G.1
  • 32
    • 0036632772 scopus 로고    scopus 로고
    • Singlet oxygen mediated protein oxidation: Evidence for the formation of reactive side-chain peroxides on tyrosine residues
    • Wright A., Bubb W.A., Hawkins C.L., and Davies M.J. Singlet oxygen mediated protein oxidation: Evidence for the formation of reactive side-chain peroxides on tyrosine residues. Photochem. Photobiol. 76 (2002) 35-46
    • (2002) Photochem. Photobiol. , vol.76 , pp. 35-46
    • Wright, A.1    Bubb, W.A.2    Hawkins, C.L.3    Davies, M.J.4
  • 33
    • 0037467044 scopus 로고    scopus 로고
    • Structural and vibrational study of the tautomerism of histamine free-base in solution
    • Ramírez F.J., Tuñón I., Collado J.A., and Silla E. Structural and vibrational study of the tautomerism of histamine free-base in solution. J. Am. Chem. Soc. 125 (2003) 2328-2340
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2328-2340
    • Ramírez, F.J.1    Tuñón, I.2    Collado, J.A.3    Silla, E.4
  • 34
    • 23644460666 scopus 로고    scopus 로고
    • Infrared Raman spectroscopic study of pH-induced structural changes of l-histidine in aqueous environment
    • Mesu J.G., Visser T., Soulimani F., and Weckhuysen B.M. Infrared Raman spectroscopic study of pH-induced structural changes of l-histidine in aqueous environment. Vib. Spectrosc. 39 (2005) 114-125
    • (2005) Vib. Spectrosc. , vol.39 , pp. 114-125
    • Mesu, J.G.1    Visser, T.2    Soulimani, F.3    Weckhuysen, B.M.4
  • 36
    • 32044472563 scopus 로고    scopus 로고
    • Experiemntal and theoretical Raman investigation on interactions of Cu(II) with histamine
    • Torreggiani A., Esposti A.D., Tamba M., Marconi G., and Fini G. Experiemntal and theoretical Raman investigation on interactions of Cu(II) with histamine. J. Raman Spectrosc. 37 (2006) 291-298
    • (2006) J. Raman Spectrosc. , vol.37 , pp. 291-298
    • Torreggiani, A.1    Esposti, A.D.2    Tamba, M.3    Marconi, G.4    Fini, G.5
  • 37
    • 33645092667 scopus 로고    scopus 로고
    • New insights into the coordination chemistry and molecular structure of copper(II) histidine complexes in aqueous solutions
    • Mesu J.G., Visser T., Soulimani F., van Faassen E.E., de Peinder P., Beale A.M., and Weckhuysen B.M. New insights into the coordination chemistry and molecular structure of copper(II) histidine complexes in aqueous solutions. Inorg. Chem. 45 (2006) 1960-1971
    • (2006) Inorg. Chem. , vol.45 , pp. 1960-1971
    • Mesu, J.G.1    Visser, T.2    Soulimani, F.3    van Faassen, E.E.4    de Peinder, P.5    Beale, A.M.6    Weckhuysen, B.M.7
  • 39
    • 0034598055 scopus 로고    scopus 로고
    • Synthesis of a C-13, N-15 labeled imidazole and characterization of the 2,5-endoperoide and its decomposition
    • Kang P., and Foote C.S. Synthesis of a C-13, N-15 labeled imidazole and characterization of the 2,5-endoperoide and its decomposition. Tetrahedron Lett. 41 (2000) 9623-9626
    • (2000) Tetrahedron Lett. , vol.41 , pp. 9623-9626
    • Kang, P.1    Foote, C.S.2
  • 40
    • 31644437921 scopus 로고    scopus 로고
    • Sensitizer-mediated photooxidation of histidine residues: Evidence for the formation of reactive side-chain peroxides
    • Agon V.V., Bubb W.A., Wright A., Hawkins C.L., and Davies M.J. Sensitizer-mediated photooxidation of histidine residues: Evidence for the formation of reactive side-chain peroxides. Free Radic. Biol. Med. 40 (2006) 698-710
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 698-710
    • Agon, V.V.1    Bubb, W.A.2    Wright, A.3    Hawkins, C.L.4    Davies, M.J.5
  • 41
    • 0002015458 scopus 로고    scopus 로고
    • Binding of copper(II) to carnosine: Raman and IR spectroscopic study
    • Torreggiani A., Tamba M., and Fini G. Binding of copper(II) to carnosine: Raman and IR spectroscopic study. Biopolymers (Biospectroscopy) 57 (2000) 149-159
    • (2000) Biopolymers (Biospectroscopy) , vol.57 , pp. 149-159
    • Torreggiani, A.1    Tamba, M.2    Fini, G.3
  • 42
  • 43
    • 0033771231 scopus 로고    scopus 로고
    • Raman and IR spectroscopic investigation of zinc(II)-carnosine complexes
    • Torreggiania A., Bonora S., and Finib G. Raman and IR spectroscopic investigation of zinc(II)-carnosine complexes. Biopolymers (Biospectroscopy) 57 (2002) 352-364
    • (2002) Biopolymers (Biospectroscopy) , vol.57 , pp. 352-364
    • Torreggiania, A.1    Bonora, S.2    Finib, G.3
  • 44
    • 0014640056 scopus 로고
    • Sensitized photooxidation of histidine and its derivatives. Products and mechanism of the reaction
    • Tomita M., Irie M., and Ukita T. Sensitized photooxidation of histidine and its derivatives. Products and mechanism of the reaction. Biochemistry 8 (1969) 5149-5160
    • (1969) Biochemistry , vol.8 , pp. 5149-5160
    • Tomita, M.1    Irie, M.2    Ukita, T.3


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