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Volumn 118, Issue 10, 2014, Pages 1864-1878

Photosensitized singlet oxygen luminescence from the protein matrix of Zn-substituted myoglobin

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; EXCITED STATES; OXYGEN; RATE CONSTANTS; ZINC;

EID: 84896280075     PISSN: 10895639     EISSN: 15205215     Source Type: Journal    
DOI: 10.1021/jp501615h     Document Type: Article
Times cited : (37)

References (61)
  • 1
    • 0038322621 scopus 로고    scopus 로고
    • Physical Mechanisms of Generation and Deactivation of Singlet Oxygen
    • Schweitzer, C.; Schmidt, R. Physical Mechanisms of Generation and Deactivation of Singlet Oxygen Chem. Rev. 2003, 103, 1685-1757
    • (2003) Chem. Rev. , vol.103 , pp. 1685-1757
    • Schweitzer, C.1    Schmidt, R.2
  • 2
    • 38949177764 scopus 로고    scopus 로고
    • Electronic Mechanisms of Molecular Oxygen Activation
    • Minaev, B. F. Electronic Mechanisms of Molecular Oxygen Activation Russ. Chem. Rev. 2007, 76, 988-1010
    • (2007) Russ. Chem. Rev. , vol.76 , pp. 988-1010
    • Minaev, B.F.1
  • 3
    • 42049096770 scopus 로고    scopus 로고
    • Luminescence and Photochemical Studies of Singlet Oxygen Photonics
    • Krasnovsky, A. A., Jr. Luminescence and Photochemical Studies of Singlet Oxygen Photonics J. Photochem. Photobiol. A: Chem. 2008, 196, 210-218
    • (2008) J. Photochem. Photobiol. A: Chem. , vol.196 , pp. 210-218
    • Krasnovsky Jr., A.A.1
  • 4
    • 84862211032 scopus 로고    scopus 로고
    • Reaction of Singlet Oxygen with Tryptophan in Proteins: A Pronounced Effect of the Local Environment on the Reaction Rate
    • Jensen, R. L.; Arnbjerg, J.; Ogilby, P. R. Reaction of Singlet Oxygen with Tryptophan in Proteins: A Pronounced Effect of the Local Environment on the Reaction Rate J. Am. Chem. Soc. 2012, 134, 9820-9826
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 9820-9826
    • Jensen, R.L.1    Arnbjerg, J.2    Ogilby, P.R.3
  • 5
    • 84884134220 scopus 로고    scopus 로고
    • Oxygen-Dependent Photochemistry and Photophysics of "miniSOG," a Protein-Encased Flavin
    • Pimenta, F. M.; Jensen, R. L.; Breitenbach, T.; Etzerodt, M.; Ogilby, P. R. Oxygen-Dependent Photochemistry and Photophysics of "MiniSOG," a Protein-Encased Flavin Photochem. Photobiol. 2013, 89, 1116-1126
    • (2013) Photochem. Photobiol. , vol.89 , pp. 1116-1126
    • Pimenta, F.M.1    Jensen, R.L.2    Breitenbach, T.3    Etzerodt, M.4    Ogilby, P.R.5
  • 8
    • 0001266102 scopus 로고
    • A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-ray Analysis
    • Kendrew, J. C.; Bodo, G.; Dintzis, H. M.; Parrish, R. G.; Wyckoff, H.; Phillips, D. C. A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-ray Analysis Nature 1958, 181, 662-666
    • (1958) Nature , vol.181 , pp. 662-666
    • Kendrew, J.C.1    Bodo, G.2    Dintzis, H.M.3    Parrish, R.G.4    Wyckoff, H.5    Phillips, D.C.6
  • 9
    • 0025061598 scopus 로고
    • Activation Parameters for Ligand Escape from Myoglobin Proteins at Room Temperature
    • Chatfield, M. D.; Walda, K. N.; Magde, D. Activation Parameters for Ligand Escape from Myoglobin Proteins at Room Temperature J. Am. Chem. Soc. 1990, 112, 4680-4687
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 4680-4687
    • Chatfield, M.D.1    Walda, K.N.2    Magde, D.3
  • 12
    • 0037023751 scopus 로고    scopus 로고
    • Structural Dynamics of Myoglobin. Ligand Migration among Protein Cavities Studied by Fourier Transform Infrared/Temperature Derivative Spectroscopy
    • Lamb, D. S.; Nienhaus, K.; Arcovito, A.; Draghi, F.; Miele, A. E.; Brunori, M.; Nienhaus, G. U. Structural Dynamics of Myoglobin. Ligand Migration among Protein Cavities Studied by Fourier Transform Infrared/Temperature Derivative Spectroscopy J. Biol. Chem. 2002, 277, 11636-11644
    • (2002) J. Biol. Chem. , vol.277 , pp. 11636-11644
    • Lamb, D.S.1    Nienhaus, K.2    Arcovito, A.3    Draghi, F.4    Miele, A.E.5    Brunori, M.6    Nienhaus, G.U.7
  • 13
    • 0021766921 scopus 로고
    • Cavities in Proteins: Structure of a Metmyoglobin - Xenon Complex Solved to 1.9 Å
    • Tilton, R. F., Jr.; Kuntz, I. D., Jr.; Petsko, G. A. Cavities in Proteins: Structure of a Metmyoglobin-Xenon Complex Solved to 1.9 Å Biochemistry 1984, 23, 2849-2857
    • (1984) Biochemistry , vol.23 , pp. 2849-2857
    • Tilton Jr., R.F.1    Kuntz Jr., I.D.2    Petsko, G.A.3
  • 15
    • 44849137851 scopus 로고    scopus 로고
    • The Kinetics of Ligand Migration in Crystallized Myoglobin as Revealed by Molecular Dynamics Simulation
    • Anselmi, M.; Di Nola, A.; Amadei, A. The Kinetics of Ligand Migration in Crystallized Myoglobin as Revealed by Molecular Dynamics Simulation Biophys. J. 2008, 94, 4277-4281
    • (2008) Biophys. J. , vol.94 , pp. 4277-4281
    • Anselmi, M.1    Di Nola, A.2    Amadei, A.3
  • 19
    • 0023919078 scopus 로고
    • Photophysics and Reactivity of Heme Proteins: A Femtosecond Absorption Study of Hemoglobin, Myoglobin, and Protoheme
    • Petrich, J. W.; Poyart, C.; Martin, J. L. Photophysics and Reactivity of Heme Proteins: A Femtosecond Absorption Study of Hemoglobin, Myoglobin, and Protoheme Biochemistry 1988, 27, 4049-4060
    • (1988) Biochemistry , vol.27 , pp. 4049-4060
    • Petrich, J.W.1    Poyart, C.2    Martin, J.L.3
  • 21
    • 0014963392 scopus 로고
    • Conformational Studies on Modified Proteins and Peptides. Artificial Myoglobins Prepared with Modified and Metalloporphyrins
    • Andrest, S. F.; Atassi, M. Z. Conformational Studies on Modified Proteins and Peptides. Artificial Myoglobins Prepared with Modified and Metalloporphyrins Biochemistry 1970, 9, 2268-2275
    • (1970) Biochemistry , vol.9 , pp. 2268-2275
    • Andrest, S.F.1    Atassi, M.Z.2
  • 22
    • 0001620852 scopus 로고
    • Bonding in Zinc Proto- and Mesoporphyrin Substituted Myoglobin and Model Compounds Studied by Resonance Raman Spectroscopy
    • Feitelson, J.; Spiro, T. G. Bonding in Zinc Proto- and Mesoporphyrin Substituted Myoglobin and Model Compounds Studied by Resonance Raman Spectroscopy Inorg. Chem. 1986, 25, 861-865
    • (1986) Inorg. Chem. , vol.25 , pp. 861-865
    • Feitelson, J.1    Spiro, T.G.2
  • 23
    • 0031836879 scopus 로고    scopus 로고
    • Real-Time Observation of Conformational Fluctuations in Zn-Substituted Myoglobin by Time-Resolved Transient Hole-Burning Spectroscopy
    • Shibata, Y.; Kurita, A.; Kushida, T. Real-Time Observation of Conformational Fluctuations in Zn-Substituted Myoglobin by Time-Resolved Transient Hole-Burning Spectroscopy Biophys. J. 1998, 75, 521-527
    • (1998) Biophys. J. , vol.75 , pp. 521-527
    • Shibata, Y.1    Kurita, A.2    Kushida, T.3
  • 24
    • 0035143046 scopus 로고    scopus 로고
    • Time-Resolved Hole-Burning Study on Myoglobin: Fluctuation of Restricted Water within Distal Pocket
    • Shibata, Y.; Ishikawa, H.; Takahashi, S.; Morishima, I. Time-Resolved Hole-Burning Study on Myoglobin: Fluctuation of Restricted Water within Distal Pocket Biophys. J. 2001, 80, 1013-1023
    • (2001) Biophys. J. , vol.80 , pp. 1013-1023
    • Shibata, Y.1    Ishikawa, H.2    Takahashi, S.3    Morishima, I.4
  • 26
    • 49749199032 scopus 로고
    • Cleavage of the Haem-Protein Link by Acid Methylethylketone
    • Teale, F. W. J. Cleavage of the Haem-Protein Link by Acid Methylethylketone Biochim. Biophys. Acta 1959, 35, 543
    • (1959) Biochim. Biophys. Acta , vol.35 , pp. 543
    • Teale, F.W.J.1
  • 27
    • 0023757084 scopus 로고
    • PH-Dependence of Photo-Induced Electron Transfer in Zinc-Substituted Sperm Whale Myoglobin
    • Shosheva, A. Ch.; Christova, P. K.; Atanasov, B. P. pH-Dependence of Photo-Induced Electron Transfer in Zinc-Substituted Sperm Whale Myoglobin Biochim. Biophys. Acta 1988, 957, 202-206
    • (1988) Biochim. Biophys. Acta , vol.957 , pp. 202-206
    • Shosheva, A.Ch.1    Christova, P.K.2    Atanasov, B.P.3
  • 29
    • 0001165315 scopus 로고
    • Probabilities of Intercombination Transitions in Porphyrin and Metalloporphyrin Molecules
    • Gradyushko, A. T.; Tsvirko, M. P. Probabilities of Intercombination Transitions in Porphyrin and Metalloporphyrin Molecules Opt. Spectrosc. (USSR) 1971, 31, 291-295
    • (1971) Opt. Spectrosc. (USSR) , vol.31 , pp. 291-295
    • Gradyushko, A.T.1    Tsvirko, M.P.2
  • 30
    • 2342509626 scopus 로고    scopus 로고
    • Kinetic Studies of Differences between α- And β-Chains of Human Hemoglobin: An Approach for Determination of the Chain Affinity to Oxygen
    • Dzhagarov, B. M.; Lepeshkevich, S. V. Kinetic Studies of Differences between α- and β-Chains of Human Hemoglobin: An Approach for Determination of the Chain Affinity to Oxygen Chem. Phys. Lett. 2004, 390, 59-64
    • (2004) Chem. Phys. Lett. , vol.390 , pp. 59-64
    • Dzhagarov, B.M.1    Lepeshkevich, S.V.2
  • 31
    • 28244449040 scopus 로고    scopus 로고
    • Mutual Effects of Proton and Sodium Chloride on Oxygenation of Liganded Human Hemoglobin: Oxygen Affinities of the α and β Subunits
    • Lepeshkevich, S. V.; Dzhagarov, B. M. Mutual Effects of Proton and Sodium Chloride on Oxygenation of Liganded Human Hemoglobin: Oxygen Affinities of the α and β Subunits FEBS J. 2005, 272, 6109-6119
    • (2005) FEBS J. , vol.272 , pp. 6109-6119
    • Lepeshkevich, S.V.1    Dzhagarov, B.M.2
  • 32
    • 56449105547 scopus 로고    scopus 로고
    • Effect of Zinc and Cadmium Ions on Structure and Function of Myoglobin
    • Lepeshkevich, S. V.; Dzhagarov, B. M. Effect of Zinc and Cadmium Ions on Structure and Function of Myoglobin Biochim. Biophys. Acta 2009, 1794, 103-109
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 103-109
    • Lepeshkevich, S.V.1    Dzhagarov, B.M.2
  • 33
    • 73249143026 scopus 로고    scopus 로고
    • Molecular Oxygen Binding with α and β Subunits within the R Quaternary State of Human Hemoglobin in Solutions and Porous Sol-Gel Matrices
    • Lepeshkevich, S. V.; Parkhats, M. V.; Stepuro, I. I.; Dzhagarov, B. M. Molecular Oxygen Binding with α and β Subunits within the R Quaternary State of Human Hemoglobin in Solutions and Porous Sol-Gel Matrices Biochim. Biophys. Acta 2009, 1794, 1823-1830
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1823-1830
    • Lepeshkevich, S.V.1    Parkhats, M.V.2    Stepuro, I.I.3    Dzhagarov, B.M.4
  • 34
    • 0141683763 scopus 로고    scopus 로고
    • Laser Kinetic Studies of Bimolecular Oxygenation Reaction of α and β Subunits within the R State of Human Hemoglobin
    • Lepeshkevich, S. V.; Konovalova, N. V.; Dzhagarov, B. M. Laser Kinetic Studies of Bimolecular Oxygenation Reaction of α and β Subunits within the R State of Human Hemoglobin Biochem. (Russian) 2003, 68, 676-685
    • (2003) Biochem. (Russian) , vol.68 , pp. 676-685
    • Lepeshkevich, S.V.1    Konovalova, N.V.2    Dzhagarov, B.M.3
  • 35
    • 0025313093 scopus 로고
    • Reactions of Excited Triplet States of Metal Substituted Myoglobin with Dioxygen and Quinone
    • Papp, S.; Vanderkooi, J. M.; Owen, C. S.; Holtom, G. R.; Phillips, C. M. Reactions of Excited Triplet States of Metal Substituted Myoglobin with Dioxygen and Quinone Biophys. J. 1990, 58, 177-186
    • (1990) Biophys. J. , vol.58 , pp. 177-186
    • Papp, S.1    Vanderkooi, J.M.2    Owen, C.S.3    Holtom, G.R.4    Phillips, C.M.5
  • 36
    • 0023128930 scopus 로고
    • Fluctuation Domains in Myoglobin Fluorescence Quenching Studies
    • Albani, J.; Alpert, B. Fluctuation Domains in Myoglobin Fluorescence Quenching Studies Eur. J. Biochem. 1987, 162, 175-178
    • (1987) Eur. J. Biochem. , vol.162 , pp. 175-178
    • Albani, J.1    Alpert, B.2
  • 37
    • 34547454818 scopus 로고    scopus 로고
    • Ultrafast Relaxation of Zinc Protoporphyrin Encapsulated within Apomyoglobin in Buffer Solutions
    • Luo, L.; Chang, Ch.-H.; Chen, Y.-Ch.; Wu, T.-K.; Diau, E. W.-G. Ultrafast Relaxation of Zinc Protoporphyrin Encapsulated within Apomyoglobin in Buffer Solutions J. Phys. Chem. B 2007, 111, 7656-7664
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7656-7664
    • Luo, L.1    Chang, Ch.-H.2    Chen, Y.-Ch.3    Wu, T.-K.4    Diau, E.W.-G.5
  • 38
    • 0000175237 scopus 로고    scopus 로고
    • Extra-Liganding Effects in Zn-Octaethylporphyrin Solutions in a Temperature Interval of 300-77 K
    • Knyukshto, V. N.; Shulga, A. M.; Sagun, E. I.; Zenkevich, E. I. Extra-Liganding Effects in Zn-Octaethylporphyrin Solutions in a Temperature Interval of 300-77 K J. Appl. Spectrosc. 1998, 65, 943-951
    • (1998) J. Appl. Spectrosc. , vol.65 , pp. 943-951
    • Knyukshto, V.N.1    Shulga, A.M.2    Sagun, E.I.3    Zenkevich, E.I.4
  • 39
    • 0343267065 scopus 로고
    • Effectiveness of the Formation of Singlet Oxygen Photosensitised by Water-Soluble Porphyrins
    • Dzhagarov, B. M.; Salokhiddinov, K. I.; Egorova, G. D.; Gurinovich, G. P. Effectiveness of the Formation of Singlet Oxygen Photosensitised by Water-Soluble Porphyrins Russ. J. Phys. Chem. 1987, 61, 1281-1283
    • (1987) Russ. J. Phys. Chem. , vol.61 , pp. 1281-1283
    • Dzhagarov, B.M.1    Salokhiddinov, K.I.2    Egorova, G.D.3    Gurinovich, G.P.4
  • 40
  • 41
    • 0342785231 scopus 로고    scopus 로고
    • Determination of Triplet Quantum Yields from Triplet-Triplet Annihilation Fluorescence
    • Bachilo, S. M.; Weisman, R. B. Determination of Triplet Quantum Yields from Triplet-Triplet Annihilation Fluorescence J. Phys. Chem. A 2000, 104, 7711-7714
    • (2000) J. Phys. Chem. A , vol.104 , pp. 7711-7714
    • Bachilo, S.M.1    Weisman, R.B.2
  • 42
    • 0000723751 scopus 로고
    • Long-Range Triplet-Triplet Energy Transfer within Metal-Substituted Hemoglobins
    • Zemel, H.; Hoffman, B. M. Long-Range Triplet-Triplet Energy Transfer within Metal-Substituted Hemoglobins J. Am. Chem. Soc. 1981, 103, 1192-1201
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 1192-1201
    • Zemel, H.1    Hoffman, B.M.2
  • 43
    • 0023278441 scopus 로고
    • Quenching of Zinc-Protoporphyrin Triplet State as a Measure of Small-Molecule Diffusion through the Structure of Myoglobin
    • Barboy, N.; Feitelson, J. Quenching of Zinc-Protoporphyrin Triplet State as a Measure of Small-Molecule Diffusion through the Structure of Myoglobin Biochemistry 1987, 26, 3240-3244
    • (1987) Biochemistry , vol.26 , pp. 3240-3244
    • Barboy, N.1    Feitelson, J.2
  • 44
    • 0024401914 scopus 로고
    • Diffusion of Small Molecules through the Structure of Myoglobin. Environmental Effects
    • Barboy, N.; Feitelson, J. Diffusion of Small Molecules through the Structure of Myoglobin. Environmental Effects Biochemistry 1989, 28, 5450-5456
    • (1989) Biochemistry , vol.28 , pp. 5450-5456
    • Barboy, N.1    Feitelson, J.2
  • 45
    • 0037157156 scopus 로고    scopus 로고
    • 2 and the Vibrational Relaxation of the Six-Coordinate Heme Species
    • 2 and the Vibrational Relaxation of the Six-Coordinate Heme Species J. Am. Chem. Soc. 2002, 124, 5914-5924
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5914-5924
    • Ye, X.1    Demidov, A.2    Champion, P.M.3
  • 46
    • 1042294532 scopus 로고    scopus 로고
    • Photodissociation of Oxygenated Forms of the Native Hemoglobin HbA and Its Isolated α- And β-Subunits and Kinetics of Molecular Oxygen Rebinding
    • Dzhagarov, B. M.; Galievsky, V. A.; Kruk, N. N.; Yakutovich, M. D. Photodissociation of Oxygenated Forms of the Native Hemoglobin HbA and Its Isolated α- and β-Subunits and Kinetics of Molecular Oxygen Rebinding Dokl. Biophys. (Dokl. Akad. Nauk) 1999, 366, 38-41
    • (1999) Dokl. Biophys. (Dokl. Akad. Nauk) , vol.366 , pp. 38-41
    • Dzhagarov, B.M.1    Galievsky, V.A.2    Kruk, N.N.3    Yakutovich, M.D.4
  • 47
    • 0030768765 scopus 로고    scopus 로고
    • Ligand Migration in Sperm Whale Myoglobin
    • Scott, E. E.; Gibson, Q. H. Ligand Migration in Sperm Whale Myoglobin Biochemistry 1997, 36, 11909-11917
    • (1997) Biochemistry , vol.36 , pp. 11909-11917
    • Scott, E.E.1    Gibson, Q.H.2
  • 50
    • 0037414281 scopus 로고    scopus 로고
    • 2+- Protoporphyrin IX Deoxymyoglobin Mimic: Application to Oxygen Migration Pathway Analysis
    • 2+-Protoporphyrin IX Deoxymyoglobin Mimic: Application to Oxygen Migration Pathway Analysis J. Am. Chem. Soc. 2003, 125, 3813-3820
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3813-3820
    • McNaughton, L.1    Hernández, G.2    Lemaster, D.M.3
  • 51
    • 0028391073 scopus 로고
    • Reactivity of Singlet Oxygen toward Amino Acids and Peptides
    • Michaeli, A.; Feitelson, J. Reactivity of Singlet Oxygen toward Amino Acids and Peptides Photochem. Photobiol. 1994, 59, 284-289
    • (1994) Photochem. Photobiol. , vol.59 , pp. 284-289
    • Michaeli, A.1    Feitelson, J.2
  • 52
    • 84985430616 scopus 로고
    • Rate Parameters for the Quenching of Singlet Oxygen by Water-Soluble and Lipid-Soluble Substrates in Aqueous and Micellar Systems
    • Lindig, B. A.; Rodgers, M. A. J. Rate Parameters for the Quenching of Singlet Oxygen by Water-Soluble and Lipid-Soluble Substrates in Aqueous and Micellar Systems Photochem. Photobiol. 1981, 33, 627-634
    • (1981) Photochem. Photobiol. , vol.33 , pp. 627-634
    • Lindig, B.A.1    Rodgers, M.A.J.2
  • 54
    • 0000147096 scopus 로고
    • Quenching of Singlet Oxygen by the Chlorophylls and Porphyrines
    • Krasnovsky, A. A., Jr.; Venediktov, E. A.; Chernenko, O. M. Quenching of Singlet Oxygen by the Chlorophylls and Porphyrines Biophysics 1982, 27, 1009-1016
    • (1982) Biophysics , vol.27 , pp. 1009-1016
    • Krasnovsky Jr., A.A.1    Venediktov, E.A.2    Chernenko, O.M.3
  • 60
    • 0014663430 scopus 로고
    • Measurement of Protein Concentration with Interferences Optics
    • Babul, J.; Stellwagen, E. Measurement of Protein Concentration with Interferences Optics Analyt. Biochem. 1969, 28, 216-221
    • (1969) Analyt. Biochem. , vol.28 , pp. 216-221
    • Babul, J.1    Stellwagen, E.2
  • 61
    • 84890903363 scopus 로고    scopus 로고
    • Temperature Effect on Radiative Lifetimes: The Case of Singlet Oxygen in Liquid Solvents
    • Jensen, R. L.; Holmegaard, L.; Ogilby, P. R. Temperature Effect on Radiative Lifetimes: The Case of Singlet Oxygen in Liquid Solvents J. Phys. Chem. B 2013, 117, 16227-16235
    • (2013) J. Phys. Chem. B , vol.117 , pp. 16227-16235
    • Jensen, R.L.1    Holmegaard, L.2    Ogilby, P.R.3


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