Does photodissociation of molecular oxygen from myoglobin and hemoglobin yield singlet oxygen?

Journal of Photochemistry and Photobiology B: Biology

Volumn 120, Issue , 2013, Pages 130-141

  Lepeshkevich, Sergei V ^a   Stasheuski, Alexander S ^a   Parkhats, Marina V ^a   Galievsky, Victor A ^a   Dzhagarov, Boris M ^a  

^a B I STEPANOV INSTITUTE OF PHYSICS   (Belarus)

Author keywords

Hemoglobin; Luminescence; Myoglobin; Photodissociation; Quantum yield; Singlet oxygen

Indexed keywords

HEMOGLOBIN; MYOGLOBIN; OXYGEN; SINGLET OXYGEN;

ARTICLE; ENERGY TRANSFER; LUMINESCENCE; PHOTODEGRADATION; PHOTODISSOCIATION; PHOTODYNAMICS; PRIORITY JOURNAL; QUANTUM YIELD; SIGNAL NOISE RATIO;

ANIMALS; HUMANS; KINETICS; METALLOPORPHYRINS; MYOGLOBIN; OXYGEN; OXYHEMOGLOBINS; PHOTOLYSIS; SINGLET OXYGEN;

EID: 84875447825     PISSN: 10111344     EISSN: 18732682     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2012.12.012     Document Type: Article

References (63)

1. V.R.I. Kaila, M.I. Verkhovsky, and M. Wikström Proton-coupled electron transfer in cytochrome oxidase Chem. Rev. 110 2010 7062 7081
2. A.A. Krasnovsky Jr. Luminescence and photochemical studies of singlet oxygen photonics J. Photochem. Photobiol. A: Chem. 196 2008 210 218
3. C.S. Foote W.A. Pryor, Free Radicals in Biology vol. 2 1976 Academic Press New York
4. C. Schweitzer, and R. Schmidt Physical mechanisms of generation and deactivation of singlet oxygen Chem. Rev. 103 2003 1685 1757
5. B.F. Minaev Electronic mechanisms of molecular oxygen activation Russ. Chem. Rev. 76 2007 988 1010
6. D.M. Wagnerová, and K. Lang Photorelease of triplet and singlet oxygen from dioxygen complexes Coord. Chem. Rev. 255 2011 2904 2911
7. P.R. Ogilby Singlet oxygen: there is still something new under the sun, and it is better than ever Photochem. Photobiol. Sci. 9 2010 1543 1560
8. A.N. Macpherson, A. Telfer, J. Barber, and T.G. Truscott Direct detection of singlet oxygen from isolated Photosystem II reaction centres Biochim. Biophys. Acta 1143 1993 301 309 (Pubitemid 23216739)
9. A.U. Khan, P. Gebauer, and L.P. Hager Chloroperoxidase generation of singlet Δ molecular oxygen observed directly by spectroscopy in the 1- to 1.6-μm region Proc. Natl. Acad. Sci. USA 80 1983 5195 5197
10. J.R. Kanofsky Singlet oxygen production by lactoperoxidase. Evidence from 1270 nm chemiluminescence J. Biol. Chem. 258 1983 5991 5993
11. J.R. Kanofsky, and B. Axelrod Singlet oxygen production by soybean lipoxygenase isozymes J. Biol. Chem. 261 1986 1099 1104 (Pubitemid 16144771)
12. J.R. Kanofsky Singlet oxygen production by bleomycin: a comparison with heme-containing compounds J. Biol. Chem. 261 1986 13546 13550 (Pubitemid 17196373)
13. J.R. Kanofsky, H. Hoogland, R. Wever, and S.J. Weiss Singlet oxygen production by human eosinophils J. Biol. Chem. 263 1988 9692 9696
14. A.U. Khan, and M. Kasha Singlet molecular oxygen in the Haber-Weiss reaction Proc. Natl. Acad. Sci. USA 91 1994 12365 12367
15. R.W. Redmond, and I.E. Kochevar Spatially resolved cellular responses to singlet oxygen Photochem. Photobiol. 82 2006 1178 1186 (Pubitemid 44701996)
16. D.A. Case, B.H. Huynh, and M. Karplus Binding of oxygen and carbon monoxide to hemoglobin. An analysis of the ground and excited states J. Am. Chem. Soc. 101 1979 4433 4453
17. 2 binds to heme: reasons for rapid binding and spin inversion J. Biol. Chem. 279 2004 14561 14569 (Pubitemid 38618843)
18. B.D. Olafson, and W.A. Goddard III Molecular description of dioxygen bonding in hemoglobin Proc. Natl. Acad. Sci. USA 74 1977 1315 1319 (Pubitemid 8086883)
19. 2 to heme in oxyhemoglobin Proc. Natl. Acad. Sci. USA 72 1975 2335 2339
20. J.J. Weiss Nature of the iron-oxygen bond in oxyhæmoglobin Nature 202 1964 83 84
21. L. Pauling Nature of the iron-oxygen bond in oxyhæmoglobin Nature 203 1964 182 183
22. T.E. Tsai, J.L. Groves, and C.S. Wu Electronic structure of iron-dioxygen bond in oxy-Hb-A and its isolated oxy - α and oxy-β chains J. Chem. Phys. 74 1981 4306 4314
23. E. Bucci, and C. Fronticelli A new method for the preparation of α and β subunits of human hemoglobin J. Biol. Chem. 240 1965 551 552
24. V.A. Galievsky, A.S. Stasheuski, V.V. Kiselyov, A.I. Shabusov, M.V. Belkov, and B.M. Dzhagarov Laser NIR lifetime spectrometer with nanosecond time resolution Instrum. Exp. Tech. 53 2010 568 574
25. J.B. Verlhac, A. Gaudemer, and I. Krajlic Water-soluble porphyrins and metalloporphyrins as photosensitizers in aerated aqueous solutions. I. Detection and determination of quantum yield of formation of singlet oxygen Nouv. J. Chim. 8 1984 401 406
26. P.K. Frederiksen, S.P. Mcllroy, C.B. Nielsen, L. Nikolajsen, E. Skovsen, M. Jørgensen, K.V. Mikkelsen, and P.R. Ogilby Two-photon photosensitized production of singlet oxygen in water J. Am. Chem. Soc. 127 2005 255 269 (Pubitemid 40103568)
27. S. Nonell, and S.E. Braslavsky Time-resolved singlet oxygen detection Method Enzymol. 319 2000 37 49 (Pubitemid 30448028)
28. J. Baier, T. Fuβ, C. Pöllmann, C. Wiesmann, K. Pindl, R. Engl, D. Baumer, M. Maier, M. Landthaler, and W. Bäumler Theoretical and experimental analysis of the luminescence signal of singlet oxygen for different photosensitizers J. Photochem. Photobiol. B: Biol. 87 2007 163 173 (Pubitemid 46888137)
29. S.Yu. Yegorov, and A.A. Krasnovskii Jr. Photosensitized luminescence of oxygen on pulsed laser excitation. Kinetics of decay in aqueous solutions Biophysics 28 1983 532 534
30. g) in liquid water as determined by time-resolved infrared luminescence measurements J. Am. Chem. Soc. 104 1982 5541 5543
31. g state generated in water by porphyrin-sensitizer Opt. Spektr. 55 1983 71 73
32. F. Wilkinson, W.P. Helman, and A.B. Ross Rate constants for the decay and reactions of the lowest electronically excited singlet state of molecular oxygen in solution. An expanded and revised compilation J. Phys. Chem. Ref. Data 24 1995 663 1021
33. B.M. Dzhagarov, V.S. Chirvony, and G.P. Gurinovich Picosecond dynamics of electronic excitation energy redistribution in metalloporphyrins V.S. Letokhov, Laser Picoseconds Spectroscopy and Photochemistry of Biomolecules 1987 Adam Hilger Bristol 137 182
34. S.V. Lepeshkevich, J. Karpiuk, I.V. Sazanovich, and B.M. Dzhagarov A kinetic description of dioxygen motion within alpha- and beta-subunits of human hemoglobin in the R-state: geminate and bimolecular stages of the oxygenation reaction Biochemistry 43 2004 1675 1684 (Pubitemid 38200574)
35. S. Sottini, S. Abbruzzetti, C. Viapiani, S. Bettati, L. Ronda, and A. Mozzarelli Evidence for two geminate rebinding states following laser photolysis of R state hemoglobin encapsulated in wet silica gels J. Phys. Chem. B 109 2005 11411 11413 (Pubitemid 40925592)
36. J. Huang, A. Ridsdale, J. Wang, and J.M. Friedman Kinetic hole burning, hole filling, and conformational relaxation in heme proteins: direct evidence for the functional significance of a hierarchy of dynamical processes Biochemistry 36 1997 14353 14365 (Pubitemid 27509927)
37. S.V. Lepeshkevich, S.A. Biziuk, A.M. Lemeza, and B.M. Dzhagarov The kinetics of molecular oxygen migration in the isolated α chains of human hemoglobin as revealed by molecular dynamics simulations and laser kinetic spectroscopy Biochim. Biophys. Acta 1814 2011 1279 1288
38. 2 and hemoglobin Proc. Nat. Acad. Sci. USA 77 1980 5606 5610 (Pubitemid 11222764)
39. J.W. Petrich, C. Poyart, and J.L. Martin Photophysics and reactivity of heme proteins: a femtosecond absorption study of hemoglobin, myoglobin, and protoheme Biochemistry 27 1988 4049 4060
40. B.I. Greene, R.M. Hochstrasser, R.B. Weisman, and W.A. Eaton Spectroscopic studies of oxy- and carbonmonoxyhemoglobin after pulsed optical excitation Proc. Natl. Acad. Sci. USA 75 1978 5255 5259 (Pubitemid 9079771)
41. W.A. Eaton, L.K. Hanson, P.J. Stephens, J.C. Sutherland, and J.B.R. Dunn Optical spectra of oxy- and deoxyhemoglobin J. Am. Chem. Soc. 100 1978 4991 5003
42. H. Eicher, D. Bade, and F. Parak Theoretical determination of the electronic structure and the spatial arrangement of ferrous iron in deoxygenated sperm whale myoglobin and human hemoglobin from Mössbauer experiments J. Chem. Phys. 64 1976 1446 1455
43. B.M. Dzhagarov, V.A. Galievsky, N.N. Kruk, and M.D. Yakutovich Photodissociation of oxygenated forms of the native hemoglobin HbA and its isolated α-and β-subunits and kinetics of molecular oxygen rebinding Dokl. Biophys. (Doklady Akademii Nauk) 366 1999 38 41
44. 2 and the vibrational relaxation of the sixcoordinate heme species J. Am. Chem. Soc. 124 2002 5914 5924 (Pubitemid 34533531)
45. S.V. Lepeshkevich, and B.M. Dzhagarov Effect of zinc and cadmium ions on structure and function of myoglobin Biochim. Biophys. Acta 1794 2009 103 109
46. B.M. Hoffman, and Q.H. Gibson On the photosensitivity of liganded hemoproteins and their metal-substituted analogues Proc. Natl. Acad. Sci. USA 75 1978 21 25 (Pubitemid 8290440)
47. B.M. Dzhagarov, N.N. Kruk, S.A. Tikhomirov, V. Gulbinas, and G.M. Andreyuk Laser picosecond and nanosecond flash-photolysis of hemoglobin: excited-state spectra and lifetimes, oxygen photodissociation and recombination, the pH-effect Lietuvos fizikos žurnalas 34 1994 108 113
48. A. Waleh, and G.H. Loew Quantum mechanical studies of the photodissociation of oxyheme complexes J. Am. Chem. Soc. 104 1982 2352 2356
49. 2 and CO to subunit chains of hemoglobin A J. Biol. Chem. 254 1979 2875 2880 (Pubitemid 9196120)
50. 2+ in normal human hemoglobin and its isolated subunits J. Chem. Phys. 61 1974 3750 3758
51. S.V. Lepeshkevich, M.V. Parkhats, I.I. Stepuro, and B.M. Dzhagarov 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 1794 2009 1823 1830
52. D. Mogilevtsev, A. Maloshtan, S.V. Lepeshkevich, and B.M. Dzhagarov Spontaneous emission of singlet oxygen near dielectric nano-objects and radiative diagnostics of bio-objects J. Fluoresc. 22 2012 1415 1419
53. S.V. Lepeshkevich, and B.M. Dzhagarov Mutual effects of proton and sodium chloride on oxygenation of liganded human hemoglobin: oxygen affinities of the α and β subunits FEBS J. 272 2005 6109 6119 (Pubitemid 41713700)
54. 2) J. Phys. Chem. 91 1987 4599 4602
55. g) J. Phys. Chem. 99 1995 3521 3526
56. J. Babul, and E. Stellwagen Measurement of protein concentration with interferences optics Anal. Biochem. 28 1969 216 221
57. N. Barboy, and J. Feitelson Quenching of the zinc-protoporphyrin triplet state as a measure of small-molecule diffusion through the structure of myoglobin Biochemistry 26 1987 3240 3244 (Pubitemid 17087862)
58. B. Alpert, and L. Lindqvist Porphyrin triplet state probing the diffusion of oxygen in hemoglobin Science 187 1975 836 837
59. E.A. Venediktov, and A.A. Krasnovsky Jr. Quenching of luminescence of singlet molecular oxygen by porphyrin complexes with high-charge metal ions Biophysics 25 1980 347 348
60. A. Michaeli, and J. Feitelson Reactivity of singlet oxygen toward amino acids and peptides Photochem. Photobiol. 59 1994 284 289
61. R.L. Jensen, J. Arnbjerg, and P.R. Ogilby Reaction of singlet oxygen with tryptophan in proteins: a pronounced effect of the local environment on the reaction rate J. Am. Chem. Sci. 134 2012 9820 9826
62. 2) production in photoexcited organic molecule-molecular oxygen complexes J. Phys. Chem. 95 1991 5190 5197
63. A.A. Krasnovsky Jr., E.A. Venediktov, and O.M. Chernenko Quenching of singlet oxygen by the chlorophylls and porphyrines Biophysics 27 1982 1009 1016