Abstract
The fluorescence and phosphorescence of natural proteins arise from emission by the fluorogenic ring moieties of the aromatic amino acids. Such macromolecular luminescence may be visualized as corresponding to the intrinsic luminescence representing the summed contribution of the amino acid fluorogens, as perturbed by incorporation into a Polypeptide and by the influence of the secondary and tertiary structure of the protein. Accordingly, an understanding of the luminescence properties of tryptophan, tyrosine, and Phenylalanine is basic to an interpretation of the fluorescence and phosphorescence of the proteins.
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References
R. L. Bowman, P. A. Caulfield, and S. Udenfriend, Spectrophotofluorometric assay in the visible and ultraviolet, Science 122, 32–33 (1955).
D. E. Duggan and S. Udenfriend, The spectrophotofluorometric determination of tryptophan in plasma and of tryptophan and tyrosine in protein hydrolysates, J. Biol. Chem. 223, 313–319 (1956).
D. E. Duggan, R. L. Bowman, B. B. Brodie, and S. Udenfriend, A spectrophoto-fluorometric study of compounds of biological interest, Arch. Biochem. Biophys. 68, 1–14 (1957).
H. Sprince, G. R. Rowley, and D. Jameson, Spectrophotofluorometric studies of 5-hydroxyindoles and related compounds, Science 125, 442–443 (1957).
V. G. Shore and A. B. Pardee, Fluorescence of some proteins, nucleic acids, and related compounds, Arch. Biochem. Biophys. 60, 100–107 (1956).
F. W. J. Teale and G. Weber, Ultraviolet fluorescence of the aromatic amino acids, Biochem. J. 65, 476–482 (1957).
P. Debye and J. O. Edwards, A note on the phosphorescence of proteins, Science 116, 143–144 (1952).
R. H. Steele and A. Szent-Gyorgyi, On excitation of biological substances, Proc. Nat. Acad. Sci. 43, 477–491 (1957).
H. M. Hershenson, “Ultraviolet and Visible Absorption Spectra. Index for 1930–1954,” Academic Press, New York (1956).
H. M. Hershenson, “Ultraviolet and Visible Absorption Spectra. Index for 1955–1959,” Academic Press, New York (1961).
D. B. Wetlaufer, Ultraviolet spectra of proteins and amino acids, Advan. Protein. Chem. 17, 303–390 (1962).
G. H. Beaven and E. R. Holiday, Ultraviolet absorption spectra of proteins and amino acids, Advan. Protein. Chem. 7, 319–386 (1952).
C. S. Hicks, The relationship of thyroxin to tryptophan, J. Chem. Soc. 127, 771–776 (1925).
F. C. Smith, The ultra-violet absorption spectra of certain aromatic amino-acids, and of the serum proteins, Proc. Roy. Soc. (London) B104, 198–205 (1929).
C. B. Coulter, F. M. Stone, and E. A. Kabat, The structure of the ultraviolet absorption spectra of certain proteins and amino acids, J. Gen. Physiol. 19, 739–752 (1936).
G. L. Brown and J. T. Randall, Low-temperature ultra-violet absorption spectra of biologically important compounds, Nature 163, 209–210 (1949).
B. G. Edwards, Ultraviolet spectra of some indole derivatives, including tryptophan and gramicidin, Arch. Biochem. 21, 103–108 (1949).
H. Grinspan, J. Birnbaum, and J. Feitelson, Environmental effects on the ultraviolet absorption spectrum of tyrosine, Biochim. Biophys. Acta 126, 13–18 (1966).
T. W. Campbell, S. Linden, S. Godshalk, and W. G. Young, The absorption spectra of some benzene derivatives with unsaturated side chains, J. Am. Chem. Soc. 69, 880–883 (1947).
L. Doub and J. M. Vendenbelt, The ultraviolet absorption spectra of simple unsaturated compounds. I. Mono-and p-disubstituted benzene derivatives, J. Am. Chem. Soc. 69, 2714–2723 (1947).
H. Sponer, G. Nordheim, A. L. Sklar, and E. Teller, Analysis of the near ultraviolet electronic transition of benzene, J. Chem. Phys. 7, 207–220 (1939).
A. L. Sklar, The near ultraviolet absorption of substituted benzenes, J. Chem. Phys. 7, 984–993 (1939).
J. R. Platt and H. B. Klevens, Absolute absorption intensities of alkylbenzenes in the 2250-1700 A. region, Chem. Rev. 41, 301–310 (1947).
A. L. Sklar, Theory of color of organic compounds, J. Chem. Phys. 5, 669–681 (1937).
G. N. Lewis and M. Kasha, Phosphorescence in fluid media and the reverse process of singlet-triplet absorption, J. Am. Chem. Soc. 67, 994–1003 (1945).
A. C. Pitts, Near ultraviolet absorption spectrum of liquid benzene from 2795 to 3560 A, J. Chem. Phys. 18, 1416–1417 (1950).
L. Pauling, “The Nature of the Chemical Bond,” Cornell University Press, Ithaca, New York (1960).
G. Weber, Fluorescence-polarization spectrum and electronic-energy transfer in tyrosine, tryptophan, and related compounds, Biochem. J. 75, 335–345 (1960).
B. L. Van Duuren, Solvent effects in the fluorescence of indole and substituted indoles, J. Org. Chem. 26, 2954–2960 (1961).
J. C. D. Brand and A. I. Scott, in “Techniques of Organic Chemistry” (A. Weiss-berger, ed.), Vol. XI, Part I (D. W. Bentley, ed.), p. 98, Interscience, New York (1963).
E. Yeargers, A. self-consistent-field study of tryptophan, Biophys. J. 8, 1505–1510 (1968).
K. Rosenheck and P. Doty, The far ultraviolet absorption spectra of Polypeptides and protein solutions and their dependence on conformation, Proc. Nat. Acad. Sci. 47, 1775–1785 (1961).
R. B. Setlow and W. R. Guild, The spectrum of the peptide bond and other substances below 230 mμ, Arch. Biochem. Biophys. 34, 223–225 (1951).
A. D. McLaren, Photochemistry of enzymes, proteins, and viruses, Adv. Enzymol. 9, 75–170 (1949).
K. Sommermeyer, V. Birkwald, and H. Pruetz, X-ray excitation of fluorescence of dilute aqueous solutions of aromatic compounds, Naturwissenschaften 48, 666–667 (1961).
L. Augenstein, E. Yeargers, J. Carter, and D. Nelson, Excitation, dissipative, and emissive mechanisms in biochemicals, Radiation Res. Suppl. 7, 128–138 (1967).
H. B. Steen, Excitation of tryptophan in solution during irradiation with x-rays and UV light between 77°K and 300°K, Radiation Res. 41, 268–287 (1970).
D. R. Nelson, J. G. Carter, R. D. Birkhoff, R. N. Hamm, and L. G. Augenstein, Yield of luminescence from X-irradiated biochemicals, Radiation Res. 32, 723–743 (1967).
J. G. Carter, D. R. Nelson, and L. G. Augenstein, Effects of temperature on X-ray-induced light emission from powders of amino acids and trypsin, Arch. Biochem. Biophys. 111, 270–282 (1965).
J. A. Gally and G. M. Edelman, The effect of temperature on the fluorescence of some aromatic amino acids and proteins, Biochim. Biophys. Acta 60, 499–509 (1962).
J. A. Gaily and G. M. Edelman, Effects of conformation and environment on the fluorescence of proteins and Polypeptides, Biopolymers Symp. 1, 367–381 (1964).
F. Bishai, E. Kuntz, and L. Augenstein, Intra-and intermolecular factors affecting the excited states of aromatic amino acids, Biochim. Biophys. Acta 140, 381–394 (1967).
J. Nag-Chaudhuri and L. Augenstein, Effect of the physical environment on excited states of amino acids and proteins, Biopolymers Symp. 1, 441–452 (1964).
E. Yeargers and L. Augenstein, UV spectral properties of Phenylalanine powder, Biophys. J. 5, 687–696 (1965).
S. V. Konev, M. Y. Kostko, L. G. Pikulik, and I. D. Volotovskii, Possible sources of different activity of the excited state of fluorescence of protein solutions, Dokl. Akad. Nauk Belorussk. SSR 10, 500–502 (1966).
E. Kuntz, Tryptophan emission from trypsin and polymer films, Nature 217, 845–846 (1968).
E. Lippert, Spektroskopische Bestimmung des Dipolmoments aromatischer Verbindungen in ersten angeregten Singuletzustand, Z. Elektrochem. 61, 962–975 (1957).
R. W. Cowgill, Fluorescence and protein structure. X. Reappraisal of solvent and structural effects, Biochim. Biophys. Acta 133, 6–18 (1967).
M. S. Walker, T. W. Bednar, and R. Lumry, Exciplex studies. II. Indole and indole derivatives, J. Chem. Phys. 47, 1020–1028 (1967).
L. F. Gladchenko and L. G. Pikulik, Determination of dipole moments of indole and tryptophan in excited states, Zh. Prikl. Spektrosk. 6, 355–360 (1967).
N. Mataga, Y. Torihashi, and K. Ezumi, Electronic structures of carbazole and indole and the solvent effects on the electronic spectra, Theoret. Chim. Acta (Berlin) 2, 158–167 (1964).
B. L. Van Duuren, Effects of the environment on the fluorescence of aromatic compounds in solution, Chem. Rev. 63, 325–354 (1963).
M. S. Walker, T. W. Bednar, and R. Lumry, Exciplex formation in the excited state of indole, J. Chem. Phys. 45, 3455–3456 (1966).
V. P. Bobrovich, G. S. Kembrovskii, and N. I. Marenko, Indole luminescence peculiarities, Dokl. Akad. Nauk Belorussk. SSR 10, 936–940 (1966).
M. S. Walker, T. W. Bednar, and R. Lumry, Exciplex studies. III. Radiative and non-radiative relaxation of the fluorescence state of indole and methyl derivatives of indole, in “Molecular Luminescence” (E. C. Lim, ed.), p. 135, W. A. Benjamin, Inc., New York (1969).
W. E. Kurtin and P. S. Song, A spectroscopic study of the polarized luminescence of indoles, J. Am. Chem. Soc. 91, 4892–4906 (1969).
H. U. Schuett and H. Zimmerman, Polarization of electron bonds of aromatic compounds. VII. Indole, indazole, benzimidazole, benztriazole, and carbazole, Bev. Bunsenges. Physik. Chem. 67, 54–62 (1963).
G. S. Kembrovskii, V. P. Bobrovich, and S. V. Konev, Low-temperature luminescence spectra of indole, Zh. Prikl. Spektrosk. 5, 695–698 (1966).
J. W. Bridges and R. T. Williams, The fluorescence of indoles and aniline derivatives, Biochem. J. 107, 225–237 (1968).
G. M. Barenboim, Interaction of excited biomolecules with oxygen. I. Quenching of photoluminescence of biomolecules by oxygen and nitric oxide, Biofizika 8, 154–164 (1963).
G. M. Barenboim and A. N. Domanskii, Interaction of excited biomolecules with oxygen. II. Extinguishing of tryptophan and tyrosine X-ray fluorescence with oxygen and nitric oxide, Biofizika 8, 321–330 (1963).
J. Feitelson, On the mechanism of fluorescence quenching. Tyrosine and similar compounds, J. Phys. Chem. 68, 391–397 (1964).
W. M. Vaughan and G. Weber, Oxygen quenching of pyrenebutyric acid fluorescence in water. A dynamic probe of the microenvironment, Biochemistry 9, 464–473 (1970).
I. Weinryb, The effect of solvent viscosity on the fluorescence of tryptophan derivatives, Biochem. Biophys. Res. Commun. 34, 865–868 (1969).
G. Weber and K. Rosenheck, Proton-transfer effects in the’ quenching of fluorescence of tyrosine copolymers, Biopolymers Symp. 1, 333–341 (1964).
P. Cuatrecasas, H. Edelhoch, and C. B. Anfinsen, Fluorescence studies of the interaction of nucleotides with the active site of the nuclease of Staphylococcus aureus, Proc. Nat. Acad. Sci. 58, 2043–2050 (1967).
J. Feitelson, Environmental effects on the fluorescence of tyrosine and its homologues, Photochem. Photobiol. 9, 401–410 (1969).
J. W. Longworth, Conformation and interactions of excited states. II. Polystyrene, Polypeptides, and proteins, Biopolymers 4, 1131–1148 (1966).
A. White, Effect of pH on fluorescence of tyrosine, tryptophan, and related compounds, Biochem. J. 71, 217–220 (1959).
G. Weber and F. W. J. Teale, Determination of the absolute quantum yield of fluorescence solutions, Trans. Faraday Soc. 53, 646–655 (1957).
R. F. Chen, Fluorescence quantum yields of tryptophan and tyrosine, Anal. Lett. 1, 35–42 (1967).
R. F. Chen, Some characteristics of the fluorescence of quinine, Anal. Biochem. 19, 374–387 (1967).
W. R. Dawson and M. W. Windsor, Fluorescence yields of aromatic compounds, J. Phys. Chem. 72, 3251–3260 (1968).
J. E. Gill, The fluorescence excitation spectrum of quinine bisulfate, Photochem. Photobiol. 9, 313–322 (1969).
A. N. Fletcher, Quinine sulfate as a fluorescence quantum yield standard, Photochem. Photobiol. 9, 439–444 (1969).
A. Weisstuch and A. C. Testa, A fluorescence study of aminopyridines, J. Phys. Chem. 72, 1982–1987 (1968).
R. F. Chen, G. G. Vurek, and N. Alexander, Fluorescence decay times: Proteins, coenzymes, and other compounds in water, Science 156, 949–951 (1967).
L. F. Gladchenko, M. Y. Kostko, L. G. Pikulik, and A. N. Sevchenko, Duration of the excited state of ultraviolet fluorescence of aromatic amino acids, Dokl. Akad. Nauk Belorussk. SSR 9, 647–650 (1965).
I. Weinryb and R. F. Steiner, The luminescence of tryptophan and Phenylalanine derivatives, Biochemistry 7, 2488–2495 (1968).
R. W. Cowgill, Fluorescence and the structure of proteins. I. Effects of substituents on the fluorescence of indole and phenol compounds, Arch. Biochem. Biophys. 100, 36–44 (1963).
R. W. Cowgill, Fluorescence and the structure of proteins. II. Fluorescence of Peptides containing tryptophan or tyrosine, Biochim. Biophys. Acta 75, 272–273 (1963).
H. Edelhoch, R. S. Bernstein, and M. Wilchek, The fluorescence of tyrosyl and tryptophanyl diketopiperazines, J. Biol. Chem. 243, 5985–5992 (1968).
H. Edelhoch, L. Brand, and M. Wilchek, Fluorescence studies with tryptophyl Peptides, Biochemistry 6, 547–559 (1967).
M. Shinitsky and R. Goldman, Fluorometric detection of histidine-tryptophan complexes in peptides and proteins, Europ. J. Biochem. 3, 139–144 (1967).
H. Edelhoch, R. L. Perlman, and M. Wilchek, Fluorescence studies with tyrosyl peptides, Biochemistry 7, 3893–3900 (1968).
E. C. Russell and R. W. Cowgill, Fluorescence and protein structure. XIII. Further effects of side-chain groups, Biochim. Biophys. Acta 154, 231–233 (1968).
R. W. Cowgill, Fluorescence and protein structure. XVII. On the mechanism of peptide quenching, Biochim. Biophys. Acta 200, 18–25 (1970).
R. W. Cowgill, Fluorescence and protein structure. IV. Iodinated tyrosyl residues, Biochim. Biophys. Acta 94, 74–80 (1965).
R. W. Cowgill, Fluorescence and protein structure. XI. Fluorescence quenching by disulfide and sulfhydryl groups, Biochim. Biophys. Acta 100, 37–44 (1967).
J. Eisinger and G. Navon, Fluorescence quenching and isotope effects of tryptophan, J. Chem. Phys. 50, 2069–2077 (1969).
R. F. Steiner and E. Kirby, The interaction of the ground and excited states of indole derivatives with electron scavengers, J. Phys. Chem. 73, 4130–4135 (1969).
R. F. Steiner and E. Kirby, The influence of solvent and temperature upon the fluorescence of indole derivatives, J. Phys. Chem. 74, 4480–4490 (1970).
L. I. Grossweiner and H.-I. Joschek, Optical generation of hydrated electrons from aromatic compounds, Advan. Chem. Ser. 50, 279–288 (1965).
H.-I. Joschek and L. I. Grossweiner, Optical generation of hydrated electrons from aromatic compounds. II, J. Am. Chem. Soc. 88, 3261–3268 (1966).
T. R. Hopkins and R. Lumry, Energy transfer in proteins: Ejection of electrons from indole exciplexes, Biophys. J. 9, A–216 (1969).
M. Anbar, Reactions of the hydrated electron, Advan. Chem. Ser. 50, 55–81 (1965).
R. Braams, Rate constants of hydrated electron reactions with amino acids, Radiation Res. 27, 319–329 (1966).
G. Weber, in “Light and Life” (W. M. McElroy and B. Glass, eds.), pp. 82–105, The Johns Hopkins Press, Baltimore (1961).
R. C. Armstrong, A third dissociation constant for tryptophan, Biochim. Biophys. Acta 158, 174–175 (1968).
P.-S. Song and W. E. Kurtin, The charge distribution in the excited states of some indoles, Photochem. Photobiol. 9, 175–178 (1969).
H. V. Drushel, A. L. Sommers, and R. C. Cox, Correction of luminescence spectra and calculation of quantum efficiencies using computer techniques, Anal. Chem. 35, 2166–2172 (1963).
W. E. Blumberg, J. Eisinger, and G. Navon, The lifetimes of excited states of some biological molecules, Biophys. J. 8, A–106 (1968).
H. C. Borreson and C. A. Parker, Some precautions required in the calibration of fluorescence spectrometers in the ultraviolet region, Anal. Chem. 38, 1073–1074 (1966).
H. C. Borresen, The fluorescence of guanine and guanosine, Acta Chem. Scand. 21, 920–936 (1967).
H. Ley and K. V. Englehardt, Ultraviolet fluorescence and chemical constitution of cyclic compounds, Z. Physik. Chem. 74, 1–64 (1910).
R. A. Badley and R. W. J. Teale, Resonance energy transfer in pepsin conjugates, J. Mol. Biol. 44, 71–88 (1969).
I. B. Berlman, “Handbook of Fluorescence Spectra of Aromatic Molecules,” Academic Press, New York (1965).
J. Koudelka and L. Augenstein, The importance of the microenvironment surrounding a chromophore in determining its spectroscopic behavior, Photochem. Photobiol. 7, 613–617 (1968).
Z. P. Gribova, cited in “The Fluorescence and Phosphorescence of Proteins and Nucleic Acids” (S. V. Konev, ed.), Plenum Press, New York (1967).
L. I. Grossweiner and W. A. Mulac, Primary processes in the flash photolysis of ovalbumin and constituents, Radiation Res. 10, 515–521 (1959).
S. L. Aksentsev, Y. A. Vladimirov, V. I. Olenev, and Y. Y. Fesenko, Impulse photolysis study of primary photoproducts of aromatic amino acids at 80°K, Biofizika 12, 63–68 (1967).
G. M. Barenboim, Short-lived phosphorescence of dl-tryptophan in solutions, Biofizika 7, 227–232 (1962).
J. W. Longworth, Tyrosine phosphorescence of proteins, Biochem. J. 81, 23p–24p (1961).
J. W. Longworth, Excited state interactions in macromolecules, Photochem. Photobiol. 7, 587–596 (1968).
G. Weber, Polarization of the fluorescence of solutions, in “Fluorescence and Phosphorescence Analysis” (D. M. Hercules, ed.), pp. 217–239, Interscience, New York (1966).
F. Perrin, Polarization of light in fluorescence, average life of molecules in the excited state, J. Phys. Radium 7, 390–401 (1926).
A. Jablonski, Theory of the polarization of photoluminescence of colored solutions, Z. Physik. 96, 236–246 (1935).
J. Lynn and G. D. Fasman, Conformational dependence of fluorescence polarization spectra of l-tryptophan-containing copolypeptides, Biopolymers 6, 159–163 (1968).
R. H. McKay, Effect of various environments on the intrinsic fluorescence polarization spectra of horse liver alchol dehydrogenase, Arch. Biochem. Biophys. 135, 218–230 (1969).
T. Forster, “Fluoreszens organisches Verbindungen,” Vandenhoeck and Ruprecht, Gottingen (1951).
T. Forster, Transfer mechanisms of electronic excitation, Dis. Faraday Soc. 27, 7–17 (1959).
J. W. Longworth, J. J. Ten Bosch, J. A. Knopp, and R. O. Rahn, Electronic energy transfer in oligomers and polymers of l-tyrosine, in “Molecular Luminescence” (E. C. Lim, ed.), p. 529, W. A. Benjamin, Inc., New York (1969).
J. A. Knopp and J. W. Longworth, Energy transfer in oligotyrosyl compounds: Fluorescence quenching as a function of the ionization of the phenolic hydroxyl groups, Biochim. Biophys. Acta 154, 436–443 (1968).
R. F. Steiner, The phosphorescence of tyrosine Oligopeptides, Biochem. Biophys. Res. Commun. 30, 502–507 (1968).
R. F. Steiner and R. Kolinski, The phosphorescence of Oligopeptides containing tryptophan and tyrosine, Biochemistry 7, 1014–1018 (1968).
T. Cassen and D. Kearns, Investigation of energy transfer in peptides by excitation difference spectra techniques, Biochem. Biophys. Res. Commun. 31, 851–855 (1968).
C. Hélène, M. Ptak, and R. Santus, Optical and magnetic study of the excited states in the polynucleotides and Polypeptides, J. Chim. Phys. 65, 160–166 (1968).
J. E. Gill and M. Weissbluth, Thermoluminescence of amino acids and proteins irradiated with ultraviolet light, Biopolymers Symp. 1, 433–439 (1964).
S. Prydz and T. Rogeberg, Spectral study of thermoluminescence from aromatic amino acids, Phys. Norvegica 1, 227–233 (1963).
M. Guermonprez, R. Santus, and M. Ptak, Delayed luminescence of aromatic amino acids in boric acid, Comp. Rend. 261 (Group 6), 387–390 (1965).
D. I. Roshchupkin, Effect of gases on the thermoluminescence and prolonged afterglow of frozen proteins and aromatic amino acids irradiated by ultraviolet light, Biofizika 11, 167–168 (1966).
A. K. Kukushkin and A. N. Kuznetsov, Possible physical mechanisms of the thermal luminescence of some aromatic amino acids and proteins, Biofizika 11, 223–227 (1966).
E. E. Fesenko, E. A. Burshtein, and Y. A. Vladimirov, Biphotonic ionization of aromatic acids in alkaline medium at 80°K, Biofizika 12, 616–623 (1967).
R. W. Ricci, Deuterium-isotope effect on the fluorescence yields and lifetimes of indole derivatives—including tryptophan and tryptamine, Photochem. Photobiol. 12, 67–75 (1970).
S. S. Lehrer, Deuterium-isotope effects on the fluorescence of tryptophan in peptides and in lysozyme, J. Am. Chem. Soc. 92, 3459–3462 (1970).
J. Feitelson, Environmental effects on the fluorescence of tryptophan and other indole derivatives, Israel J. Chem. 8, 241–252 (1970).
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Weinryb, I., Steiner, R.F. (1971). The Luminescence of the Aromatic Amino Acids. In: Steiner, R.F., Weinryb, I. (eds) Excited States of Proteins and Nucleic Acids. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1878-1_7
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