Abstract
The bulk of the fluorescence of lysozyme is located in Trp 62 and Trp 108. By examination of the fluorescence of derivatives in which Trp 62 and/or Trp 108 are specifically oxidized, it has been possible to detect a pH-dependent interaction between tryptophan residues. This interaction is interpreted as energy transfer from Trp 108 to Trp 62.
Keywords: pH dependence, spectroscopy, protein structure, enzyme-substrate complex
Full text
PDF




Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Blake C. C., Johnson L. N., Mair G. A., North A. C., Phillips D. C., Sarma V. R. Crystallographic studies of the activity of hen egg-white lysozyme. Proc R Soc Lond B Biol Sci. 1967 Apr 18;167(1009):378–388. doi: 10.1098/rspb.1967.0035. [DOI] [PubMed] [Google Scholar]
- Blake C. C., Mair G. A., North A. C., Phillips D. C., Sarma V. R. On the conformation of the hen egg-white lysozyme molecule. Proc R Soc Lond B Biol Sci. 1967 Apr 18;167(1009):365–377. doi: 10.1098/rspb.1967.0034. [DOI] [PubMed] [Google Scholar]
- COWGILL R. W. FLUORESCENCE AND THE STRUCTURE OF PROTEINS. II. FLUORESCENCE OF PEPTIDES CONTAINING TRYPTOPHAN OR TYROSINE. Biochim Biophys Acta. 1963 Sep 24;75:272–273. doi: 10.1016/0006-3002(63)90607-3. [DOI] [PubMed] [Google Scholar]
- Eisinger J., Feuer B., Lamola A. A. Intramolecular singlet excitation transfer. Applications to polypeptides. Biochemistry. 1969 Oct;8(10):3908–3915. doi: 10.1021/bi00838a005. [DOI] [PubMed] [Google Scholar]
- Eisinger J. Intramolecular energy transfer in adrenocorticotropin. Biochemistry. 1969 Oct;8(10):3902–3908. doi: 10.1021/bi00838a004. [DOI] [PubMed] [Google Scholar]
- Glickson J. D., Phillips W. D., Rupley J. A. Proton magnetic resonance study of the indole NH resonances of lysozyme. Assignment, deuterium exchange kinetics, and inhibitor binding. J Am Chem Soc. 1971 Aug 11;93(16):4031–4038. doi: 10.1021/ja00745a035. [DOI] [PubMed] [Google Scholar]
- HAMAGUCHI K., KURONO A. STRUCTURE OF MURAMIDASE (LYSOZYME). I. THE EFFECT OF GUANIDINE HYDROCHLORIDE ON MURAMIDASE. J Biochem. 1963 Aug;54:111–122. [PubMed] [Google Scholar]
- Hayashi K., Imoto T., Funatsu G., Funatsu M. The position of the active tryptophan residue in lysozyme. J Biochem. 1965 Sep;58(3):227–235. doi: 10.1093/oxfordjournals.jbchem.a128190. [DOI] [PubMed] [Google Scholar]
- Lehrer S. S., Fasman G. D. Fluorescence of lysozyme and lysozyme substrate complexes. Separation of tryptophan contributions by fluorescence difference methods. J Biol Chem. 1967 Oct 25;242(20):4644–4651. [PubMed] [Google Scholar]
- Lehrer S. S., Fasman G. D. The fluorescence of lysozyme and lysozyme substrate complexes. Biochem Biophys Res Commun. 1966 Apr 19;23(2):133–138. doi: 10.1016/0006-291x(66)90517-1. [DOI] [PubMed] [Google Scholar]
- Lehrer S. S. Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry. 1971 Aug 17;10(17):3254–3263. doi: 10.1021/bi00793a015. [DOI] [PubMed] [Google Scholar]
- Rupley J. A., Butler L., Gerring M., Hartdegen F. J., Pecoraro R. Studies on the enzymic activity of lysozyme, 3. The binding of saccharides. Proc Natl Acad Sci U S A. 1967 Apr;57(4):1088–1095. doi: 10.1073/pnas.57.4.1088. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Steiner R. F. Varying luminescence behavior of the different tryptophan residues of papain. Biochemistry. 1971 Mar 2;10(5):771–778. doi: 10.1021/bi00781a008. [DOI] [PubMed] [Google Scholar]
- Takahashi T., Hamaguchi K., Hayashi K., Imoto T., Funatsu M. Structure of lysozyme. X. On the structural role of tryptophan residues. J Biochem. 1965 Oct;58(4):385–387. doi: 10.1093/oxfordjournals.jbchem.a128215. [DOI] [PubMed] [Google Scholar]
- Tanford C., Aune K. C. Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. 3. Dependence on temperature. Biochemistry. 1970 Jan 20;9(2):206–211. doi: 10.1021/bi00804a003. [DOI] [PubMed] [Google Scholar]
- Teichberg V. I., Kay C. M., Sharon N. Separation of contributions of tryptophans and tyrosines to the ultraviolet circular dichroism spectrum of hen egg-white lysozyme. Eur J Biochem. 1970 Sep;16(1):55–59. doi: 10.1111/j.1432-1033.1970.tb01052.x. [DOI] [PubMed] [Google Scholar]
