Porphyrin-induced protein structural alterations of heme enzymes
Some alterations in the protein structure of d-aminolevulinic acid dehydratase (ALA-D) and porphobilinogen deaminase (PBG-D) induced by uroporphyrin (URO) and prototoporphyrin (PROTO) have been observed previously. To obtain further evidence of these phenomena, the absorption and fluorescence spectr...
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| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
1997
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 11186caa a22010817a 4500 | ||
|---|---|---|---|
| 001 | PAPER-20048 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518205126.0 | ||
| 008 | 190411s1997 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0342601352 | |
| 024 | 7 | |2 cas |a Amino Acids; Heme, 14875-96-8; Hydroxymethylbilane Synthase, EC 2.5.1.61; Porphobilinogen Synthase, EC 4.2.1.24; Porphyrins; protoporphyrin IX, 553-12-8; Protoporphyrins; Sulfhydryl Compounds; uroporphyrin I, 607-14-7; Uroporphyrins | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a IJBBF | ||
| 100 | 1 | |a Afonso, S.G. | |
| 245 | 1 | 0 | |a Porphyrin-induced protein structural alterations of heme enzymes |
| 260 | |c 1997 | ||
| 270 | 1 | 0 | |m Enriquez De Salamanca, R.Francisco Gervas 9, 28020 Madrid, Spain |
| 506 | |2 openaire |e Política editorial | ||
| 504 | |a Afonso, S., Chinarro, S., Muñoz, J., Salamanca, R.E., Batlle, A., Light-dependent and light-independent inactivation of red cell porphobilinogenase by type I and III porphyrins (1987) Bolletino Istituto Dermatologico San Gallicano, 13, pp. 35-40 | ||
| 504 | |a Afonso, S., Chinarro, S., Muñoz, J., Salamanca, R.E., Batlle, A., Photodynamic and non-photodynamic action of several porphyrins on the activity of some heme-enzymes (1990) Journal of Enzyme Inhibition, 3, pp. 303-310 | ||
| 504 | |a Afonso, S., Chinarro, S., Salamanca, R.E., Batlle, A., Further evidence on the photodynamic and the novel non-photodynamic inactivation of uroporphyrinogen decarboxylase by uroporphyrin I (1991) Journal of Enzyme Inhibition, 5, pp. 225-233 | ||
| 504 | |a Afonso, S., Chinarro, S., Salamanca, R.E., Batlle, A., δ-aminolevulinic acid dehydratase inactivation by uroporphyrin i in light and darkness (1994) International Journal of Biochemistry, 26, pp. 255-258 | ||
| 504 | |a Afonso, S.G., Polo, C.F., Enríquez de Salamanca, R., Batlle, A., Mechanistic studies on URO I-induced enzyme photoinactivation (1996) International Journal of Biochemistry and Cell Biology, 28, pp. 415-420 | ||
| 504 | |a Afonso, S., Salamanca, R.E., Batlle, A., Folding and unfolding of δ-aminolevulinic acid dehydratase and porphobilinogen deaminase induced by Uro and Protoporphyrin (1997) International Journal of Biochemistry and Cell Biology, 29, pp. 493-503 | ||
| 504 | |a Batlle, A.M.D.C., Salamanca, R.E., Chinarro, S., Afonso, S., Stella, A.M., Photodynamic inactivation of red cell uroporphyrinogen decarboxylase by porphyrins (1986) International Journal of Biochemistry, 18, pp. 143-147 | ||
| 504 | |a Bodaness, S.R., The nonphotosensitized potentiation by the photosensitizer hematoporphyrin of the horse-radish peroxidase-catalyzed hydrogen peroxide-mediated oxidation of NADPH to NADP + (1984) Biochemical and Biophysical Research Communications, 118, pp. 191-197 | ||
| 504 | |a Brun, A., Sandberg, S., Photodynamic release of proto-porphyrin from intact erythrocytes in erythropoietic protoporphyrin: The effect of small repetitive light doses (1985) Photochemistry and Photobiology, 41, pp. 535-541 | ||
| 504 | |a Chinarro, S., Afonso, S., Stella, A.M., Salamanca, R.E., Battle, A., Acción fotodinámica de las porfirinas sobre la actividad de la uroporfirinogeno decarboxilasa eritrocitaria (1985) Biometrica, 10, pp. 75-80 | ||
| 504 | |a Dubbelman, T.M.A.R., De Goeij, A.F.P.M., Van Steveninck, J., Photodynamic effect of protoporphyrin on human erythrocytes. Nature of the cross-linking of membrane proteins (1978) Biochimica et Biophysica Acta, 511, pp. 141-151 | ||
| 504 | |a Firey, P.A., Rodgers, M.J.A., Photochemical properties of erythrocyte ghosts containing porphyrin (1988) Photochemistry and Photobiology, 47, pp. 615-619 | ||
| 504 | |a Habeeb, A.F.S., Reaction of protein sulfhydryl groups with Ellman's reagent (1972) Methods in Enzymology, 25, pp. 457-464. , Edited by Colowick S. and Kaplan N., Academic Press, New York | ||
| 504 | |a Ignarro, L.J., Wood, K.S., Wolin, M.S., Activation of purified soluble guanylate cyclase by protoporphyrin IX (1982) Proceedings of the National Academy of Sciences U.S.A., 70, pp. 2870-2873 | ||
| 504 | |a Lim, H.W., Gigli, I., Wasserman, S.I., Differential effects of protoporphyrin and uroporphyrin on murine mast cells (1987) Journal of Investigative Dermatology, 88, pp. 281-286 | ||
| 504 | |a Lowry, O.H., Rosebrough, N.J., Farr, A.O., Randall, R.J., Protein measurement with the folin phenol reagent (1951) Journal of Biological Chemistry, 193, pp. 265-275 | ||
| 504 | |a Magnus, I., Porter, A.D., Rimington, C., The action spectrum for skin lesions in porphyria cutanea tarda (1959) Lancet, 1, pp. 912-914 | ||
| 504 | |a Moan, J., The photochemical yield of singlet oxygen from porphyrins in different states of aggregation (1984) Photochemistry and Photobiology, 39, pp. 445-449 | ||
| 504 | |a Sandberg, S., Brun, A., Light-induced protoporphyrin release from erythrocytes in erythropoietic protoporphyria (1982) Journal of Clinical Investigation, 70, pp. 693-698 | ||
| 504 | |a Spikes, J.D., Porphyrins and related compounds as photodynamic sensitizers (1975) Annals of the New York Academy of Science, 244, pp. 496-508 | ||
| 504 | |a Spikes, J.D., A preliminary comparisson of the photosensitizing properties of porphyrins in aqueous solution and liposomal systems (1983) Advances in Experimental Medicine and Biology, 60, pp. 180-192 | ||
| 504 | |a Udenfriend, S., Stein, S., Bohlen, P., Dalrman, W., Fluorescamine: A reagent for assay of aminoacids, peptides, proteins and primary amines in the picomole range (1972) Science, 178, pp. 871-872 | ||
| 504 | |a Van Steveninck, J., Dubbelman, T.M.A.R., Verweij, H., Photodynamic membrane damage (1983) Porphyrin Photosensitization, pp. 2227-2240. , Plenum Press, New York | ||
| 504 | |a Van Steveninck, J., Boegheim, J.P.J., Dubbelman, T.M.A.R., Van der Zee, J., The influence of porphyrins on iron-catalyzed generation of hydroxyl radicals (1988) Biochemical Journal, 250, pp. 197-201 | ||
| 504 | |a Varigos, G., Schiltz, J.R., Bickers, D.R., Uroporphyrin I stimulation of collagen biosynthesis in human skin fibroblasts (1982) Journal of Clinical Investigation, 69, pp. 129-135 | ||
| 504 | |a Verweij, H., Van Steveninck, J., Model studies on photodynamic cross-linking (1982) Photochemistry and Photobiology, 35, pp. 265-267 | ||
| 504 | |a Verweij, H., Dubbelman, T.M.A.R., Van Steveninck, J., Photodynamic protein cross-linking (1981) Biochimica et Biophysica Acta, 647, pp. 87-94 | ||
| 504 | |a Vincent, S.H., Holeman, B., Cully, B.C., Müller-Eberhard, U., Porphyrin-induced photodynamic cross-linking of hepatic heme-binding proteins (1986) Life Sciences, 38, pp. 365-372 | ||
| 520 | 3 | |a Some alterations in the protein structure of d-aminolevulinic acid dehydratase (ALA-D) and porphobilinogen deaminase (PBG-D) induced by uroporphyrin (URO) and prototoporphyrin (PROTO) have been observed previously. To obtain further evidence of these phenomena, the absorption and fluorescence spectra of ALA-D and PBG-D and the total protein content of sulfhydryl and free amino groups were analyzed after exposure of the enzymes to URO I and PROTO IX. ALA-D and PBG-D were partially purified from bovine liver and exposed to URO I or PROTO IX, both in the dark and under UV light. All experiments were performed in the enzyme solutions after removing the porphyrins. Absorbance spectra changes in the region of 220-300 nm were registered, indicating the interaction of the porphyrins with the molecular structure of the enzymes. The main changes in the fluorescence spectra were observed in the spectral region of 555 nm, and only slight modifications in the spectral region of 340-360 nm; moreover, alterations were stronger upon UV irradiation and in the presence of URO P when compared with darkness and PROTO IX. Variations in total SH groups would suggest the formation of disulfur bridges induced by URO I and the rupture of some SS groups induced by PROTO IX. The effect of porphyrins on free amino groups would reflect a combination of cross-linking and fragmentation of proteins. Structural changes were observed when the enzymes were exposed to the porphyrin both in the dark or under UV light; however, they were stronger in tile latter condition. These results suggest that porphyrins per se could act directly on the protein structure and that this action would be enhanced upon UV irradiation. |l eng | |
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas, 93/112 | ||
| 536 | |a Detalles de la financiación: Directorate-General XII, Science, Research, and Development | ||
| 536 | |a Detalles de la financiación: Acknowledgements-Susana Afonso thanks the Directorate General for Science, Research and Development at the Commission of the European Communities, Belgium, for a post-doctoral fellowship. This work was supported by grants from the CONICET, Argentine and FISss (93/112) from Spain. A. Batlle is also grateful to the Ministerio de Educacibn y Ciencia (MEC), Spain, for special help. | ||
| 593 | |a Ctro. de Invest. Sobre Porfirinas P., Fac. de Cie. Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina | ||
| 593 | |a Unidad de Porfirias, Hospital Universitario 12 de Octubre, Universidad Complutense de Madrid, Madrid, Spain | ||
| 593 | |a Francisco Gervas, 9 11o A, 28020 Madrid, Spain | ||
| 690 | 1 | 0 | |a ENZGME STRUCTURE |
| 690 | 1 | 0 | |a MOLECULAR ALTERATIONS |
| 690 | 1 | 0 | |a PHOTODYNAMIC ACTION |
| 690 | 1 | 0 | |a PORPHYRINS |
| 690 | 1 | 0 | |a AMINOLEVULINIC ACID |
| 690 | 1 | 0 | |a HEME |
| 690 | 1 | 0 | |a PORPHYRIN |
| 690 | 1 | 0 | |a PROTOPORPHYRIN |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CHEMICAL STRUCTURE |
| 690 | 1 | 0 | |a CONTROLLED STUDY |
| 690 | 1 | 0 | |a ENZYME STRUCTURE |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PHOTODYNAMICS |
| 690 | 1 | 0 | |a PROTEIN STRUCTURE |
| 690 | 1 | 0 | |a AMINO ACIDS |
| 690 | 1 | 0 | |a ANIMALS |
| 690 | 1 | 0 | |a CATTLE |
| 690 | 1 | 0 | |a HEME |
| 690 | 1 | 0 | |a HYDROXYMETHYLBILANE SYNTHASE |
| 690 | 1 | 0 | |a LIVER |
| 690 | 1 | 0 | |a PORPHOBILINOGEN SYNTHASE |
| 690 | 1 | 0 | |a PORPHYRINS |
| 690 | 1 | 0 | |a PROTOPORPHYRINS |
| 690 | 1 | 0 | |a SPECTROMETRY, FLUORESCENCE |
| 690 | 1 | 0 | |a SPECTROPHOTOMETRY |
| 690 | 1 | 0 | |a SULFHYDRYL COMPOUNDS |
| 690 | 1 | 0 | |a ULTRAVIOLET RAYS |
| 690 | 1 | 0 | |a UROPORPHYRINS |
| 690 | 1 | 0 | |a BOVINAE |
| 700 | 1 | |a De Salamanca, R.E. | |
| 700 | 1 | |a Batlle, A.M.D.C. | |
| 773 | 0 | |d 1997 |g v. 29 |h pp. 1113-1121 |k n. 8-9 |p INT. J. BIOCHEM. CELL BIOL. |x 13572725 |w (AR-BaUEN)CENRE-5218 |t International Journal of Biochemistry and Cell Biology | |
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| 856 | 4 | 0 | |u https://doi.org/10.1016/S1357-2725(97)00045-9 |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_13572725_v29_n8-9_p1113_Afonso |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13572725_v29_n8-9_p1113_Afonso |y Registro en la Biblioteca Digital |
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