Porphyrin-substrate binding to murine ferrochelatase: Effect on the thermal stability of the enzyme

Biochemical Journal

Volumn 386, Issue 3, 2005, Pages 599-605

  Franco, Ricardo ^a   Bai, Guangyue ^b   Prosinecki, Vesna ^a   Abrunhosa, Filipa ^b   Ferreira, Gloria C ^c,d   Bastos, Margarida ^b  

^a INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA   (Portugal)

^b UNIVERSITY OF PORTO   (Portugal)

^c UNIVERSITY OF SOUTH FLORIDA   (United States)

^d H LEE MOFFITT CANCER CENTER AND RESEARCH INSTITUTE   (United States)

Author keywords

Differential scanning calorimetry; Ferrochelatase; Haem biosynthesis; Isothermal titration calorimetry; Porphyrin; Thermal stability

Indexed keywords

CALORIMETRY; CATALYSTS; CHELATION; CHEMICAL BONDS; ENZYMES; MONOMERS; STOICHIOMETRY; SUBSTRATES; THERMODYNAMIC STABILITY; TITRATION;

EXOTHERMIC REACTIONS; FERROCHELATASE; ISOTHERMAL TITRATION CALORIMETRY; PORPHYRIN-SUBSTRATES BINDING;

PORPHYRINS;

ALANINE; CATALASE; GLUTAMIC ACID; GLUTAMINE; MESOPORPHYRIN; PORPHYRIN; PROTOPORPHYRIN;

ARTICLE; CATALYSIS; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; ENERGY TRANSFER; ENTHALPY; ENZYME ACTIVE SITE; ENZYME STABILITY; HEME SYNTHESIS; IRON CHELATION; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTON TRANSPORT; STOICHIOMETRY; THERMODYNAMICS; THERMOSTABILITY;

ANIMALS; BACILLUS SUBTILIS; BINDING SITES; BUFFERS; CALORIMETRY, DIFFERENTIAL SCANNING; ENZYME STABILITY; FERROCHELATASE; GLUTAMIC ACID; HYDROGEN BONDING; MESOPORPHYRINS; MICE; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTONS; PROTOPORPHYRINS; SUBSTRATE SPECIFICITY; TEMPERATURE; THERMODYNAMICS;

MURINAE;

EID: 15944423583     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040921     Document Type: Article

References (47)

1. Franco, R., Lloyd, S. G., Moura, J. J. G., Moura, I., Huynh, B. H. and Ferreira, G. C. (1999) Ferrochelatase: a new iron-sulfur center-containing enzyme. In Iron Metabolism: Inorganic Biochemistry and Regulatory Mechanisms (Ferreira, G. C., Franco, R. and Moura, J. J. G., eds.), pp. 35-50, Wiley-VCH, Weinheim
2. Dailey, H. A., Dailey, T. A., Wu, C. K., Medlock, A. E., Wang, K. F., Rose, J. P. and Wang, B. C. (2000) Ferrochelatase at the millennium: structures, mechanisms and [2Fe-2S] clusters. Cell. Mol. Life Sci. 57, 1909-1926
3. Deybach, J. C. (2001) Porphyria. Painful photosensitivity. Lancet 358 (suppl.), S49
4. Al-Karadaghi, S., Hansson, M., Nikonov, S., Jonsson, B. and Hederstedt, L. (1997) Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis. Structure (London) 5, 1501-1510
5. Lecerof, D., Fodje, M., Hansson, A., Hansson, M. and Al-Karadaghi, S. (2000) Structural and mechanistic basis of porphyrin metallation by ferrochelatase. J. Mol. Biol. 297, 221-232
6. Karlberg, T., Lecerof, D., Gora, M., Silvegren, G., Labbe-Bois, R., Hansson, M. and Al-Karadaghi, S, (2002) Metal binding to Saccharomyces cerevisiae ferrochelatase. Biochemistry 41, 13499-13506
7. Wu, C.-K., Dailey, H. A., Rose, J. P., Burden, A., Sellers, V. M. and Wang, B.-C. (2001) The 2.0 A° structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. Nat. Struct. Biol. 8, 156-160
8. Gora, M., Rytka, J. and Labbe-Bois, R. (1999) Activity and cellular-location in Saccharomyces cerevisiae of chimeric mouse/yeast and Bacillus subtilis/yeast ferrochelatases. Arch. Biochem. Biophys. 361, 231-240
9. Medlock, A. E. and Dailey, H. A. (2000) Examination of the activity of carboxyl-terminal chimeric constructs of human and yeast ferrochelatases. Biochemistry 39, 7461-7467
10. Dailey, T. A. and Dailey, H. A. (2002) Identification of [2Fe-2S] clusters in microbial ferrochelatases. J. Bacteriol. 184, 2460-2464
11. Ferreira, G. C., Franco, R., Lloyd, S. G., Pereira, A. S., Moura, L., Moura, J. J. G. and Huynh, B. H. (1994) Mammalian ferrochelatase, a new addition to the metalloenzyme family. J. Biol. Chem. 269, 7062-7065
12. Dailey, H. A., Finnegan, M. G. and Johnson, M. K. (1994) Human ferrochelatase is an iron-sulfur protein. Biochemistry 33, 403-407
13. Franco, R., Ma, J.-G., Lu, Y., Ferreira, G. C. and Shelnutt, J. A. (2000) Porphyrin interactions with wild-type and mutant mouse ferrochelatase. Biochemistry 39, 2517-2529
14. Blackwood, M. E., Rush, T. S., Medlock, A., Dailey, H. A. and Spiro, T. G. (1997) Resonance Raman spectra of ferrochelatase reveal porphyrin distortion upon metal binding. J. Am. Chem. Soc. 119, 12170-12174
15. Blackwood, M. E., Rush, T. S., Rosenberg, F., Schultz, P. G. and Spiro, T. G. (1998) Alternative modes of substrate distortion in enzyme and antibody catalyzed ferrochelation reactions. Biochemistry 37, 779-782
16. Lu, Y., Sousa, A., Franco, R., Mangravita, A., Ferreira, G. C., Moura, I. and Shelnutt, J. A. (2002) Binding of protoporphyrin IX and metal derivatives to the active site of wild-type mouse ferrochelatase at low porphyrin-to-protein ratios. Biochemistry 41, 8253-8262
17. Franco, R., Pereira, A. S., Tavares, P., Mangravita, A., Barber, M. J., Moura, I. and Ferreira, G. C. (2001) Substitution of murine ferrochelatase glutamate-287 with glutamine or alanine leads to porphyrin-bound variants. Biochem. J. 356, 217-222
18. Ferreira, G. C. (1994) Mammalian ferrochelatase, overexpression in Escherichia coli as a soluble protein, purification and characterization. J. Biol. Chem. 269, 4396-4400
19. Bhairi, S. M. (2001) A Guide to the Properties and Uses of Detergents in Biological Systems. Calbiochem-Novabiochem, San Diego, U.S.A.
20. Laemmli, U. K. (1970) Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature (London) 227, 680-685
21. Franco, R., Moura, J. J. G., Moura, I., Lloyd, S. G., Huynh, B. H., Forbes, W. S. and Ferreira, G. C. (1995) Characterization of the iron-binding site in mammalian ferrochelatase by kinetic and Mössbauer methods. J. Biol. Chem. 270, 26352-26357
22. Lumry, R. and Biltonen, R. (1966) Validity of the 'two-state' hypothesis for conformational transitions of proteins. Biopolymers 4, 917-944
23. Freire, E. (1995) Thermal denaturation methods in the study of protein unfolding. Methods Enzymol. 259, 144-168
24. Bäckman, P., Bastos, M., Hallén, D., Lönnbro, P. and Wadsö, I. (1994) Heat conduction calorimeters: time constants, sensitivity and fast titration experiments. J. Biochem. Biophys. Meth. 28, 85-100
25. Bastos, M., Afonso, M., Caçote, M. H. M. and Ramos, M. J. (1997) Interactions in the model system α-cyclodextrin-glycerol. Experimental and theoretical study. J. Chem. Soc. Faraday Trans. 93, 2061-2067
26. Briggner, L-E. and Wadsö, I. (1991) Test and calibration processes for microcalorimeters, with special reference to heat conduction instruments used with aqueous systems. J. Biochem. Biophys. Meth. 22, 101-118
27. Eftink, M. and Biltonen, R. (1980) Thermodynamics of interacting biological systems. In Biological Microcalorimetry (Beezer, A. E., ed.), pp. 343-412, Academic Press, San Diego
28. Baker, B. M. and Murphy, K. P. (1996) Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry Biophys. J. 71, 2049-2055
29. Sanchez-Ruiz, J. M. (1992) Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys. J. 61, 921-935
30. 2+ on the thermal denaturation of carboxypeptidase B. Biochemistry 30, 2067-2072
31. Thórólfsoon, M., Ibarra-Molero, B., Fojan, P, Petersen, S. B., Sanchez-Ruiz, J. M. and Martínez, A. (2002) L-Phenylalanine binding and domain organization in human phenylalanine hydroxylase: a differential scanning calorimetry study. Biochemistry 41, 7573-7585
32. Vogl, T, Jatzke, C. and Hinz, H.-J. (1997) Thermodynamic stability of Annexin V E17G: equilibrium parameters from an irreversible unfolding reaction. Biochemistry 36, 1657-1668
33. Lumry, R. and Eyring, H. (1954) Conformation changes of proteins. J. Phys. Chem. 58, 110-120
34. Galisteo, M. L., Mateo, P. L. and Sanchez-Ruiz, J. M. (1991) Kinetic study on the irreversible thermal denaturation of yeast phosphoglycerate kinase. Biochemistry 30, 2061-2066
35. Freire, E., van Osdol, W. W., Mayorga, O. L. and Sanchez-Ruiz, J. M. (1990) Calorimetrically determined dynamics of complex unfolding transitions in proteins. Annu. Rev. Biophys. Biophys. Chem. 19, 159-188
36. Hernandez-Arana, A., Rojo-Dominguez, A., Altamirano, M. M. and Calcagno, M. L. (1993) Differential scanning calorimetry of the irreversible denaturation of Escherichia coli glucosamine-6-phosphate deaminase. denaturation of Escherichia coli glucosamine-6-phosphate deaminase. Biochemistry 32, 3644-3648
37. Wu, M. L. and Morgan, W. T. (1993) Characterization of hemopexin and its interaction with heme by differential scanning calorimetry and circular dichroism. Biochemistry 32, 7216-7222
38. Waldron, T. T. and Murphy, K. P. (2003) Stabilization of proteins by ligand binding: application to drug screening and determination of unfolding energetics. Biochemistry 42, 5058-5064
39. Srinivas, V. R., Singha, N. C., Schwarz, F. P. and Surolia, A. (1998) Differential scanning calorimetric studies of the glycoprotein, winged bean acidic lectin, isolated from the seeds of Psophocarpus tetrogonolobus. FEBS Lett. 425, 57-60
40. Privalov, G. P. and Privalov, P. L. (2000) Problems and prospects in microcalorimetry of biological macromolecules. Methods Enzymol. 323, 31-63
41. Carra, J. H., Anderson, E. A. and Privalov, P L. (1994) Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants. Biochemistry 33, 10842-10850
42. Freire, E., Mayorga, O. L. and Straume, M. (1990) Isothermal titration calorimetry. Anal. Chem. 62, A950-A959
43. Menze, M. A., Hellmann, N., Decker, H. and Grieshaber, M. K. (2000) Binding of urate and caffeine to hemocyanin of the lobster Homarus vulgaris (E.) as studied by isothermal titration calorimetry. Biochemistry 39, 10806-10811
44. Goldberg, R. N., Kishore, N. and Lennen, R. M. (2002) Thermodynamic quantities for the ionization reactions of buffers. J. Phys. Chem. Ref. Data 31, 231-370
45. Baker, B. M. and Murphy, K. P. (1997) Dissecting the energetics of a protein-protein interaction: the binding of ovomucoid third domain to elastase. J. Mol. Biol. 268, 557-569
46. Guzmán-Casado, M., Sánchez-Ruiz, J. M., El Harraus, M., Giménez-Gallego, G. and Parrody-Morreale, A. (2000) Energetics of myo-inositol hexasulphate binding to human acidic fibroblast growth factor. Effect of ionic strength and temperature. Eur. J. Biochem. 267, 3477-3486
47. Shi, I. and Ferreira, G. C. (2004) Probing the active site loop motif of murine ferrochelatase by random mutagenesis. J. Biol. Chem. 279, 19977-19986