Thermal denaturation of HRPA2: pH-dependent conformational changes

Enzyme and Microbial Technology

Volumn 40, Issue 4, 2007, Pages 696-703

  Carvalho, Ana Sofia L ^a   Ferreira, Bruno Sommer ^a   Neves Petersen, Maria Teresa ^b   Petersen, Steffen B ^b   Aires Barros, Maria Raquel ^a   Melo, Eduardo Pinho ^a,c  

^a INSTITUTO SUPERIOR TÉCNICO   (Portugal)

^b AALBORG UNIVERSITY   (Denmark)

^c UNIVERSITY OF ALGARVE   (Portugal)

Author keywords

Horseradish peroxidase A2; Isoenzymes; pH dependent stability; Thermal denaturation

Indexed keywords

HORSERADISH PEROXIDASE A2; ISOENZYMES; PH-DEPENDENT STABILITY; THERMAL DENATURATION;

CONFORMATIONS; DIFFERENTIAL SCANNING CALORIMETRY; FLUORESCENCE; PH EFFECTS; PROTEINS; THERMODYNAMIC STABILITY;

ENZYME KINETICS;

HEME; HORSERADISH PEROXIDASE; HORSERADISH PEROXIDASE A2; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; DIFFERENTIAL SCANNING CALORIMETRY; FLUORESCENCE; MOLECULAR PROBE; NONHUMAN; PH; PROTEIN CONFORMATION; PROTEIN MODIFICATION; PROTEIN STRUCTURE; THERMAL DENATURATION; THERMOSTABILITY; ULTRAVIOLET RADIATION;

ARMORACIA RUSTICANA;

EID: 33847263892     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2006.05.029     Document Type: Article

References (29)

1. Welinder K.G., Mauro J.M., and Norskov-Lauritsen L. Structure of plant and fungal peroxidases. Biochem Soc Trans 20 (1992) 337-340
2. Welinder K.G., Justesen A.F., Kjaersgard I.V., Jensen R.B., Rasmussen S.K., Jespersen H.M., et al. Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana. Eur J Biochem 269 (2002) 6063-6081
3. Tognolli M., Penel C., Greppin H., and Simon P. Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana. Gene 288 (2002) 129-138
4. Welinder K.G. Plant peroxidases: structure-function relationships. Plant Peroxidases 1989-1990 (1992), University of Geneva, Geneva p. 1-24
5. Veitch N.C., and Smith A.T. Horseradish peroxidase. Adv Inorg Chem 51 (2001) 107-162
6. Nielsen K.L., Indiani C., Henriksen A., Feis A., Becucci M., Gajhede M., et al. Differential activity and structure of highly similar peroxidases. spectroscopic, crystallographic, and enzymatic analyses of lignifying Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2. Biochemistry 40 (2001) 11013-11021
7. Carvalho A.S., Melo E.P., Ferreira B.S., Neves-Petersen M.T., Petersen S.B., and Aires-Barros M.R. Heme and pH-dependent stability of an anionic horseradish peroxidase. Arch Biochem Biophys 415 (2003) 257-267
8. Aibara S., Kobayashi T., and Morita Y. Isolation and properties of basic isoenzymes of horseradish peroxidase. J Biochem (Tokyo) 90 (1981) 489-496
9. Chattopadhyay K., and Mazumdar S. Structural and conformational stability of horseradish peroxidase: effect of temperature and pH. Biochemistry 39 (2000) 263-270
10. Gazaryan I.G., Chubar T.A., Ignatenko O.V., Mareeva E.A., Orlova M.A., Kapeliuch Y.L., et al. Tryptophanless recombinant horseradish peroxidase: stability and catalytic properties. Biochem Biophys Res Commun 262 (1999) 297-301
11. Huddleston S., Robertson S., Dobson C., Kwong Y.P., and Charalambous B.M. Structural and functional stability of horseradish peroxidase. Biochem Soc Trans 23 (1995) 108S
12. Morawski B., Quan S., and Arnold F.H. Functional expression and stabilization of horseradish peroxidase by directed evolution in Saccharomyces cerevisiae. Biotechnol Bioeng 76 (2001) 99-107
13. Tams J.W., and Welinder K.G. Glycosylation and thermodynamic versus kinetic stability of horseradish peroxidase. FEBS Lett 421 (1998) 234-236
14. Pina D.G., Shnyrova A.V., Gavilanes F., Rodriguez A., Leal F., Roig M.G., et al. Thermally induced conformational changes in horseradish peroxidase. Eur J Biochem 268 (2001) 120-126
15. 1H NMR studies on isoenzymes. Biochemistry 34 (1995) 13477-13484
16. Carvalho A.S., Santos A.M., Neves-Petersen M.T., Petersen S.B., Aires-Barros M.R., and Melo E.P. Conformational states of HRPA1 induced by thermal unfolding: effect of low molecular weight solutes. Biopolymers 75 (2004) 173-186
17. Shannon L.M., Kay E., and Lew J.Y. Peroxidase isozymes from horseradish roots. I. Isolation and physical properties. J Biol Chem 241 (1966) 2166-2172
18. Hiner A.N., Hernández-Ruíz J., Arnao M.B., García-Cánovas F., and Acosta M. A comparative study of the purity, enzyme activity, and inactivation by hydrogen peroxide of commercially available horseradish peroxidase isoenzymes A and C. Biotechnol Bioeng 50 (1996) 655-662
19. Strickland E.H., Kay E., Shannon L.M., and Horwitz J. Peroxidase isoenzymes from horseradish roots 3. Circular dichroism of isoenzymes and apoisoenzymes. J Biol Chem 243 (1968) 3560-3565
20. Kelly S.M., and Price N.C. The application of circular dichroism to studies of protein folding and unfolding. Biochim Biophys Acta 1338 (1997) 161-185
21. Smulevich G., Paoli M., De Sanctis G., Mantini A.R., Ascoli F., and Coletta M. Spectroscopic evidence for a conformational transition in horseradish peroxidase at very low pH. Biochemistry 36 (1997) 640-649
22. Schmid F.X. Optical spectroscopy to characterize protein conformation and conformational changes. Protein Structure. A Pratical Approach (1997), Oxford University Press Inc., Oxford p. 261-97
23. Freire E. Differential scanning calorimetry. Protein Stability and Folding. Theory and Practice (1995), Humana Press Inc., NJ p. 191-218
24. Lakowicz J.R. Energy transfer. Principles of Fluorescence Spectroscopy. 2nd ed. (1999), Kluwer Academic/Plenum Publishers, New York p. 367-94
25. Brunet J.E., Gonzalez G.A., and Sotomayor C.P. Intramolecular tryptophan heme energy transfer in horseradish peroxidase. Photochem Photobiol 38 (1983) 253-254
26. Gryczynski Z., Lubkowski J., and Bucci E. Heme-protein interactions in horse heart myoglobin at neutral pH and exposed to acid investigated by time-resolved fluorescence in the pico- to nanosecond time range. J Biol Chem 270 (1995) 19232-19237
27. Kamal J.K., and Behere D.V. Thermal and conformational stability of seed coat soybean peroxidase. Biochemistry 41 (2002) 9034-9042
28. Fersht A. Protein stability. Structure and mechanism in protein science: a guide to enzyme catalysis and protein folding (1999), W.H. Freeman and Company, New York p. 508-39
29. Howes B.D., Feis A., Indiani C., Marzocchi M.P., and Smulevich G. Formation of two types of low-spin heme in horseradish peroxidase isoenzyme A2 at low temperature. J Biol Inorg Chem 5 (2000) 227-235