The catalytic role of the distal site asparagine-histidine couple in catalase-peroxidases

European Journal of Biochemistry

Volumn 270, Issue 5, 2003, Pages 1006-1013

  Jakopitsch, Christa ^a   Auer, Markus ^a   Regelsberger, Günther ^a   Jantschko, Walter ^a   Furtmüller, Paul G ^a   Rüker, Florian ^b   Obinger, Christian ^a  

^a UNIVERSITY OF NATURAL RESOURCES AND LIFE SCIENCES   (Austria)

^b UNIVERSITY OF AGRICULTURAL SCIENCES   (Austria)

Author keywords

Catalase activity; Catalase peroxidase; Compound I; Peroxidase activity; Synechocystis PCC 6803

Indexed keywords

ACID; ASPARAGINE; BASE; CATALASE; CYANIDE; FERRIC ION; HISTIDINE; HYDROGEN PEROXIDE; PEROXIDASE;

ALKALINITY; ARTICLE; BINDING AFFINITY; CATALYST; CHEMICAL BOND; CHEMICAL REACTION; CYANOBACTERIUM; ENZYME ACTIVITY; ENZYME STRUCTURE; FLOW MEASUREMENT; HYDROGEN BOND; MOLECULAR DYNAMICS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; REACTION ANALYSIS; REDUCTION; STRUCTURE ACTIVITY RELATION; WILD TYPE;

AMINO ACID SEQUENCE; ASPARAGINE; BASE SEQUENCE; CATALASE; CATALYSIS; CYANIDES; DNA PRIMERS; HISTIDINE; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEROXIDASE; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROPHOTOMETRY, ULTRAVIOLET;

SYNECHOCYSTIS; SYNECHOCYSTIS SP. PCC 6803;

EID: 0037336945     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03476.x     Document Type: Article

References (23)

1. Welinder, K.G. (1992) Superfamily of plant, fungal and bacterial peroxidases. Curr. Opin. Struct. Biol. 2, 388-393.
2. Welinder, K.G. (1992) Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily. Biochim. Biophys. Acta 1080, 215-220.
3. Finzel, B.C., Poulos, T.L. & Kraut, J. (1984) Crystal structure of yeast cytochrome c peroxidase refined at 1.7-Å resolution. J. Biol. Chem. 259, 13027-13036.
4. Patterson, W.R. & Poulos, T.L. (1995) Crystal structure of recombinant pea cytosolic ascorbate peroxidase. Biochemistry 34, 4331-4341.
5. Yamada, Y., Fujiwara, T., Sato, T., Igarashi, N. & Tanaka, N. (2002) The 2.0 Å crystal structure of catalase-peroxidase from Haloarcula marismortui. Nat. Struct. Biol. 9, 691-695.
6. Obinger, C., Regelsberger, G., Strasser, G., Burner, U. & Peschek, G.A. (1997) Purification and characterization of a homodimeric catalase-peroxidase from the cyanobacterium Anacystis nidulans. Biochem. Biophys. Res. Commun. 235, 545-552.
7. Jakopitsch, C., Rüker, F., Regelsberger, G., Dockal, M., Peschek, G.A. & Obinger, C. (1999) Catalase-peroxidase from the cyanobacterium Synechocystis PCC 6803: cloning, overexpression in Escherichia coli, and kinetic characterization. Biol. Chem. 380, 1087-1096.
8. Engleder, M., Regelsberger, G., Jakopitsch, C., Furtmüller, P.G., Rüker, F., Peschek, G.A. & Obinger, C. (2000) Nucleotide sequence analysis, overexpression in Escherichia coli and kinetic characterization of Anacystis nidulans catalase-peroxidase. Biochimie 82, 211-219.
9. Dunford, H.B. (1999) Heme Peroxidases. Wiley-VCH, New York.
10. Sivaraja, M., Goodin, D.B., Smith, M. & Hoffman, B.M. (1989) Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES. Science 245, 738-740.
11. Hillar, A., Peters, B., Pauls, R., Loboda, A., Zhang, H., Mauk, A.G. & Loewen, P.C. (2000) Modulation of the activities of catalase-peroxidase HPI of Escherichia coli by site-directed mutagenesis. Biochemistry 39, 5868-5875.
12. Regelsberger, G., Jakopitsch, C., Furtmüller, P.G., Rüker, F., Switala, J., Loewen, P.C. & Obinger, C. (2001) The role of distal tryptophan in the bifunctional activity of catalase-peroxidases. Biochem. Soc. Trans. 29, 99-105.
13. Regelsberger, G., Jakopitsch, C., Rüker, F., Krois, D., Peschek, G.A. & Obinger, C. (2000) Effect of distal cavity mutations on the formation of compound I in catalase-peroxidases. J. Biol. Chem. 275, 22854-22861.
14. Satterlee, J.D., Alam, S.L., Mauro, J.M., Erman, J.E. & Poulos, T.L. (1994) The effect of the Asn82→Asp mutation in yeast cytochrome c peroxidase studied by proton NMR spectroscopy. Eur. J. Biochem. 224, 81-87.
15. Delauder, S.F., Mauro, J.M., Poulos, T.L., Williams, J.C. & Schwarz, F.P. (1994) Thermodynamics of hydrogen cyanide and hydrogen fluoride binding to cytochrome c peroxidase and its Asn-82→Asp mutant. Biochem. J. 302, 437-442.
16. Nagano, S., Tanaka, M., Ishimori, K., Watanabe, Y. & Morishima, I. (1996) Catalytic roles of the distal site asparagine-histidine couple in peroxidases. Biochemistry 35, 14251-14258.
17. Tanaka, M., Nagano, S., Ishimori, K. & Morishima, I. (1997) Hydrogen bond network in the distal site of peroxidases: spectroscopic properties of Asn70→Asphorseradish peroxidase mutant. Biochemistry 36, 9791-9798.
18. Poulos, T.L. & Kraut, J. (1980) The stereochemistry of peroxidase catalysis. J. Biol. Chem. 255, 8199-8205.
19. Heering, H.A., Indiani, C., Regelsberger, G., Jakopitsch, C., Obinger, C. & Smulevich, G. (2002) New insights into the heme cavity structure of catalase-peroxidase: a spectroscopic approach to the recombinant Synechocystis enzyme and selected distal cavity mutants. Biochemistry 41, 9237-9247.
20. Satterlee, J.D., Teske, J.G., Erman, J.E., Mauro, J.M. & Poulos, T.L. (2000) Temperature, pH, and solvent isotope effects on cytochrome c peroxidase mutant N82A studied by proton NMR. J. Protein Chem. 19, 535-542.
21. Nagano, S., Tanaka, M., Watanabe, Y. & Morishima, I. (1995) Putative hydrogen bond network in the heme distal site of horseradish peroxidase. Biochem. Biophys. Res. Commun. 207, 417-423.
22. Dunford, H.B. (1982) Horseradish peroxidase: structure and kinetic properties. In Peroxidases in Chemistry and Biology, Vol. II (Everse, J., Everse, K.E. & Grisham, M.B., eds), pp. 1-24. CRC Press, Boca Raton, Florida.
23. Jakopitsch, C., Regelsberger, G., Furtmüller, P.G., Rüker, F., Peschek, G.A. & Obinger, C. (2002) Engineering the proximal heme cavity of catalase-peroxidase. J. Inorg. Biochem. 91, 78-86.