Site-directed mutagenesis of a possible type I copper ligand of bilirubin oxidase; a Met467Gln mutant shows stellacyanin-like properties

Journal of Biochemistry

Volumn 125, Issue 4, 1999, Pages 662-668

  Shimizu, Atsushi ^a   Sasaki, Takashi ^a   Kwon, Jung Hee ^a   Odaka, Akito ^a   Satoh, Takanori ^a   Sakurai, Nobuhiko ^b,c   Sakurai, Takeshi ^b,c   Yamaguchi, Shotaro ^d   Samejima, Tatsuya ^a  

^a AOYAMA GAKUIN UNIVERSITY   (Japan)

^b KANAZAWA UNIVERSITY   (Japan)

^c INSTITUTE FOR MOLECULAR SCIENCE   (Japan)

^d Amano Enzyme Inc   (Japan)

Author keywords

Blue copper protein; ESR; Multicopper oxidase; Site directed mutagenesis; Stellacyanin

Indexed keywords

BILIRUBIN; COPPER; GLUTAMINE; LIGAND; METHIONINE; OXIDOREDUCTASE;

ABSORPTION SPECTROSCOPY; AMINO ACID SUBSTITUTION; ARTICLE; ELECTRON SPIN RESONANCE; NONHUMAN; SITE DIRECTED MUTAGENESIS;

MYROTHECIUM VERRUCARIA; VERRUCARIA;

EID: 0032931026     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022334     Document Type: Article

References (29)

1. Tanaka, N. and Murao, S. (1985) Reaction of bilirubin oxidase produced by Myrothecium verrucaria MT-1. Agric. Biol. Chem. 49, 843-844
2. Adman, E.T. (1991) Copper protein structure. Adv. Protein Chem. 42, 145-197
3. 15N-labeled plastocyanin. J. Am. Chem. Soc. 117, 6443-6446
4. Ducos, V., Brzowski, A.M., Wilson, K.S., Brown, S.H., Ostergaard, P., Schneider, P., Yaver, D.S., Pedersen, A.H., and Davies, G.J. (1998) Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 A resolution. Nat. Struct. Biol. 5, 310-316
5. Messerschmidt, A., Ladenstein, R., and Huber, R. (1992) Refined crystal structure of ascorbate oxidase at 1.9 A resolution. J. Mol. Biol. 224, 179-205
6. Zaitseva, I., Zaitsev, V., Card, G., Moshkov, K., Bax, B., Ralph, A., and Lindley, P. (1996) The X-ray structure of human serum cemloplasmin at 3.1 A: nature of the copper center. J. Biol. Inorg. Chem. 1, 15-23
7. Strange, R.W., Reinhammar, B., Murphy, L.M., and Hasnain, S.S. (1995) Structural and spectroscopic studies of the copper site of stellacyanin. Biochemistry 34, 220-231
8. Schinina, M.E., Maritano, S., Barra, D., Mondovi, B., and Marchesini, A. (1996) Mavicyanin, a stellacyanin-like protein from zucchini peelings: primary structure and comparison with other cupredoxins. Biochim. Biophys. Acta 1297, 28-32
9. van Driessche, G., Dennison, C., Sykes, A.G., and van Beeumen, J. (1995) Heterogeneity of the covalent structure of the blue copper protein umecyanin from horseradish roots. Protein Sci. 4, 209-227
10. Chang, T.K., Iverson, S.A., Rodrigues, C.G., Kiser, C.N., Lew, A.Y.C., Germanas, J.P., and Richards, J.H. (1991) Gene synthesis expression, and mutagenesis of the blue copper proteins azurin and plastocyanin. Proc. Natl. Acad. Sci. USA 88, 1325-1329
11. Hibino, T., Lee, B.H., and Takabe, T. (1995) Expression and characterization of Met92Gln mutant plastocyanin from Silence pratensis. J. Biochem. 117, 101-106
12. Kroes, S.J., Hoitink, C.W.G., Andrew, C.R., Ai, J., Sanders-Loehr, J., Messerschmidt, A., Hagen, W.R., and Canters, G.W. ( 1996) The mutation Met121-His create a type-1.5 copper site in Alcaligenes denitriftcans azurin. Eur. J. Biochem. 240, 342-351
13. Koikeda, S., Ando, K., Kaji, H., Inoue, T., Murao, S., Takeuchi, K., and Samejima, T. (1993) Molecular cloning of the gene for bilirubin oxidase from Myrothecium verrucaria and its expression in yeast. J. Biol. Chem. 268, 18801-18809
14. Shimizu, A., Kwon, J.-H., Sasaki, T., Satoh, S., Sakurai, N., Sakurai, T., Yamaguchi, S., and Samejima, T. (1999) Myrothecium verrucaria bilirubin oxidase and its mutants for potential copper-ligands. Biochemistry 38, 3034-3042
15. Yamaguchi, S., Takeuchi, K., Mase, T., and Matsuura, A. (1997) Efficient expression of mono-and diacylglycerol lipase gene from Penicillium camembertii U-150 in Aspergillus oryzae under the control of its own promoter. Biosci. Biotech. Biochem. 61, 800-805
16. Higuchi, R., Krummel, B., and Saiki, R.K. (1988) A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res. 16, 7351-7367
17. Hanahan, D. (1983) Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166, 557-580
18. Unkles, S.E., Campbell, E.I., Carrez, D., Grieve, C., Contreras, R., Fiers, W., Van den Hondel, C.A., and Kinghorn, J.R. (1989) Transformation of Aspergillus niger with the homologous nitrate reductase gene. Gene 78, 157-166
19. Romero, A., Hoitink, C.W., Nar, H., Huber, R., Messerschmidt, A., and Canters, G.W. (1993) X-ray analysis and spectroscopic characterization of M121Q azurin (A Copper Site Model for Stellacyanin). J. Mol. Biol. 229, 1007-1021
20. Hibino, T., Lee, B.H., and Takabe, T. (1995) Expression and characterization of Met92Gln mutant plastocyanin from Silence pratensis. J. Biochem. 117, 101-106
21. Kataoka, K., Nakai, M., Yamaguchi, K., and Suzuki, S. (1998) Gene synthesis, expression, and mutagenesis of zucchini mavicyanin: the fourth ligand of blue copper center is Gln. Biochem. Biophys. Res. Commun. 250, 409-413
22. Strange, R.W., Reinhammar, B., Murphy, L.M., and Hasnain, S.S. (1995) Structural and spectroscopic studies of the copper site of stellacyanin. Biochemistry 34, 220-231
23. 15N nuclear magnetic resonance assignments, secondary structure in solution, and solvent exchange properties of azurin from Alcaligenes denitrificans. Biochemistry 33, 3560-3571
24. Marks, R.H. and Miller, R.D. (1979) A kinetic study of the reconstitution of azurin from Cu(II) and the apoprotein. Arch. Biochem. Biophys. 195, 103-111
25. Morpurgo, L., Hartmann, H.J., Desideri, A., Weser, U., and Rotilio, G. (1983) Yeast copper-thionein can reconstitute the Japanese-lacquer-tree (Rhus vernicifera) laccase from the Type 2-copper-depleted enzyme via a direct copper(I)-transfer mechanism. Biochem. J. 211, 515-517
26. Gewirth, A.A. and Solomon, E.I. (1988) Electronic structure of plastcyanin: excited state spectral features. J. Am. Chem. Soc. 110, 3811-3819
27. Sakurai, T. and Takahashi, J. (1995) EPR spectra of type 3 coppers in Rhus vernicifera laccase and Cucumis sativus ascorbate oxidase. Biochem. Biophys. Acta 1248, 143-148
28. Murphy, M.E., Turley, S., Kukimoto, M., Nishiyama, M., Horinouchi, S., Sasaki, H., Tanokura, M., and Adman, E.T. (1995) Structure of Alcaligenes faecalis nitrite reductase and a copper site mutant, M150E, that contains zinc. Biochemistry 34, 12107-12117
29. Nar, H., Huber, R., Messerschmidt, A., Filippou, A.C., Barth, M., Jaquinod, M., van de Kamp, M., and Canters, G.W. (1992) Characterization and crystal structure of zinc azurin, a by-product of heterologous expression in Escherichia coli of Pseudomonas aeruginosa copper azurin. Eur. J. Biochem. 205, 1123-1129