Crystal structures of cyanide- and triiodide-bound forms of Arthromyces ramosus peroxidase at different pH values: Perturbations of active site residues and their implication in enzyme catalysis

Journal of Biological Chemistry

Volumn 270, Issue 37, 1995, Pages 21884-21892

  Fukuyama, Keiichi ^a   Kunishima, Naoki ^a,b   Amada, Fumiko ^a   Kubota, Tomomi ^a,c   Matsubara, Hiroshi ^a,d  

^a OSAKA UNIVERSITY   (Japan)

^b BIOMOL ENG RESEARCH INSTITUTE   (Japan)

^c NATL INST BIOSCI HUM TECHNOL   (Japan)

^d OKAYAMA UNIVERSITY OF SCIENCE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CYANIDE; CYTOCHROME C PEROXIDASE; HEME; HISTIDINE; IODINE DERIVATIVE; PEROXIDASE;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME STRUCTURE; HYDROGEN BOND; NONHUMAN; PH; PRIORITY JOURNAL; PROTON TRANSPORT; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ARGININE; BINDING SITES; COMPUTER GRAPHICS; CRYSTALLOGRAPHY, X-RAY; FOURIER ANALYSIS; HEME; HISTIDINE; HYDROGEN-ION CONCENTRATION; IODIDES; MITOSPORIC FUNGI; MODELS, MOLECULAR; PERIODIC ACID; PEROXIDASES; POTASSIUM COMPOUNDS; POTASSIUM CYANIDE; SUPPORT, NON-U.S. GOV'T;

EID: 0029129561     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.270.37.21884     Document Type: Article

References (38)

1. Akimoto, K., Shinmen, Y., Sumida, M., Asami, S., Amachi, T., Yoshizumi, H., Saeki, Y., Shimizu, S., and Yamada, H. (1990) Anal. Biochem. 189, 182-185
2. Allain, C. C., Poon, L. S., Chan, C. S. G., Richmond, W., and Fu, P. C. (1974) Clin. Chem. 20, 470-475
3. Banci, L., Bertini, I., Turano, P., Tien, M., and Kirk, T. K. (1991) Proc. Natl. Acad. Sci. U. S.A. 88, 6956-6960
4. Baunsgaard, L., Dalbøge, H., Houen, G., Rasmussen, E. M., and Welinder, K. G. (1993) Eur. J. Biochem. 213, 605-611
5. Brünger, A. T. (1992) XPLOR 3.0, Yale University, New Haven, CT
6. Brünger, A. T., Krukowski, A., and Erickson, J. W. (1990) Acta Crystallogr. Sect. A 46, 585-593
7. Deatherage, J. F., Loe, R. S., Anderson, C. M., and Moffat, K. (1976) J. Mol. Biol. 104, 687-706
8. de Ropp, J. S., La Mar, G. N., Wariishi, H., and Gold, M. H. (1991) J. Biol. Chem. 266, 15001-15008
9. Edwards, S. L., and Poulos, T. L. (1990) J. Biol. Chem. 265, 2588-2595
10. Edwards, S. L., Raag, R., Wariishi, H., Gold, M. H., and Poulos, T. L. (1993) Proc. Natl. Acad. Sci. U. S. A. 90, 750-754
11. Erman, J. E., Vitello, L. B., Miller, M. A., Shaw, A., Brown, K. A., and Kraut, J. (1993) Biochemistry 32, 9798-9806
12. Finzel, B. C., Poulos, T. L., and Kraut, J. (1984) J. Biol. Chem. 259, 13027-13036
13. Fülöp, V., Phizackerley, R. P., Soltis, S. M., Clifton, I. J., Wakatsuki, S., Erman, J., Hajdu, J., and Edwards, S. L. (1994) Structure 2, 201-208
14. Higashi, T. (1989) J. Appl. Crystallogr. 22, 9-18
15. Jones, T. A. (1978) J. Appl. Crystallogr. 11, 268-272
16. Kunishima, N., Fukuyama, K., Wakabayashi, S., Sumida, M., Takaya, M., Shibano, Y., Amachi, T., and Matsubara, H. (1993) Proteins: Struct. Funct. Genet. 15, 216-220
17. Kunishima, N., Fukuyama, K., Matsubara, H., Hatanaka, H., Shibano, Y., and Amachi, T. (1994) J. Mol. Biol. 235, 331-344
18. Kuriyan, J., Wilz, S., Karplus, M., and Petsko, G. A. (1986) J. Mol. Biol. 192, 133-154
19. Lukat, G. S., Rodgers, K. R., Jabro, M. N., and Goff, H. M. (1989) Biochemistry 28, 3338-3345
20. Luzatti, V. (1952) Acta Crystallogr. 5, 802-810
21. Morita, Y., Yamashita, H., Mikami, B., Iwamoto, H., Aibara, S., Terada, M., and Minami, J. (1988) J. Biochem. (Tokyo) 103, 693-699
22. Neya, S., Funasaki, N., Sato, T., Igarashi, N., and Tanaka, N. (1993) J. Biol. Chem. 268, 8935-8942
23. Pedersen, A. H., and Carlsen, S. (1994) The 13th International Symposium on the Life Sciences, Abstract, pp. 24-27, Kyoto, Japan
24. Perutz, M. F. (1970) Nature 228, 726-739
25. Petersen, J. F. W., Kadziola, A., and Larsen, S. (1994) FEBS Lett. 339, 291-296
26. Piontek, K., Glumoff, T., and Winterhalter, K. (1993) FEBS Lett. 315, 119-124
27. Poulos, T. L., Edwards, S. L., Wariishi, H., and Gold, M. H. (1993) J. Biol. Chem. 268, 4429-4440
28. Quillin, M. L., Arduini, R. M., Olson, J. S., and Phillips, G. N., Jr. (1993) J. Mol. Biol. 234, 140-155
29. Roussel, A., and Cambillau, C. (1989) in Silicon Graphics Geometry Partner Directory (Fall 1989) (Silicon Graphics, ed) pp. 77-78, Silicon Graphics, Mountain View, CA
30. Sakabe, N. (1991) Nucl. Instrum. Methods 303, 448-463
31. Satterlee, J. D., and Erman, J. E. (1991) Biochemistry 30, 4398-4405
32. Sawai-Hatanaka, H., Ashikari, T., Tanaka, Y, Asada, Y., Nakayama, T., Minakata, H., Kunishima, N., Fukuyama, K., Yamada, H., Shibano, Y., and Amachi, T. (1995) Biosci. Biotech. Biochem. 59, 1221-1228
33. Steigemann, W. (1974) Die Entwicklung und Anwendung von Rechenverfahren und Rechenprogrammen zur Strukturanalyse von Proteinem am Beispiel des Trypsin-Trypsininhibitor Komplexes, des Freien Inhibitors, und der L-Asperaginase. Ph.D. thesis, Technische University, München, Germany
34. Sundaramoorthy, M., Kishi, K., Gold, M. H., and Poulos, T. L. (1994) J. Biol. Chem. 269, 32759-32767
35. Thanabal, V., de Ropp, J. S., and La Mar, G. N. (1988) J. Am. Chem. Soc. 110, 3027-3035
36. Veitch, N. C., Tams, J. W., Vind, J., Dalbøge, H., and Welinder, K. G. (1994) Eur. J. Biochem. 222, 909-918
37. Vitello, L. B., Erman, J. E., Miller, M. A., Wang, J., and Kraut, J. (1993) Biochemistry 32, 9807-9818
38. Welinder, K. G. (1992) Curr. Opin. Struct. Biol. 2, 388-393