A Positively Charged Cluster Formed in the Heme-distal Pocket of Cytochrome P450nor Is Essential for Interaction with NADH

Journal of Biological Chemistry

Volumn 276, Issue 7, 2001, Pages 5020-5026

  Kudo, Takashi ^a   Takaya, Naoki ^a   Park, Sam Yong ^b   Shiro, Yoshitsugu ^b   Shoun, Hirofumi ^a  

^a UNIVERSITY OF TSUKUBA   (Japan)

^b RIKEN HARIMA INSTITUTE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; HYDROGEN BONDS; MUTAGENESIS; NEGATIVE IONS; PHOTONS; PROTEINS; X RAY CRYSTALLOGRAPHY;

PROTON DELIVERY SYSTEMS;

BIOCHEMISTRY;

ALANINE; ANION; ARGININE; BROMIDE; CYTOCHROME P450; CYTOCHROME P450NOR; GLUTAMIC ACID; GLUTAMINE; HEME; LYSINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG; CAMPHOR 5 MONOOXYGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NITRIC OXIDE; NITRIC OXIDE REDUCTASE (P450); NITRIC-OXIDE REDUCTASE (P450); OXIDOREDUCTASE; PHOSPHATE;

ARTICLE; GENE MUTATION; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY; AMINO ACID SEQUENCE; BINDING SITE; CHEMISTRY; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; SPECTROPHOTOMETRY;

AMINO ACID SEQUENCE; ARGININE; BINDING SITES; BROMIDES; CAMPHOR 5-MONOOXYGENASE; CRYSTALLOGRAPHY, X-RAY; CYTOCHROME P-450 ENZYME SYSTEM; HEME; KINETICS; LYSINE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NAD; NITRIC OXIDE; OXIDOREDUCTASES; PHOSPHATES; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROPHOTOMETRY;

EID: 0035895995     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M007244200     Document Type: Article

References (26)

1. Nakahara, K., Tanimoto, T., Hatano, K., Usuda, K., and Shoun, H. (1993) J. Biol. Chem. 268, 8350-8355
2. Shiro, Y., Fujii, M., Iizuka, T., Adachi, S., Tsukamoto, K., Nakahara, K., and Shoun, H. (1995) J. Biol. Chem. 270, 1617-1623
3. Nakahara, K., and Shoun, H. (1996) J. Biochem. 120, 1082-1087
4. Usuda, K., Toritsuka, N., Matsuo, Y., Kim, D.-H., and Shoun, H. (1995) Appl. Environ. Microbiol. 61, 883-889
5. Kudo, T., Tomura, D., Liu, D.-L., Dai, X.-Q., and Shoun, H. (1996) Biochimie (Paris) 78, 792-799
6. Park, S.-Y., Shimizu, H., Adachi, S., Nakagawa, A., Tanaka, I., Nakahara, K., Shoun, H., Obayashi, E., Nakamura, H., Iizuka, T., and Shiro, Y. (1997) Nat. Struct. Biol. 4, 827-832
7. Shimizu, H., Obayashi, E., Gomi, Y., Arakawa, H., Park, S. Y., Nakamura, H., Adachi, S., Shoun, H., Shiro, Y. (2000) J. Biol. Chem. 275, 4816-4826
8. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd Ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
9. Kizawa, H., Tomura D., Oda M., Fukamizu, A., Hoshino T., Gotoh O., Yasui T., and Shoun H. (1991) J. Biol. Chem. 266, 10632-10637
10. Higuchi, R., Krummel, B., and Saiki, R. K. (1988) Nucleic Acids Res. 16, 7351-7367
11. Adachi, S., Oguchi, T., Tanida, H., Park, S.-Y., Shimizu, H., Miyatake, H., Kamiya, N., Shiro, Y., Inoue, Y., Ueki, T., and Iizuka, T. (2001) Nucl. Instrum. Methods Phys. Res. A, in press
12. Otwinowski, Z. (1993) in Proceedings of the CCP4 Study Weekend: Data Collection and Processing (Sawyer L., Isaacs, N., and Bailey, S., eds) pp. 56-62, SERC Daresbury Laboratory, Warrington, UK
13. The CCP4 Suite (1994) Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 760-763
14. Roussel, A., and Cambillau, C. (1989) in Silicon Graphics Geometry Partner Directory, pp. 77-78, Silicon Graphics, Mountain View, CA
15. Brunger, A. T. (1992) X-PLOR, A System for X-ray Crystallography and NMR, Version 3.1, Yale University Press, New Haven, CT
16. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) J. Appl. Crystallogr. 26, 283-291
17. Poulos, T. L., Finzel, B. C., and Howard, A. J. (1987) J. Mol. Biol. 195, 687-700
18. Obayashi, E., Takahashi, S., and Shiro, Y. (1998) J. Am. Chem. Soc. 120, 12964-12965
19. Shoun, H., Sudo, Y., Seto, Y., and Beppu, T. (1983) J. Biochem. 94, 1219-1229
20. Wirrenga, R. K., De Maeyer, M. C. H., and Hol, W. G. I. (1985) Biochemistry 24, 1346-1357
21. Scrutton, N. S., Berry, A., and Perham, R. N. (1990) Nature 343, 38-43
22. Gotoh, O. (1992) J. Biol. Chem. 267, 83-90
23. Hasemann, C. A., Ravichandran, K. G., Peterson, J. A., and Deisenhofer, J. (1994) J. Mol. Biol. 236, 1169-1185
24. Cupp-Vickery, J. R., and Poulos, T. L. (1995) Nat. Struct. Biol. 2, 144-153
25. Kraulis, P. J. (1991) J. Appl. Crystallogr. 24, 946-950
26. Okamoto, N., Tsuruta, K., Imai, Y., Tomura, D., and Shoun, H. (1997) Arch. Biochem. Biophys. 337, 338-344