The C331A mutant of neuronal nitric-oxide synthase is defective in arginine binding

Journal of Biological Chemistry

Volumn 273, Issue 52, 1998, Pages 34799-34805

  Martásek, Pavel ^a   Miller, R Timothy ^a   Liu, Qing ^b   Roman, Linda J ^a   Salerno, John C ^c   Migita, Catharina Taiko ^d   Raman, C S ^a   Gross, Steven S ^b   Ikeda Saito, Masao ^d   Masters, Bettie Sue Siler ^a  

^a UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

^b WEILL CORNELL MEDICAL COLLEGE   (United States)

^c RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^d CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2,6 DICHLOROPHENOLINDOPHENOL; ALANINE; ARGININE; CYSTEINE; CYTOCHROME C; HEME; IMIDAZOLE; N(G) NITROARGININE; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; TETRAHYDROBIOPTERIN;

ARTICLE; BINDING AFFINITY; CATALYSIS; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; MUTANT; NONHUMAN; PRIORITY JOURNAL;

ANIMALS; ARGININE; BIOPTERIN; CALMODULIN; CARBON MONOXIDE; CATALYTIC DOMAIN; CONSERVED SEQUENCE; CYSTEINE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; HEME; MUTATION; NADP; NEURONS; NITRIC OXIDE SYNTHASE; NITRIC OXIDE SYNTHASE TYPE I; OXIDATION-REDUCTION; RATS; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI;

EID: 0032567421     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.52.34799     Document Type: Article

References (18)

1. Bredt, D. S., and Snyder, S. H. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 682-685
2. Tayeh, M. A., and Marietta, M. A. (1989) J. Biol. Chem. 264, 19654-19658
3. Kwon, N. S., Nathan, C. F., and Stuehr, D. J. (1989) J. Biol. Chem. 264, 20496-20501
4. Mayer, B., John, M., and Böhme, E. (1990) FEBS Lett. 277, 215-219
5. McMillan, K., Bredt, D. S., Hirsch, D. J., Snyder, S. H., Clark, J. E., and Masters, B. S. S. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 11141-11145
6. White, K. A., and Marietta, M. A. (1992) Biochemistry 31, 6627-6631
7. Stuehr, D. J., and Ikeda-Saito, M. (1992) J. Biol. Chem. 267, 20547-20550
8. Klatt, P., Schmidt, K., and Mayer, B. (1992) Biochem. J. 288, 15-17
9. Bredt, D. S., Hwang, P. M., Glatt, C. E., Lowenstein, C., Reed, R. R., and Snyder, S. H. (1991) Nature 351, 714-718
10. Stuehr, D. J., Cho, H. J., Kwon, N. S., Weise, M. F., and Nathan, C. F. (1991) Proc. Natl. Acad. Sci. U. S. A. 88, 7773-7777
11. Mayer, B., John, M., Heinzel, B., Werner, E. R., Wachter, H., Schultz, G., and Böhme, E. (1991) FEBS Lett. 288, 187-191
12. Hevel, J. M., White, K. A., and Marletta, M. A. (1991) J. Biol. Chem. 266, 22789-22791
13. Nathan C., and Xie, Q. W. (1994) Cell 78, 915-918
14. Nishimura, J. S., Martásek, P., McMillan, K., Salerno, J., Liu, Q., Gross, S. S., and Masters, B. S. S. (1995) Biochem. Biophys. Res. Commun. 210, 288-294
15. Chen, P-F., Tsai, A-L., Berka, V., and Wu, K. K. (1997) J. Biol. Chem. 272, 6114-6118
16. Gachhui, R., Ghosh, D. K., Wu, C., Parkinson, J., Crane, B. R., and Stuehr, D. J. (1997) Biochemistry 36, 5097-5103
17. McMillan, K., and Masters, B. S. S. (1995) Biochemistry 34, 3686-3693
18. Ghosh, D. K., Wu, C., Fitters, E., Moloney, M., Werner, E. R., Mayer, B., and Stuehr, D. J. (1997) Biochemistry 36, 10609-10619