The influence of chaotropic reagents on neuronal nitric oxide synthase and its flavoprotein module. Urea and guanidine hydrochloride stimulate NADPH-cytochrome c reductase activity of both proteins

Nitric Oxide - Biology and Chemistry

Volumn 1, Issue 1, 1997, Pages 39-49

  Narayanasami, Ramani ^a   Nishimura, Jonathan S ^a   McMillan, Kirk ^a   Roman, Linda J ^a   Shea, Thomas M ^a   Robida, Aaron M ^a   Horowitz, Paul M ^a   Masters, Bettie Sue S ^a  

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

Author keywords

[No Author keywords available]

Indexed keywords

2,6 DICHLOROPHENOLINDOPHENOL; CALCIUM CHLORIDE; CALMODULIN; FLAVINE ADENINE NUCLEOTIDE; FLAVINE MONONUCLEOTIDE; GUANIDINE; NITRIC OXIDE SYNTHASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE; UREA;

ARTICLE; CATALYSIS; ENZYME ACTIVATION; ENZYME INACTIVATION; FLUORESCENCE; NONHUMAN; PRIORITY JOURNAL;

EID: 0031424798     PISSN: 10898603     EISSN: None     Source Type: Journal    
DOI: 10.1006/niox.1996.0103     Document Type: Article

References (28)

1. Moncada S., Palmer R. M. J., Higgs E. A. Nitric oxide: Physiology, pathophysiology, and pharmacology. Pharmacol. Rev. 43:1991;109-142.
2. Garthwaite J. Glutamate, nitric oxide and cell-cell signaling in the nervous system. Trends Neurosci. 14:1991;60-67.
3. Bredt D. S., Snyder S. H. Nitric oxide: A physiologic messenger molecule. Annu. Rev. Biochem. 63:1994;175-195.
4. Arnold W. P., Mittal C. K., Katsuki S., Murad F. Nitric oxide activates guanylate cyclase and increases guanosine 3′,5′-cyclic monophosphate levels in various tissue preparations. Proc. Natl. Acad. Sci. USA. 74:1977;3203-3207.
5. Stuehr D. J., Griffith O. W. Mammalian nitric oxide synthases. Adv. Enzymol. Relat. Areas Mol. Biol. 65:1992;287-346.
6. Bredt D. S., Snyder S. H. Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme. Proc. Natl. Acad. Sci. USA. 87:1990;682-685.
7. Pollock J. S., Förstermann U., Mitchell J. A., Warner T. D., Schmidt H. H. H. W., Nakane M., Murad F. Purification and characterization of particulate endothelium-derived relaxing factor synthase from cultured and native bovine aortic endothelial cells. Proc. Natl. Acad. Sci. 88:1991;10480-10484.
8. Stuehr D. J., Cho H. J., Kwon N. S., Weise M., Nathan C. F. Purification and characterization of the cytokine-induced macrophage nitric oxide synthase: An FAD- and FMN-containing flavoprotein. Proc. Natl. Acad. Sci. USA. 88:1991;7773-7777.
9. Yui Y., Hattori R., Kosuga K., Eizawa H., Hiki K., Kawai C. Purification of nitric oxide synthase from rat macrophages. J. Biol. Chem. 266:1991;12544-12547.
10. Dinerman J. L., Lowenstein C. J., Snyder S. H. Molecular mechanisms of nitric oxide regulation. Circ. Res. 73:1993;217-222.
11. Porter T. D., Kasper C. B. NADPH-cytochrome P450 oxidoreductase: Flavin mononucleotide and flavin adenine dinucleotide domains evolved from different flavoproteins. Biochemistry. 25:1986;1682-1687.
12. Bredt D. S., Hwang P. M., Glatt C. E., Lowenstein C., Reed R. R., Snyder S. H. Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase. Nature. 351:1991;714-718.
13. Vermilion J., Ballou D. P., Massey V., Coon M. J. Separate roles for FMN and FAD in catalysis by liver microsomal NADPH-cytochrome P-450 reductase. J. Biol. Chem. 256:1981;266-277.
14. Sheta E. A., McMillan K., Masters B. S. S. Evidence for a bidomain structure of constitutive cerebellar nitric oxide synthase. J. Biol. Chem. 269:1994;15147-15153.
15. McMillan K., Masters B. S. S. Prokaryotic expression of the heme- and flavin-binding domains of rat neuronal nitric oxide synthase as distinct polypeptides: Identification of the heme-binding proximal thiolate ligand as cysteine-415. Biochemistry. 34:1995;3686-3693.
16. Masters B. S. S., Williams C. H. Jr., Kamin H. The preparation and properties of microsomal TPNH-cytochrome c reductase from pig liver. Methods Enzymol. 10:1967;565-573.
17. Roman L. J., Sheta E. A., Martasek P., Gross S. S., Liu Q., Masters B. S. S. High-level expression of functional rat neuronal nitric oxide synthase inEscherichia coli. Proc. Natl. Acad. Sci. USA. 92:1995;8428-8432.
18. Maniatis T., Fritsch E. F., Sambrook J. Molecular Cloning, A Laboratory Manual. 1982;Cold Spring Harbor Laboratory, Cold Spring Harbor. p. 437-437.
19. Faeder E. J., Siegel L. M. A rapid micromethod for determination of FMN and FAD in mixtures. Anal. Biochem. 53:1973;332-336.
20. Tanford C. Protein denaturation. Adv. Protein Chem. 23:1968;121-182.
21. Rosen C. G., Weber G. Dimer formation from 1-anilino-8-naphthalenesulfonate catalyzed by bovine serum albumin: A new fluorescent molecule with exceptional binding properties. Biochemistry. 8:1969;3915-3920.
22. Brand L., Gohlke J. R. Fluorescent probes for structure. Annu. Rev. Biochem. 41:1972;843-868.
23. Tsong T. Y. Ferricytochromec. Biochemistry. 15:1976;5467-5473.
24. Narayanasami R., Horowitz P. M., Masters B. S. S. Flavin-binding and protein structural integrity studies on NADPH-cytochrome P450 reductase are consistent with the presence of distinct domains. Arch. Biochem. Biophys. 316:1995;267-274.
25. 2+c. J. Biol. Chem. 267:1992;11374-11378.
26. Richards M. K., Clague M. J., Marletta M. A. Characterization of C415 mutants of neuronal nitric oxide synthase. Biochemistry. 35:1996;7772-7780.
27. Abu-Soud H. M., Yoho L. L., Stuehr D. J. Calmodulin controls neuronal nitric oxide synthase by a dual mechanism. J. Biol. Chem. 269:1994;32047-32050.
28. J. C. Salerno, D. E. Harris, K. Irizarry, B. Patel, A. J. Morales, C. L. Jones, B. A. Weissman, Q. Liu, S. S. Gross, 1996.