PMID: 9173872Apr 1, 1997Paper

Delineation of the arginine- and tetrahydrobiopterin-binding sites of neuronal nitric oxide synthase

The Biochemical Journal
A BoyhanP N Lowe

Abstract

Nitric oxide synthase (EC 1.14.13.39) catalyses the conversion of arginine, NADPH and oxygen to nitric oxide and citrulline, using haem, (6R)-5,6,7,8-tetrahydro-l-biopterin (tetrahydrobiopterin), calmodulin, FAD and FMN as cofactors. The enzyme consists of a central calmodulin-binding sequence flanked on the N-terminal side by a haem-binding region that contains the arginine and tetrahydrobiopterin sites and on the C-terminal side by a region homologous with NADPH:cytochrome P-450 reductase. By using domain boundaries defined by limited proteolysis of full-length enzyme, recombinant haem-binding regions of rat brain neuronal nitric oxide synthase were expressed and purified. Two proteins were made in high yield: one, corresponding to residues 221-724, contained bound haem and tetrahydrobiopterin and was able to bind Nomega-nitro-l-arginine (nitroarginine) or arginine; the other, containing residues 350-724, contained bound haem but was unable to bind tetrahydrobiopterin, nitroarginine or arginine. These results showed that rat brain neuronal nitric oxide synthase contains a critical determinant for arginine/tetrahydrobiopterin binding between residues 221 and 350. Limited proteolysis with chymotrypsin of the former protein resu...Continue Reading

Citations

Dec 18, 1998·The Journal of Biological Chemistry·P MartásekB S Masters
Jul 9, 2003·The Journal of Biological Chemistry·Koustubh PandaDennis J Stuehr
May 13, 1999·Biochimica Et Biophysica Acta·D J Stuehr

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