Mutation of W457 Alters N-Hydroxy-L-Arginine Oxidation by Inducible no Synthase: A Single Turnover Study
Nitric oxide synthases (NOS) are homodimeric enzymes which catalyze Arg to nitric oxide and citrulline (1). Its subunits contain a N-terminal oxygenase domain which can bind Fe-protoporphyrin IX (heme), Arg, and the essential cofactor 6R-tetrahydrobiopterin (H4B) and a C-terminal reductase domain containing binding sites for FAD, FMN, and NADPH.
KeywordsMidpoint Potential Reductase Domain Single Turnover Ferric Protein Oxygenase Domain
Unable to display preview. Download preview PDF.
- 2.Wang Z.Q., Wei C.C., Ghosh S., Meade A., Hemann, C., Hille, R, Stuehr D.J. Rapid kinetic studies link tetrahydrobiopterin radical formation to heme-dioxy reduction and arginine hydroxylation in inducible nitric-oxide synthase. Biochemistry, in press, 2001.Google Scholar
- 6.Aoyagi M., Arvai A.S., Ghosh S., Stuehr D.J., Tainer J.A., Getzoff, E.D. Structural studies of mutations at the tetrahydrobiopterin binding site in inducible nitric oxide synthase oxygenase dimmer. Biochemistry, in press, 2001.Google Scholar