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Nitric-oxide synthases (NOS) catalyze the conversion of L-arginine to NO, which then stimulates many physiological processes. In the active form, each NOS is a dimer; each strand has both a heme-binding oxygenase domain and a reductase domain. In neuronal NOS (nNOS), there is a conserved cysteine motif (CX 4 C) that participates in a ZnS 4 center, which stabilizes the dimer interface and/or the flavoprotein-heme domain interface. Previously, the Cys 331 3 Ala mutant was produced, and it proveddoi:10.1074/jbc.m007461200 pmid:11067850 fatcat:ie3qrk6ktvhwhkvjhwsvh5jbg4