[HTML][HTML] Kinetics of CO and NO ligation with the Cys331→ Ala mutant of neuronal nitric-oxide synthase
JS Scheele, E Bruner, T Zemojtel, P Martásek… - Journal of Biological …, 2001 - ASBMB
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→ Ala mutant was produced, and it proved to be inactive in catalysis …
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→ Ala mutant was produced, and it proved to be inactive in catalysis …