[HTML][HTML] Zinc content of Escherichia coli-expressed constitutive isoforms of nitric-oxide synthase: enzymatic activity and effect of pterin
RT Miller, P Martásek, CS Raman… - Journal of Biological …, 1999 - ASBMB
Recently, we obtained x-ray crystallographic data showing the presence of a ZnS 4 center in
the structure of Escherichia coli-expressed bovine endothelial nitric-oxide synthase (eNOS)
and rat neuronal nitric-oxide synthase (nNOS). The zinc atom is coordinated by two
CXXXXC motifs, one motif being contributed by each NOS monomer (cysteine 326 through
cysteine 331 in rat nNOS). Mutation of the nNOS cysteine 331 to alanine (C331A) results in
the loss of NO⋅ synthetic activity and also results in an inability to bind zinc efficiently …
the structure of Escherichia coli-expressed bovine endothelial nitric-oxide synthase (eNOS)
and rat neuronal nitric-oxide synthase (nNOS). The zinc atom is coordinated by two
CXXXXC motifs, one motif being contributed by each NOS monomer (cysteine 326 through
cysteine 331 in rat nNOS). Mutation of the nNOS cysteine 331 to alanine (C331A) results in
the loss of NO⋅ synthetic activity and also results in an inability to bind zinc efficiently …