[HTML][HTML] Crystal structures of zinc-free and-bound heme domain of human inducible nitric-oxide synthase: Implications for dimer stability and comparison with …
H Li, CS Raman, CB Glaser, E Blasko, TA Young… - Journal of Biological …, 1999 - ASBMB
The crystal structures of the heme domain of human inducible nitric-oxide synthase (NOS-2)
in zinc-free and-bound states have been solved. In the zinc-free structure, two symmetry-
related cysteine residues form a disulfide bond. In the zinc-bound state, these same two
cysteine residues form part of a zinc-tetrathiolate (ZnS 4) center indistinguishable from that
observed in the endothelial isoform (NOS-3). As in NOS-3, ZnS 4 plays a key role in
stabilizing intersubunit contacts and in maintaining the integrity of the cofactor …
in zinc-free and-bound states have been solved. In the zinc-free structure, two symmetry-
related cysteine residues form a disulfide bond. In the zinc-bound state, these same two
cysteine residues form part of a zinc-tetrathiolate (ZnS 4) center indistinguishable from that
observed in the endothelial isoform (NOS-3). As in NOS-3, ZnS 4 plays a key role in
stabilizing intersubunit contacts and in maintaining the integrity of the cofactor …