A new decoration for nitric oxide synthase - a Zn(Cys)4 site.
Intense interest in the action and synthesis of nitric oxide has fueled structural studies of nitric oxide synthase (NOS). The monomeric and dimeric heme domains of inducible NOS were the first NOS structures to be described. A recent independent analysis of the corresponding heme domains from endothelial NOS confirms most of the features found earlier and also reveals a novel Zn(Cys)4 center - a new feature for NOS.
Ludwig
M L
ML
Biophysics Research Division, Department of Biological Chemistry, University of Michigan, Ann Arbor 48109, MI, USA. ludwig@biop.umich.edu
Marletta
M A
MA
D000818:Animals; D001120:Arginine / Q000378:metabolism; D001665:Binding Sites; D001708:Biopterins / Q000031:analogs & derivatives / Q000502:physiology; D002956:Citrulline / Q000378:metabolism; D003545:Cysteine / Q000737:chemistry*; D019281:Dimerization; D004579:Electron Transport; D046911:Macromolecular Substances; D008958:Models, Molecular; D009249:NADP / Q000378:metabolism; D009569:Nitric Oxide / Q000096:biosynthesis; D019001:Nitric Oxide Synthase / Q000737:chemistry*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D015032:Zinc / Q000737:chemistry*
D046911:Macromolecular Substances; D001708:Biopterins; D002956:Citrulline; D009569:Nitric Oxide; D009249:NADP; D001120:Arginine; D019001:Nitric Oxide Synthase; C003402:sapropterin; D015032:Zinc; D003545:Cysteine