Article
The role of a conserved serine residue within hydrogen bonding distance of FAD in redox properties and the modulation of catalysis by Ca2+/calmodulin of constitutive nitric-oxide synthases.
The Journal of biological chemistry - 10 Nov 2006
Panda Satya Prakash, Gao Ying Tong, Roman Linda J, Martásek Pavel, Salerno John C, Masters Bettie Sue S
Abstract excerpt
The crystal structure of the neuronal nitric-oxide synthase (nNOS) NADPH/FAD binding domain indicated that Ser-1176 is within hydrogen bonding distance of Asp-1393 and the O4 atom of FAD and is also near the N5 atom of FAD (3.7 A). This serine residue is conserved in most of the ferredoxin-NADP+ reductase family of proteins and is important in electron transfer. In the present study, the homologous serines of...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.