Detection of a clamp-shaped conformation of a neuronal nitric oxide synthase construct by pulsed EPR.

ABSTRACT: Nitric oxide synthase (NOS) is an enzyme responsible for the production of nitric oxide in living organisms. Structurally, it is a homodimer composed of multiple domains connected by random coil tethers. The resulting structural flexibility, along with the diverse conformational states it enables, is essential for NOS function and remains an active area of investigations. Here, we studied the docking interactions between the reductase domains of NOS subunits. To probe these interactions, a nitroxide-based bifunctional spin label was attached to each T34C/S38C calmodulin (CaM) molecule bound to the CaM-binding region of the tether, which connects the oxygenase and flavin mononucleotide (FMN) domains in each subunit of the homodimeric oxygenase/FMN (oxyFMN) construct of rat neuronal NOS (nNO

SUBMITTER: Astashkin AV 

PROVIDER: S-EPMC12746763 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature