Mutations in the FMN Domain Modulate MCD Spectra of the Heme Site in the Oxygenase Domain of Inducible Nitric Oxide Synthase

摘要

In mammals, nitric oxide (NO) is synthesized by nitric oxide synthase (NOS), a homodimeric flavohemoprotein that catalyzes the oxidation of L-arginine (L-Arg) to NO and L-citrulline with NADPH and O_2 as cosubstrates. Each NOS subunit contains a C-terminal electron-supplying reductase unit with binding sites for NADPH (the electron source), flavin adenine dinucleotide (FAD), and flavin mononucleotide (FMN) and an N-terminal catalytic heme-containing oxygenase domain.