title: Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain.
abstract: Nitric oxide synthases belong to a family of dual-flavin enzymes that transfer electrons from NAD(P)H to a variety of heme protein acceptors. During catalysis, their FMN subdomain plays a central role by acting as both an electron acceptor (receiving electrons from FAD) and an electron donor, and is thought to undergo large conformational movements and engage in two distinct protein-protein interactions in the process. This minireview summarizes what we know about the many factors regulating nitric oxide synthase flavoprotein domain function, primarily from the viewpoint of how they impact electron input/output and conformational behaviors of the FMN subdomain.
authors: Department of Pathobiology, Lerner Research Institute, Cleveland, OH 44195, USA. stuehrd@ccf.org
authors: Dennis J
authors: DJ
authors: Stuehr
authors: Jesús
authors: J
authors: Tejero
authors: Mohammad M
authors: MM
authors: Haque
mesh_terms: D000818:Animals; D001665:Binding Sites; D019281:Dimerization; D004579:Electron Transport; D005486:Flavin Mononucleotide / Q000378:metabolism; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D005420:Flavoproteins / Q000737:chemistry* / Q000378:metabolism*; D006418:Heme / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D019001:Nitric Oxide Synthase / Q000737:chemistry* / Q000378:metabolism*; D010084:Oxidation-Reduction; D011487:Protein Conformation
chemical_list: D005420:Flavoproteins; D005182:Flavin-Adenine Dinucleotide; D006418:Heme; D005486:Flavin Mononucleotide; D019001:Nitric Oxide Synthase