title: A structural model for FOXRED1, an FAD-dependent oxidoreductase necessary for NADH: Ubiquinone oxidoreductase (complex I) assembly.
abstract: The biogenesis of mitochondrial respiratory chain components is complex. Mammalian complex I (NADH:ubiquinone oxidoreductase) contains 44 different subunits, an FMN and seven iron-sulfur centers. Its assembly involves at least twelve additional proteins, called assembly factors. One of these is FOXRED1, a 486-amino acid FAD-dependent oxidoreductase. FOXRED1 is a member of the d-amino acid oxidase (DAO) family. A structural model of FOXRED1 reveals a large substrate-binding cavity and a putative oxygen-binding site. These features strongly suggest that FOXRED1 is catalytically active as an oxidoreductase. A metabolic role for FOXRED1 in the biogenesis of complex I should be considered.
authors.affiliation: Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada. Electronic address: bernard.lemire@ualberta.ca.
authors.forename: Bernard D
authors.initials: BD
authors.lastname: Lemire
mesh_terms: D000595:Amino Acid Sequence; D020134:Catalytic Domain; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism*; D008969:Molecular Sequence Data; D009243:NAD / Q000378:metabolism*; D010088:Oxidoreductases / Q000737:chemistry* / Q000378:metabolism*; D016415:Sequence Alignment
chemical_list: C556294:FOXRED1 protein, human; D018832:Molecular Chaperones; D009243:NAD; D005182:Flavin-Adenine Dinucleotide; D010088:Oxidoreductases
keywords: Flavoprotein; Leigh syndrome; Mitochondrial disease; NADH:ubiquinone oxidoreductase; Oxidase; Structural model