A structural model for FOXRED1, an FAD-dependent oxidoreductase necessary for NADH: Ubiquinone oxidoreductase (complex I) assembly
Copyright policy )A structural model for FOXRED1, an FAD-dependent oxidoreductase necessary for NADH: Ubiquinone oxidoreductase (complex I) assembly
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.
- University of Alberta Canada
Models, Molecular, Molecular Sequence Data, NAD, Catalytic Domain, Flavin-Adenine Dinucleotide, Humans, Amino Acid Sequence, Oxidoreductases, Sequence Alignment, Molecular Chaperones
Models, Molecular, Molecular Sequence Data, NAD, Catalytic Domain, Flavin-Adenine Dinucleotide, Humans, Amino Acid Sequence, Oxidoreductases, Sequence Alignment, Molecular Chaperones
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