title: Formate dehydrogenase--a versatile enzyme in changing environments.
abstract: Several structures belonging to the large bis-molybdopterin guanine dinucleotide enzyme family have been published during the past four years. These include the structures of three formate dehydrogenases containing intrinsic selenocysteine residues - two soluble enzymes and one integral membrane protein. Together these have given detailed structural and mechanistic information about this family of enzymes.
authors.affiliation: Division of Biomedical Sciences Imperial College London, London SW7 2AZ, UK. mika.jormakka@imperial.ac.uk
authors.forename: Mika
authors.initials: M
authors.lastname: Jormakka
authors.forename: Bernadette
authors.initials: B
authors.lastname: Byrne
authors.forename: So
authors.initials: S
authors.lastname: Iwata
mesh_terms: D000595:Amino Acid Sequence; D004579:Electron Transport; D004926:Escherichia coli / Q000201:enzymology; D005560:Formate Dehydrogenases / Q000502:physiology*; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary
chemical_list: D005560:Formate Dehydrogenases