title: Zinc metallochemistry in biochemistry.
abstract: The chemically stable but stereochemically flexible, non-toxic nature of zinc combined with its amphoteric properties has permitted it to orchestrate a number of zinc-binding motifs critical to life processes. For zinc enzymes, catalytic, cocatalytic, and structural zinc sites exist. DNA-binding proteins have zinc fingers, twists, and clusters exist.
authors.affiliation: Center for Biochemical and Biophysical Sciences and Medicine, Harvard Medical School, Boston, MA 02115, USA.
authors.forename: B L
authors.initials: BL
authors.lastname: Vallee
authors.forename: D S
authors.initials: DS
authors.lastname: Auld
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D006801:Humans; D008024:Ligands; D008666:Metalloendopeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008667:Metalloproteins / Q000737:chemistry* / Q000378:metabolism*; D008668:Metallothionein / Q000737:chemistry; D008969:Molecular Sequence Data; D015032:Zinc / Q000737:chemistry / Q000378:metabolism*; D016335:Zinc Fingers
chemical_list: D008024:Ligands; D008667:Metalloproteins; D008668:Metallothionein; D008666:Metalloendopeptidases; D015032:Zinc