Molecules of the metalloprotein, ferritin, have an outer shell comprised of a polymeric assembly of 24 polypeptide subunits (apoferritin). This protein shell encloses a hydrated space, the central cavity, within which up to several thousand iron atoms can be deposited as the biomineral, ferrihydrite. The actual pathway taken by iron moving across the protein shell is not known; an analogous question exists for the demonstrated entrance of negative stains into the central cavity. Intersubunit interstices at the 4-fold and 3-fold symmetry axes have been defined with x-ray diffraction, and were hypothesized to provide a pathway for penetration through the outer shell; however, since these channels are only 4Å in width, they are much too small to allow simple permeation of either hydrated iron or stain ions. A different hypothesis, based on studies of subunit dissociation from highly diluted ferritin, proposes that transient gaps in the protein shell are created by a rapid reversible subunit release and permit the direct passage of large ions into the central cavity.
Metabolism of Aminoguanidine, Diaminoguanidine, andNG-Amino-l-arginine by Neuronal NO-Synthase and Covalent Alteration of the Heme Prosthetic Group
