scholarly journals Effect of Heme and Non-Heme Ligands on Subunit Dissociation of Normal and Carboxypeptidase-digested Hemoglobin

1974 ◽  
Vol 249 (18) ◽  
pp. 5689-5694
Author(s):  
Emilia Chiancone ◽  
Naomi M. Anderson ◽  
Eraldo Antonini ◽  
Joseph Bonaventura ◽  
Celia Bonaventura ◽  
...  
Keyword(s):  
Subunit Dissociation ◽  
Heme Ligands

Pathways for penetration of iron and negative stain across the protein shell of ferritin: Ultrastructural perspectives

1992 ◽  
Vol 50 (2) ◽  
pp. 1012-1013
Author(s):  
William H. Massover
Keyword(s):  
Outer Shell ◽  
X Ray Diffraction ◽  
Central Cavity ◽  
X Ray ◽  
Subunit Dissociation ◽  
Negative Stain ◽  
Analogous Question ◽  
Protein Shell

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.

scholarly journals Subunit Dissociation of the Unstable Hemoglobin Bibba (α2136 ro (H19)β2)

1970 ◽  
Vol 245 (8) ◽  
pp. 2185-2188
Author(s):  
Linda L. Smith ◽  
Betty P. Barton ◽  
T.H.J. Huisman
Keyword(s):  
Subunit Dissociation ◽  
Unstable Hemoglobin

scholarly journals Site-directed Replacement of the Coaxial Heme Ligands of Bacterioferritin Generates Heme-free Variants

1995 ◽  
Vol 270 (40) ◽  
pp. 23268-23274 ◽  
Author(s):  
Simon C. Andrews ◽  
Nick E. Le Brun ◽  
Vladimir Barynin ◽  
Andrew J. Thomson ◽  
Geoffrey R. Moore ◽  
...  
Keyword(s):  
Heme Ligands
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