Haem binding to horse spleen ferritin.
Horse spleen ferritin, a spherical protein shell of 24 subunits, contains no haem when extracted. This contrasts with ferritins isolated from bacterial sources which have the capacity to bind up to 24 haem groups [(1990) FEBS Lett. 271, 141-143] via two methionine residues [(1990) Nature 341, 771]. Here it is shown that horse spleen ferritin can bind between 15 and 17 haems per 24 subunits with an apparent association constant of 2.2-3.2 x 10(4) M-1. The strength of haem binding appears to be unaffected either by the presence of the core or by the oxidation state of the haem. The demonstration of the ability of animal ferritin to bind haem strengthens the similarity between it and bacterioferritin and could have major consequences for its mechanism of action in physiological iron uptake and release processes.
Kadir
F H
FH
Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences, University of East Anglia, Norwich, UK.
Moore
G R
GR
D000818:Animals; D005293:Ferritins / Q000302:isolation & purification / Q000378:metabolism*; D006418:Heme / Q000378:metabolism*; D006736:Horses; D011485:Protein Binding; D013053:Spectrophotometry; D013154:Spleen / Q000378:metabolism*
D006418:Heme; D005293:Ferritins