Haem binding to ferritin and possible mechanisms of physiological iron uptake and release by ferritin.
Haem binding to horse spleen ferritin and Pseudomonas aeruginosa bacterioferritin has been studied by spectroscopic methods. A maximum of 16 haems per ferritin molecule, and 24 haems per bacterioferritin molecule, has been shown to bind. The influence of the bound haem on the rate of reductive iron release has been investigated. With a range of reductants and in the absence of haem the rate of release varied with the reductant, but in the presence of haem the rate was both independent of the reductant and faster than with any of the reductants alone. This indicates the rate-limiting step for iron release in the absence of haem was electron-transfer across the protein shell. Based on the results obtained with the in vitro assay system and from a consideration of data currently in the literature, plausible schemes for ferritin and bacterioferritin iron uptake and release are described.
Moore
G R
GR
Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences, University of East Anglia, Norwich, United Kingdom.
Kadir
F H
FH
al-Massad
F
F
D000818:Animals; D001426:Bacterial Proteins; D003573:Cytochrome b Group / Q000378:metabolism; D005293:Ferritins / Q000737:chemistry / Q000378:metabolism*; D006418:Heme / Q000378:metabolism*; D006736:Horses; D007501:Iron / Q000378:metabolism*; D007700:Kinetics; D010084:Oxidation-Reduction; D011550:Pseudomonas aeruginosa / Q000737:chemistry; D013053:Spectrophotometry; D013154:Spleen / Q000737:chemistry
D001426:Bacterial Proteins; D003573:Cytochrome b Group; D006418:Heme; D005293:Ferritins; C018032:bacterioferritin; D007501:Iron