Structural analysis of haemin demetallation by L-chain apoferritins

Journal of Inorganic Biochemistry
Natalia de ValR R Crichton

Abstract

There are extensive structural similarities between eukaryotic and prokaryotic ferritins. However, there is one essential difference between these two types of ferritins: bacterioferritins contain haem whereas eukaryotic ferritins are considered to be non-haem proteins. In vitro experiments had shown that horse spleen apoferritin or recombinant horse L chain apoferritins, when co-crystallised with haemin, undergoes demetallation of the porphyrin. In the present study a cofactor has been isolated directly from horse spleen apoferritin and from crystals of the mutant horse L chain apoferritin (E53Q, E56Q, E57Q, E60Q and R59M) which had been co-crystallised with haemin. In both cases the HPLC/ESI-MS results confirm that the cofactor is a N-ethylprotoporphyrin IX. Crystal structures of wild type L chain horse apoferritin and its three mutants co-crystallised with haemin have been determined to high resolution and in all cases a metal-free molecule derived from haemin was found in the hydrophobic pocket, close to the two-fold axis. The X-ray structure of the E53Q, E56Q, E57Q, E60Q+R59M recombinant horse L-chain apoferritin has been obtained at a higher resolution (1.16Å) than previously reported for any mammalian apoferritins. Simil...Continue Reading

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Citations

Nov 19, 2014·Nanomedicine·Zbynek HegerRene Kizek
Jul 24, 2015·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Rabindra K BeheraElizabeth C Theil
Dec 17, 2014·Science·Christopher J Russo, Lori A Passmore
Feb 19, 2016·Chemical Communications : Chem Comm·Nicola PontilloAntonello Merlino
Oct 19, 2012·Dalton Transactions : an International Journal of Inorganic Chemistry·Craig T ArmstrongJ L Ross Anderson
Nov 1, 2015·The Biochemical Journal·Paolo ArosioMaura Poli
Nov 7, 2019·Acta Crystallographica. Section D, Structural Biology·David W MoreauRobert E Thorne

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