Mechanisms of iron mineralization in ferritins:one size does not fit all

Bradley, Justin M, Moore, Geoffrey R and Le Brun, Nick E ORCID: https://orcid.org/0000-0001-9780-4061 (2014) Mechanisms of iron mineralization in ferritins:one size does not fit all. JBIC Journal of Biological Inorganic Chemistry, 19 (6). pp. 775-785. ISSN 0949-8257

Full text not available from this repository.

Abstract

Significant progress has been made in recent years toward understanding the processes by which an iron mineral is deposited within members of the ferritin family of 24mer iron storage proteins, enabled by high-resolution structures together with spectroscopic and kinetic studies. These suggest common characteristics that are shared between ferritins, namely, a highly symmetric arrangement of subunits that provides a protein coat around a central cavity in which the mineral is formed, channels through the coat that facilitate ingress and egress of ions, and catalytic sites, called ferroxidase centers, that drive Fe(2+) oxidation. They also reveal significant variations in both structure and mechanism amongst ferritins. Here, we describe three general types of structurally distinct ferroxidase center and the mechanisms of mineralization that they are associated with. The highlighted variation leads us to conclude that there is no universal mechanism by which ferritins function, but instead there exists several distinct mechanisms of ferritin iron mineralization.

Item Type: Article
Faculty \ School: Faculty of Science > School of Chemistry (former - to 2024)
UEA Research Groups: Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017)
Faculty of Science > Research Groups > Centre for Ocean and Atmospheric Sciences
Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Faculty of Science > Research Groups > Chemistry of Life Processes
Depositing User: Pure Connector
Date Deposited: 09 Jul 2014 10:06
Last Modified: 25 Sep 2024 11:19
URI: https://ueaeprints.uea.ac.uk/id/eprint/49063
DOI: 10.1007/s00775-014-1136-3

Actions (login required)

View Item View Item