Ontology highlight
ABSTRACT:
SUBMITTER: Bradley JM
PROVIDER: S-EPMC4691338 | biostudies-literature | 2015 Dec
REPOSITORIES: biostudies-literature
Bradley Justin M JM Svistunenko Dimitri A DA Lawson Tamara L TL Hemmings Andrew M AM Moore Geoffrey R GR Le Brun Nick E NE
Angewandte Chemie (International ed. in English) 20151016 49
Ferritins are iron storage proteins that overcome the problems of toxicity and poor bioavailability of iron by catalyzing iron oxidation and mineralization through the activity of a diiron ferroxidase site. Unlike in other ferritins, the oxidized di-Fe(3+) site of Escherichia coli bacterioferritin (EcBFR) is stable and therefore does not function as a conduit for the transfer of Fe(3+) into the storage cavity, but instead acts as a true catalytic cofactor that cycles its oxidation state while dr ...[more]