Tyr25, Tyr58 and Trp133 ofEscherichia colibacterioferritin transfer electrons between iron in the central cavity and the ferroxidase centre
Author:
Affiliation:
1. Centre for Molecular and Structural Biochemistry
2. School of Chemistry
3. University of East Anglia
4. Norwich Research Park
5. Norwich
6. School of Biological Sciences
7. University of Essex
8. Wivenhoe Park
9. Colchester CO4 3SQ
10. UK
Abstract
Tyr58 and Trp133 play key roles in the formation and decay of the Tyr25 radical species ofE. coliBFR.
Funder
Biotechnology and Biological Sciences Research Council
Leverhulme Trust
Publisher
Oxford University Press (OUP)
Subject
Metals and Alloys,Biochemistry,Biomaterials,Biophysics,Chemistry (miscellaneous)
Link
http://pubs.rsc.org/en/content/articlepdf/2017/MT/C7MT00187H
Reference39 articles.
1. The Ferritin-like superfamily: Evolution of the biological iron storeman from a rubrerythrin-like ancestor
2. Ferritins: iron/oxygen biominerals in protein nanocages
3. Ferritins: furnishing proteins with iron
4. Azotobacter cytochrome b557.5 is a bacterioferritin
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