Literature summary for 1.16.3.2 extracted from

Bradley, J.M.; Svistunenko, D.A.; Moore, G.R.; Le Brun, N.E.
Tyr25, Tyr58 and Trp133 of Escherichia coli bacterioferritin transfer electrons between iron in the central cavity and the ferroxidase centre (2017), Metallomics, 9, 1421-1428 .

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Protein Variants

Protein Variants	Comment	Organism
W133F	the Tyr25 radical spectrum simulated for the radical in the wild-type protein is overlaid with the difference spectrum proposed to originate from the same species in the mutant variant, overview	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	in bacterioferritin, iron mineralization kinetics are dependent on an intra-subunit catalytic diiron cofactor site (the ferroxidase centre), three closely located aromatic residues and an inner surface iron site. One of the aromatic residues, Tyr25, is the site of formation of a transient radical. The other two residues are Tyr58 and Trp133, these residues are important for the rates of formation and decay of the Tyr25 radical and decay of a secondary radical observed during Tyr25 radical decay. Mechanism in which these aromatic residues function in electron transfer from the inner surface site to the ferroxidase centre, overview	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
bacterioferritin	-	Escherichia coli
BFR	-	Escherichia coli

General Information

General Information	Comment	Organism
additional information	iron mineralization kinetics	Escherichia coli

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Release 2023.1 (January 2023)