4toc: Difference between revisions

Line 9:

</table>

== Function ==

[https://www.uniprot.org/uniprot/~~Q9HY79_PSEAE Q9HY79_PSEAE~~] ~~Iron~~-storage protein (~~By similarity~~). ~~Iron-storage protein, whose~~ ferroxidase center binds Fe(2+) ~~ions~~, oxidizes ~~them by~~ dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex (~~By similarity~~).~~[PIRNR~~:~~PIRNR002560]~~

[https://www.uniprot.org/uniprot/BFRB_PSEAE BFRB_PSEAE] The major iron-storage protein, part of the heterooligomeric bacterioferritin (BFR) complex. The ferroxidase center binds Fe(2+), oxidizes it using dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the BFR protein shell. Can store up to 600 iron atoms per bacterioferritin protein molecule (PubMed:19575528, PubMed:20067302, PubMed:25640193, PubMed:26368531). In iron-sufficient conditions (10 uM Fe(2+)) iron accumulates in BFR until about 12 hours, when it starts to deplete; stored iron is no longer detectable by 24 hours growth, iron is mobilized from the BFR as levels drop in the growth media (PubMed:28318006). Iron release from the BFR requires ferredoxin NADP reductase (FPR) and bacterioferritin-associated ferredoxin (Bfd) (PubMed:19575528, PubMed:22812654, PubMed:26368531). Reduction of the BfrB heme group occurs in the presence of Bfd, strongly suggesting that the BfrB-Bfd complex allows heme to mediate electron transfer from FPR to the Fe(3+) iron core in the BFR shell prior to its release as Fe(2+) (PubMed:19575528, PubMed:22812654, PubMed:26368531).<ref>PMID:19575528</ref> <ref>PMID:20067302</ref> <ref>PMID:22812654</ref> <ref>PMID:25640193</ref> <ref>PMID:26368531</ref> <ref>PMID:28318006</ref>

== Publication Abstract from PubMed ==

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 9: / Line 9: @@
 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/Q9HY79_PSEAE Q9HY79_PSEAE] Iron-storage protein (By similarity).  Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex (By similarity).[PIRNR:PIRNR002560]
+[https://www.uniprot.org/uniprot/BFRB_PSEAE BFRB_PSEAE] The major iron-storage protein, part of the heterooligomeric bacterioferritin (BFR) complex. The ferroxidase center binds Fe(2+), oxidizes it using dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the BFR protein shell. Can store up to 600 iron atoms per bacterioferritin protein molecule (PubMed:19575528, PubMed:20067302, PubMed:25640193, PubMed:26368531). In iron-sufficient conditions (10 uM Fe(2+)) iron accumulates in BFR until about 12 hours, when it starts to deplete; stored iron is no longer detectable by 24 hours growth, iron is mobilized from the BFR as levels drop in the growth media (PubMed:28318006). Iron release from the BFR requires ferredoxin NADP reductase (FPR) and bacterioferritin-associated ferredoxin (Bfd) (PubMed:19575528, PubMed:22812654, PubMed:26368531). Reduction of the BfrB heme group occurs in the presence of Bfd, strongly suggesting that the BfrB-Bfd complex allows heme to mediate electron transfer from FPR to the Fe(3+) iron core in the BFR shell prior to its release as Fe(2+) (PubMed:19575528, PubMed:22812654, PubMed:26368531).<ref>PMID:19575528</ref> <ref>PMID:20067302</ref> <ref>PMID:22812654</ref> <ref>PMID:25640193</ref> <ref>PMID:26368531</ref> <ref>PMID:28318006</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==