<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Fukushima T</submitter><funding>NIAID NIH HHS</funding><funding>National Institutes of Health</funding><pagination>2092-100</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4168784</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>9(9)</volume><pubmed_abstract>Iron is an essential element for all organisms, and microorganisms produce small molecule iron-chelators, siderophores, to efficiently acquire Fe(III). Gram-positive bacteria possess lipoprotein siderophore-binding proteins (SBPs) on the membrane. Some of the SBPs bind both apo-siderophores (iron-free) and Fe-siderophore (iron-chelated) and only import Fe-siderophores. When the SBP initially binds an apo-siderophore, the SBP uses the Gram-positive siderophore-shuttle mechanism (the SBPs exchange Fe(III) from a Fe-siderophore to the apo-siderophore bound to the protein) and/or displacement mechanism (the apo-siderophore bound to the SBP is released and a Fe-siderophore is then bound to the protein) to import the Fe-siderophore. Previously, we reported that the Bacillus cereus SBP, YxeB, exc</pubmed_abstract><journal>ACS chemical biology</journal><pubmed_title>Direct evidence of iron uptake by the Gram-positive siderophore-shuttle mechanism without iron reduction.</pubmed_title><pmcid>PMC4168784</pmcid><funding_grant_id>R01 AI011744</funding_grant_id><funding_grant_id>AI11744</funding_grant_id><pubmed_authors>Allred BE</pubmed_authors><pubmed_authors>Raymond KN</pubmed_authors><pubmed_authors>Fukushima T</pubmed_authors></additional><is_claimable>false</is_claimable><name>Direct evidence of iron uptake by the Gram-positive siderophore-shuttle mechanism without iron reduction.</name><description>Iron is an essential element for all organisms, and microorganisms produce small molecule iron-chelators, siderophores, to efficiently acquire Fe(III). Gram-positive bacteria possess lipoprotein siderophore-binding proteins (SBPs) on the membrane. Some of the SBPs bind both apo-siderophores (iron-free) and Fe-siderophore (iron-chelated) and only import Fe-siderophores. When the SBP initially binds an apo-siderophore, the SBP uses the Gram-positive siderophore-shuttle mechanism (the SBPs exchange Fe(III) from a Fe-siderophore to the apo-siderophore bound to the protein) and/or displacement mechanism (the apo-siderophore bound to the SBP is released and a Fe-siderophore is then bound to the protein) to import the Fe-siderophore. Previously, we reported that the Bacillus cereus SBP, YxeB, exc</description><dates><release>2014-01-01T00:00:00Z</release><publication>2014 Sep</publication><modification>2025-04-22T21:08:52.041Z</modification><creation>2019-03-27T01:35:56Z</creation></dates><accession>S-EPMC4168784</accession><cross_references><pubmed>25007174</pubmed><doi>10.1021/cb500319n</doi></cross_references></HashMap>