Bacillibactin-Mediated Iron Transport in Bacillus subtilis
The hexadentate triscatecholamide bacillibactin delivers iron to Bacillus subtilis and is structurally similar to enterobactin, although in a more oblate conformation. B. subtilis uses two partially overlapping permeases (1 and 2) to acquire iron from its endogenous siderophores (bacillibactin and i...
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| Veröffentlicht in: | Journal of the American Chemical Society 2006-01, Vol.128 (1), p.22-23 |
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| container_title | Journal of the American Chemical Society |
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| creator | DERTZ, Emily A. XU, Jide STINTZI, Alain RAYMOND, Kenneth N. |
| description | The hexadentate triscatecholamide bacillibactin delivers iron to Bacillus subtilis and is structurally similar to enterobactin, although in a more oblate conformation. B. subtilis uses two partially overlapping permeases (1 and 2) to acquire iron from its endogenous siderophores (bacillibactin and itoic acid). Enterobactin and bacillibactin have opposite metal chiralities, different affinity for ferric ion, and dissimilar iron transport behaviors. The solution thermodynamic stability of ferric bacillibactin has been investigated through potentiometric and spectrophotometric titrations. The addition of a glycine to the catechol chelating arms causes a destabilization of the ferric complex of bacillibactin compared to ferric enterobactin. B. subtilis appears to express a separate receptor for enterobactin (permease 3), although enterobactin can also be transported through the permease for bacillibactin (permease 2). |
| doi_str_mv | 10.1021/ja055898c |
| format | Article |
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B. subtilis uses two partially overlapping permeases (1 and 2) to acquire iron from its endogenous siderophores (bacillibactin and itoic acid). Enterobactin and bacillibactin have opposite metal chiralities, different affinity for ferric ion, and dissimilar iron transport behaviors. The solution thermodynamic stability of ferric bacillibactin has been investigated through potentiometric and spectrophotometric titrations. The addition of a glycine to the catechol chelating arms causes a destabilization of the ferric complex of bacillibactin compared to ferric enterobactin. B. subtilis appears to express a separate receptor for enterobactin (permease 3), although enterobactin can also be transported through the permease for bacillibactin (permease 2).</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja055898c</identifier><identifier>PMID: 16390102</identifier><identifier>CODEN: JACSAT</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Bacillus subtilis - metabolism ; Biological and medical sciences ; Biological membranes ; Cell physiology ; Enterobactin - chemistry ; Enterobactin - metabolism ; Esters - chemistry ; Esters - metabolism ; Ferric Compounds - metabolism ; Fundamental and applied biological sciences. Psychology ; Iron - metabolism ; Kinetics ; Membrane and intracellular transports ; Membrane physicochemistry ; Molecular and cellular biology ; Molecular biophysics ; Oligopeptides - chemistry ; Oligopeptides - metabolism ; ortho-Aminobenzoates - chemistry ; ortho-Aminobenzoates - metabolism ; Siderophores - chemistry ; Siderophores - metabolism ; Thermodynamics</subject><ispartof>Journal of the American Chemical Society, 2006-01, Vol.128 (1), p.22-23</ispartof><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17720238$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16390102$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>DERTZ, Emily A.</creatorcontrib><creatorcontrib>XU, Jide</creatorcontrib><creatorcontrib>STINTZI, Alain</creatorcontrib><creatorcontrib>RAYMOND, Kenneth N.</creatorcontrib><title>Bacillibactin-Mediated Iron Transport in Bacillus subtilis</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>The hexadentate triscatecholamide bacillibactin delivers iron to Bacillus subtilis and is structurally similar to enterobactin, although in a more oblate conformation. B. subtilis uses two partially overlapping permeases (1 and 2) to acquire iron from its endogenous siderophores (bacillibactin and itoic acid). Enterobactin and bacillibactin have opposite metal chiralities, different affinity for ferric ion, and dissimilar iron transport behaviors. The solution thermodynamic stability of ferric bacillibactin has been investigated through potentiometric and spectrophotometric titrations. The addition of a glycine to the catechol chelating arms causes a destabilization of the ferric complex of bacillibactin compared to ferric enterobactin. B. subtilis appears to express a separate receptor for enterobactin (permease 3), although enterobactin can also be transported through the permease for bacillibactin (permease 2).</description><subject>Bacillus subtilis - metabolism</subject><subject>Biological and medical sciences</subject><subject>Biological membranes</subject><subject>Cell physiology</subject><subject>Enterobactin - chemistry</subject><subject>Enterobactin - metabolism</subject><subject>Esters - chemistry</subject><subject>Esters - metabolism</subject><subject>Ferric Compounds - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Iron - metabolism</subject><subject>Kinetics</subject><subject>Membrane and intracellular transports</subject><subject>Membrane physicochemistry</subject><subject>Molecular and cellular biology</subject><subject>Molecular biophysics</subject><subject>Oligopeptides - chemistry</subject><subject>Oligopeptides - metabolism</subject><subject>ortho-Aminobenzoates - chemistry</subject><subject>ortho-Aminobenzoates - metabolism</subject><subject>Siderophores - chemistry</subject><subject>Siderophores - metabolism</subject><subject>Thermodynamics</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFz0tLw0AQB_BFFFurB7-A5KK36L4f3mzxUWyxYgVvYTbZwNY0qdkE9Nu70qqnYZjfzPBH6JTgS4IpuVoBFkIbne-hIREUp4JQuY-GGGOaKi3ZAB2FsIotp5ocogGRzOC4OkTXY8h9VXkLeefrdO4KD50rkmnb1MmyhTpsmrZLfJ1sYR-S0NvOVz4co4MSquBOdnWEXu9ul5OHdPZ0P53czFLPOOvSAhsOsiTGMKqLkguOQYI2VklKcm05lSWjxhBwVpS6kFRZKhW2nEhHLWMjdLG9u2mbj96FLlv7kLuqgto1fcikkpgR8wPPdrC3a1dkm9avof3KftNGcL4DEHKoyhgv9-HfKUWj0tGlW-dD5z7_5tC-x2dMiWy5eMlmc_749rwYZ5p9A2MpcDs</recordid><startdate>20060111</startdate><enddate>20060111</enddate><creator>DERTZ, Emily A.</creator><creator>XU, Jide</creator><creator>STINTZI, Alain</creator><creator>RAYMOND, Kenneth N.</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20060111</creationdate><title>Bacillibactin-Mediated Iron Transport in Bacillus subtilis</title><author>DERTZ, Emily A. ; XU, Jide ; STINTZI, Alain ; RAYMOND, Kenneth N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i343t-d094a6f199328df4540a6a89b7621c8b426f32991aeb5f8d627b2670b416e2b33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Bacillus subtilis - metabolism</topic><topic>Biological and medical sciences</topic><topic>Biological membranes</topic><topic>Cell physiology</topic><topic>Enterobactin - chemistry</topic><topic>Enterobactin - metabolism</topic><topic>Esters - chemistry</topic><topic>Esters - metabolism</topic><topic>Ferric Compounds - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Iron - metabolism</topic><topic>Kinetics</topic><topic>Membrane and intracellular transports</topic><topic>Membrane physicochemistry</topic><topic>Molecular and cellular biology</topic><topic>Molecular biophysics</topic><topic>Oligopeptides - chemistry</topic><topic>Oligopeptides - metabolism</topic><topic>ortho-Aminobenzoates - chemistry</topic><topic>ortho-Aminobenzoates - metabolism</topic><topic>Siderophores - chemistry</topic><topic>Siderophores - metabolism</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>DERTZ, Emily A.</creatorcontrib><creatorcontrib>XU, Jide</creatorcontrib><creatorcontrib>STINTZI, Alain</creatorcontrib><creatorcontrib>RAYMOND, Kenneth N.</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>DERTZ, Emily A.</au><au>XU, Jide</au><au>STINTZI, Alain</au><au>RAYMOND, Kenneth N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bacillibactin-Mediated Iron Transport in Bacillus subtilis</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2006-01-11</date><risdate>2006</risdate><volume>128</volume><issue>1</issue><spage>22</spage><epage>23</epage><pages>22-23</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>The hexadentate triscatecholamide bacillibactin delivers iron to Bacillus subtilis and is structurally similar to enterobactin, although in a more oblate conformation. B. subtilis uses two partially overlapping permeases (1 and 2) to acquire iron from its endogenous siderophores (bacillibactin and itoic acid). Enterobactin and bacillibactin have opposite metal chiralities, different affinity for ferric ion, and dissimilar iron transport behaviors. The solution thermodynamic stability of ferric bacillibactin has been investigated through potentiometric and spectrophotometric titrations. The addition of a glycine to the catechol chelating arms causes a destabilization of the ferric complex of bacillibactin compared to ferric enterobactin. B. subtilis appears to express a separate receptor for enterobactin (permease 3), although enterobactin can also be transported through the permease for bacillibactin (permease 2).</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>16390102</pmid><doi>10.1021/ja055898c</doi><tpages>2</tpages></addata></record> |
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| subjects | Bacillus subtilis - metabolism Biological and medical sciences Biological membranes Cell physiology Enterobactin - chemistry Enterobactin - metabolism Esters - chemistry Esters - metabolism Ferric Compounds - metabolism Fundamental and applied biological sciences. Psychology Iron - metabolism Kinetics Membrane and intracellular transports Membrane physicochemistry Molecular and cellular biology Molecular biophysics Oligopeptides - chemistry Oligopeptides - metabolism ortho-Aminobenzoates - chemistry ortho-Aminobenzoates - metabolism Siderophores - chemistry Siderophores - metabolism Thermodynamics |
| title | Bacillibactin-Mediated Iron Transport in Bacillus subtilis |
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