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Because it did not use ferric enterobactin, the catecholate aposiderophore was an effective agent for iron deprivation. We determined the kinetics and thermodynamics of [\n            <jats:sup>59<\/jats:sup>\n            Fe]apoferrichrome and\n            <jats:sup>59<\/jats:sup>\n            Fe-citrate binding and transport by NA1000. Its affinity and uptake rate for ferrichrome (equilibrium dissociation constant [\n            <jats:italic>\n              K\n              <jats:sub>d<\/jats:sub>\n            <\/jats:italic>\n            ], 1 nM; Michaelis-Menten constant [\n            <jats:italic>\n              K\n              <jats:sub>M<\/jats:sub>\n            <\/jats:italic>\n            ], 0.1 nM;\n            <jats:italic>V<\/jats:italic>\n            <jats:sub>max<\/jats:sub>\n            , 19 pMol\/10\n            <jats:sup>9<\/jats:sup>\n            cells\/min) were similar to those of\n            <jats:named-content content-type=\"genus-species\">Escherichia coli<\/jats:named-content>\n            FhuA. Transport properties for\n            <jats:sup>59<\/jats:sup>\n            Fe-citrate were similar to those of\n            <jats:named-content content-type=\"genus-species\">E. coli<\/jats:named-content>\n            FecA (\n            <jats:italic>\n              K\n              <jats:sub>M<\/jats:sub>\n            <\/jats:italic>\n            , 5.3 nM;\n            <jats:italic>V<\/jats:italic>\n            <jats:sub>max<\/jats:sub>\n            , 29 pMol\/10\n            <jats:sup>9<\/jats:sup>\n            cells\/min). Bioinformatic analyses implicated Fur-regulated loci\n            <jats:italic>00028<\/jats:italic>\n            ,\n            <jats:italic>00138<\/jats:italic>\n            ,\n            <jats:italic>02277<\/jats:italic>\n            , and\n            <jats:italic>03023<\/jats:italic>\n            as TonB-dependent transporters (TBDT) that participate in iron acquisition. We resolved TBDT with elevated expression under high- or low-iron conditions by SDS-PAGE of sodium sarcosinate cell envelope extracts, excised bands of interest, and analyzed them by mass spectrometry. These data identified five TBDT: three were overexpressed during iron deficiency (00028, 02277, and 03023), and 2 were overexpressed during iron repletion (00210 and 01196). CLUSTALW analyses revealed homology of putative TBDT 02277 to\n            <jats:named-content content-type=\"genus-species\">Escherichia coli<\/jats:named-content>\n            FepA and BtuB. A \u0394\n            <jats:italic>02277<\/jats:italic>\n            mutant did not transport hemin or hemoglobin in nutrition tests, leading us to designate the\n            <jats:italic>02277<\/jats:italic>\n            structural gene as\n            <jats:italic>hutA<\/jats:italic>\n            (for\n            <jats:underline>h<\/jats:underline>\n            eme\/hemoglobin\n            <jats:underline>u<\/jats:underline>\n            tilization).\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            The physiological roles of the 62 putative TBDT of\n            <jats:named-content content-type=\"genus-species\">C. crescentus<\/jats:named-content>\n            are mostly unknown, as are their evolutionary relationships to TBDT of other bacteria. We biochemically studied the iron uptake systems of\n            <jats:named-content content-type=\"genus-species\">C. crescentus<\/jats:named-content>\n            , identified potential iron transporters, and clarified the phylogenetic relationships among its numerous TBDT. Our findings identified the first outer membrane protein involved in iron acquisition by\n            <jats:named-content content-type=\"genus-species\">C. crescentus<\/jats:named-content>\n            , its heme\/hemoglobin transporter (HutA).\n          <\/jats:p>","DOI":"10.1128\/jb.00723-16","type":"journal-article","created":{"date-parts":[[2016,12,29]],"date-time":"2016-12-29T02:50:51Z","timestamp":1482979851000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":29,"title":["TonB-Dependent Heme\/Hemoglobin Utilization by Caulobacter crescentus HutA"],"prefix":"10.1128","volume":"199","author":[{"given":"Heloise","family":"Balhesteros","sequence":"first","affiliation":[{"name":"Departamento de Microbiologia, Instituto de Ciencias Biomedicas, Universidade de S\u00e3o Paulo, S\u00e3o Paulo, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yan","family":"Shipelskiy","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Noah J.","family":"Long","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aritri","family":"Majumdar","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Benjamin B.","family":"Katz","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naara M.","family":"Santos","sequence":"additional","affiliation":[{"name":"Departamento de Microbiologia, Instituto de Ciencias Biomedicas, Universidade de S\u00e3o Paulo, S\u00e3o Paulo, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura","family":"Leaden","sequence":"additional","affiliation":[{"name":"Departamento de Microbiologia, Instituto de Ciencias Biomedicas, Universidade de S\u00e3o Paulo, S\u00e3o Paulo, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Salete M.","family":"Newton","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marilis V.","family":"Marques","sequence":"additional","affiliation":[{"name":"Departamento de Microbiologia, Instituto de Ciencias Biomedicas, Universidade de S\u00e3o Paulo, S\u00e3o Paulo, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Phillip E.","family":"Klebba","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","first-page":"107","article-title":"Siderophores: diverse roles in microbial and human physiology","volume":"51","author":"Neilands JB","year":"1976","unstructured":"Neilands JB . 1976. 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