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Their environmental versatility depends on the ability to produce numerous iron-rich proteins, mainly multiheme\n                    <jats:italic>c<\/jats:italic>\n                    -type cytochromes. Although iron plays a vital role in the versatility of\n                    <jats:italic>Shewanella<\/jats:italic>\n                    species, very few studies exist regarding the strategies by which these bacteria scavenge iron from the environment. Siderophore-mediated iron transport is a commonly employed strategy for iron acquisition, and it was identified among\n                    <jats:italic>Shewanella<\/jats:italic>\n                    spp. over two decades ago.\n                    <jats:italic>Shewanella<\/jats:italic>\n                    species produce hydroxamate-type siderophores and iron removal from these compounds can occur in the cytoplasm via Fe(III)\u2013siderophore reduction mediated by siderophore-interacting proteins (SIPs). The genome of\n                    <jats:italic>Shewanella putrefaciens<\/jats:italic>\n                    DSM 9451 isolated from an infected child contains representatives of the two different families of SIPs: the flavin-containing siderophore reductase (\n                    <jats:italic>Sb<\/jats:italic>\n                    SIP) and the iron\u2013sulfur cluster-containing ferric\u2013siderophore reductase (\n                    <jats:italic>Sb<\/jats:italic>\n                    FSR). Here, we report their expression, purification, and further biochemical characterization of\n                    <jats:italic>Sb<\/jats:italic>\n                    SIP. The structural and functional characterization of\n                    <jats:italic>Sb<\/jats:italic>\n                    SIP and comparison with the homologous SIP from\n                    <jats:italic>Shewanella frigidimarina<\/jats:italic>\n                    (\n                    <jats:italic>Sf<\/jats:italic>\n                    SIP) revealed similarities between these proteins including a common binding pocket for NADH, NADPH, and siderophore substrates plus a pronounced redox-Bohr effect that ensures coupled transfer of electrons and protons in the physiological pH range. These mechanistic aspects open the door for further investigations on developing drugs that interfere with the iron metabolism of these bacteria and thereby prevent their spread.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:bold>Graphical abstract<\/jats:bold>\n                  <\/jats:p>","DOI":"10.1007\/s00775-025-02106-z","type":"journal-article","created":{"date-parts":[[2025,3,13]],"date-time":"2025-03-13T09:04:38Z","timestamp":1741856678000},"page":"241-255","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Flavin-containing siderophore-interacting protein of Shewanella putrefaciens DSM 9451 reveals common structural and functional aspects of ferric\u2013siderophore reduction"],"prefix":"10.1007","volume":"30","author":[{"given":"In\u00eas B.","family":"Trindade","sequence":"first","affiliation":[]},{"given":"Bruno M.","family":"Fonseca","sequence":"additional","affiliation":[]},{"given":"Teresa","family":"Catarino","sequence":"additional","affiliation":[]},{"given":"Pedro M.","family":"Matias","sequence":"additional","affiliation":[]},{"given":"Elin","family":"Moe","sequence":"additional","affiliation":[]},{"given":"Ricardo O.","family":"Louro","sequence":"additional","affiliation":[]}],"member":"297","published-online":{"date-parts":[[2025,3,13]]},"reference":[{"key":"2106_CR1","doi-asserted-by":"publisher","first-page":"1205","DOI":"10.1007\/s00775-008-0404-5","volume":"13","author":"C Andreini","year":"2008","unstructured":"Andreini C, Bertini I, Cavallaro G, Holliday GL, Thornton JM (2008) Metal ions in biological catalysis: from enzyme databases to general principles. 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