{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T10:20:35Z","timestamp":1785406835058,"version":"3.56.0"},"reference-count":67,"publisher":"International Union of Crystallography (IUCr)","issue":"5","license":[{"start":{"date-parts":[[2026,4,7]],"date-time":"2026-04-07T00:00:00Z","timestamp":1775520000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/legalcode"},{"start":{"date-parts":[[2026,4,7]],"date-time":"2026-04-07T00:00:00Z","timestamp":1775520000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/legalcode"}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr D Struct Biol","Acta Crystallogr D","Acta Cryst D","Acta Cryst D Struct Biol","Acta Cryst Sect D","Acta Cryst Sect D Struct Biol","Acta Crystallogr Sect D","Acta Crystallogr Sect D Struct Biol","Acta Crystallogr D Biol Crystallogr","Acta Cryst D Biol Cryst"],"accepted":{"date-parts":[[2026,2,27]]},"published-print":{"date-parts":[[2026,5,1]]},"abstract":"<jats:p>\n                    Flavodiiron proteins (FDPs) are NO and\/or O\n                    <jats:sub>2<\/jats:sub>\n                    reductases which contain a di-iron catalytic center. Interestingly, they exhibit different selectivities towards each one of these substrates, despite having the same ligands of the iron ions.\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    FDP is a selective NO reductase that protects this bacterium against nitric oxide by catalyzing two-electron reduction to the nontoxic N\n                    <jats:sub>2<\/jats:sub>\n                    O. Previously, based on kinetic studies, we explored the possible role of two amino acids located in the di-iron second coordination sphere, Lys53 and Tyr271, in modulation of the substrate selectivity of\n                    <jats:italic>Entamoeba histolytica<\/jats:italic>\n                    FDP, a selective O\n                    <jats:sub>2<\/jats:sub>\n                    reductase. In this work, we replaced the structurally equivalent residues in\n                    <jats:italic>E.\u00a0coli<\/jats:italic>\n                    FDP, Asp52 and Ser262, by those present in the O\n                    <jats:sub>2<\/jats:sub>\n                    -selective FDP and determined their crystal structures in both oxidized and reduced states. Furthermore, the molecular-substrate tunnels were experimentally identified using krypton pressurization of the crystals. The data obtained corroborated previous molecular-dynamics calculations on this FDP. The side chains of residues in both positions 52 and 262 of\n                    <jats:italic>E. coli<\/jats:italic>\n                    FDP variants and wild type are in the vicinity of the shorter intramolecular tunnel, which is suggested to be the exit route for the reaction products N\n                    <jats:sub>2<\/jats:sub>\n                    O and H\n                    <jats:sub>2<\/jats:sub>\n                    O. The\n                    <jats:italic>E. coli<\/jats:italic>\n                    FDP S262Y variant shows photoreduction of the di-iron center and partial loss of electron density in some of its coordinating ligands after X-ray exposure, and these effects are consistent with increased radiation sensitivity. The kinetic properties of the variants towards NO and O\n                    <jats:sub>2<\/jats:sub>\n                    were not significantly different from the wild type, contrary to what was observed previously for\n                    <jats:italic>E. histolytica<\/jats:italic>\n                    FDP.\n                  <\/jats:p>","DOI":"10.1107\/s2059798326002214","type":"journal-article","created":{"date-parts":[[2026,3,23]],"date-time":"2026-03-23T11:41:16Z","timestamp":1774266076000},"page":"457-470","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":0,"title":["Structures of variants of\n                    <i>Escherichia coli<\/i>\n                    flavodiiron-type nitric oxide reductase reveal changes in the di-iron site"],"prefix":"10.1107","volume":"82","author":[{"given":"Patr\u00edcia T.","family":"Borges","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02xankh89","id-type":"ROR","asserted-by":"publisher"}],"department":["ITQB NOVA, Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica Ant\u00f3nio Xavier"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Filipe","family":"Folgosa","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02xankh89","id-type":"ROR","asserted-by":"publisher"}],"department":["ITQB NOVA, Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica Ant\u00f3nio Xavier"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria C.","family":"Martins","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02xankh89","id-type":"ROR","asserted-by":"publisher"}],"department":["ITQB NOVA, Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica Ant\u00f3nio Xavier"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2830-0286","authenticated-orcid":true,"given":"Guillaume","family":"Gotthard","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03eh3y714","id-type":"ROR","asserted-by":"publisher"}],"department":["Swiss Light Source"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3481-0787","authenticated-orcid":true,"given":"Peter","family":"van der Linden","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02550n020","id-type":"ROR","asserted-by":"publisher"}]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1268-7826","authenticated-orcid":true,"given":"Philippe","family":"Carpentier","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02550n020","id-type":"ROR","asserted-by":"publisher"}]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4124-6237","authenticated-orcid":true,"given":"Miguel","family":"Teixeira","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02xankh89","id-type":"ROR","asserted-by":"publisher"}],"department":["ITQB NOVA, Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica Ant\u00f3nio Xavier"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carlos","family":"Fraz\u00e3o","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02xankh89","id-type":"ROR","asserted-by":"publisher"}],"department":["ITQB NOVA, Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica Ant\u00f3nio Xavier"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9474-2405","authenticated-orcid":true,"given":"C\u00e9lia V.","family":"Rom\u00e3o","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/02xankh89","id-type":"ROR","asserted-by":"publisher"}],"department":["ITQB NOVA, Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica Ant\u00f3nio Xavier"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"329","published-online":{"date-parts":[[2026,4,7]]},"reference":[{"key":"gm5120_bb1","doi-asserted-by":"crossref","first-page":"1729","DOI":"10.1016\/j.str.2004.07.013","volume":"12","author":"Adam","year":"2004","journal-title":"Structure"},{"key":"gm5120_bb2","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Cryst. 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