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Each subunit contains a high\u2010spin iron atom tetrahedrally bound to four cysteinyl sulfur atoms, a metal center similar to that found in rubredoxin (Rd) type proteins. The simplicity of the active center in Dx and the possibility of replacing the iron by other metals make this protein an attractive case for the crystallographic analysis of metal\u2010substituted derivatives. This study extends the relevance of Dx to the bioinorganic chemistry field and is important to obtain model compounds that can mimic the four sulfur coordination of metals in biology. Metal replacement experiments were carried out by reconstituting the apoprotein with In<jats:sup>3+<\/jats:sup>, Ga<jats:sup>3<\/jats:sup> <jats:sup>+<\/jats:sup>, Cd<jats:sup>2+<\/jats:sup>, Hg<jats:sup>2+<\/jats:sup>, and Ni<jats:sup>2+<\/jats:sup> salts. The In<jats:sup>3<\/jats:sup> <jats:sup>+<\/jats:sup> and Ga<jats:sup>3+<\/jats:sup> derivatives are isomorphous with the iron native protein; whereas Cd<jats:sup>2+<\/jats:sup>, Hg<jats:sup>2+<\/jats:sup>, and Ni<jats:sup>2+<\/jats:sup> substituted Dx crystallized under different experimental conditions, yielding two additional crystal morphologies; their structures were determined by the molecular replacement method. A comparison of the three\u2010dimensional structures for all metal derivatives shows that the overall secondary and tertiary structures are maintained, while some differences in metal coordination geometry occur, namely, bond lengths and angles of the metal with the sulfur ligands. These data are discussed in terms of the entatic state theory.<\/jats:p>","DOI":"10.1110\/ps.8.7.1536","type":"journal-article","created":{"date-parts":[[2009,2,17]],"date-time":"2009-02-17T22:12:45Z","timestamp":1234908765000},"page":"1536-1545","source":"Crossref","is-referenced-by-count":22,"title":["Structural studies by X\u2010ray diffraction on metal substituted desulforedoxin, a rubredoxin\u2010type protein"],"prefix":"10.1002","volume":"8","author":[{"given":"M.","family":"Archer","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.L.","family":"Carvalho","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S.","family":"Teixeira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"I.","family":"Moura","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J.J.G.","family":"Moura","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"F.","family":"Rusnak","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M.J.","family":"Rom\u00e3o","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2008,12,31]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.72.12.4854"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(05)80360-2"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1995.0465"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1021\/ic951653x"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja00006a027"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1007\/s007750050272"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1128\/jb.172.12.7289-7292.1990"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1128\/jb.171.9.4996-5004.1989"},{"key":"e_1_2_1_10_1","volume-title":"X\u2010PLOR (version 3.1). 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