{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T09:33:24Z","timestamp":1790328804834,"version":"4.1.0"},"reference-count":31,"publisher":"National Academy of Sciences","issue":"28","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2005,7,12]]},"abstract":"\n The synthetic cubane-type iron\u2013sulfur clusters [Fe\n 4<\/jats:sub>\n S\n 4<\/jats:sub>\n (SR)\n 4<\/jats:sub>\n ]\n \n z<\/jats:sup>\n <\/jats:italic>\n form a four-member electron transfer series (\n z<\/jats:italic>\n = 3\u2013, 2\u2013, 1\u2013, and 0), all members of which except that with\n z<\/jats:italic>\n = 0 have been isolated and characterized. They serve as accurate analogues of protein-bound [Fe\n 4<\/jats:sub>\n S\n 4<\/jats:sub>\n (SCys)\n 4<\/jats:sub>\n ]\n \n z<\/jats:sup>\n <\/jats:italic>\n redox centers, which, in terms of core oxidation states, exhibit the redox couples [Fe\n 4<\/jats:sub>\n S\n 4<\/jats:sub>\n ]\n 3+\/2+<\/jats:sup>\n and [Fe\n 4<\/jats:sub>\n S\n 4<\/jats:sub>\n ]\n 2+\/1+<\/jats:sup>\n . Clusters with the all-ferrous core [Fe\n 4<\/jats:sub>\n S\n 4<\/jats:sub>\n ]\n 0<\/jats:sup>\n have never been isolated because of their oxidative sensitivity. Recent work on the Fe protein of\n Azotobacter vinelandii<\/jats:italic>\n nitrogenase has demonstrated the formation of the all-ferrous state upon reaction with a strong reductant. Treatment of the cyanide cluster [Fe\n 4<\/jats:sub>\n S\n 4<\/jats:sub>\n (CN)\n 4<\/jats:sub>\n ]\n 3\u2013<\/jats:sup>\n with K[Ph\n 2<\/jats:sub>\n CO] in acetonitrile\/tetrahydrofuran affords the all-ferrous cluster [Fe\n 4<\/jats:sub>\n S\n 4<\/jats:sub>\n (CN)\n 4<\/jats:sub>\n ]\n 4\u2013<\/jats:sup>\n , isolated as the Bu\n 4<\/jats:sub>\n N\n +<\/jats:sup>\n salt. The x-ray structure demonstrates retention of a cubane-type structure with idealized\n D<\/jats:italic>\n 2<\/jats:sub>\n \n d<\/jats:sub>\n <\/jats:italic>\n symmetry. The M\u00f6ssbauer spectrum unambiguously demonstrates the [Fe\n 4<\/jats:sub>\n S\n 4<\/jats:sub>\n ]\n 0<\/jats:sup>\n oxidation state. Bond distances, core volumes,\n 57<\/jats:sup>\n Fe isomer shifts, and visible absorption spectra make evident the high degree of structural and electronic similarity with the fully reduced Fe protein. The attribute of cyanide ligation causes positive [Fe\n 4<\/jats:sub>\n S\n 4<\/jats:sub>\n ]\n 2+\/1+<\/jats:sup>\n and [Fe\n 4<\/jats:sub>\n S\n 4<\/jats:sub>\n ]\n 1+\/0<\/jats:sup>\n redox potential shifts, facilitating the initial isolation of an analogue of the [Fe\n 4<\/jats:sub>\n S\n 4<\/jats:sub>\n ]\n 0<\/jats:sup>\n protein site.\n <\/jats:p>","DOI":"10.1073\/pnas.0504258102","type":"journal-article","created":{"date-parts":[[2005,6,29]],"date-time":"2005-06-29T12:42:52Z","timestamp":1120048972000},"page":"9741-9744","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":75,"title":["Initial synthesis and structure of an all-ferrous analogue of the fully reduced [Fe\n 4<\/sub>\n S\n 4<\/sub>\n ]\n 0<\/sup>\n cluster of the nitrogenase iron protein"],"prefix":"10.1073","volume":"102","author":[{"given":"Thomas A.","family":"Scott","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry, Miami University, Oxford, OH 45056; and Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Curtis P.","family":"Berlinguette","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, Miami University, Oxford, OH 45056; and Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard H.","family":"Holm","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, Miami University, Oxford, OH 45056; and Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hong-Cai","family":"Zhou","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry, Miami University, Oxford, OH 45056; and Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2005,6,28]]},"reference":[{"key":"e_1_3_2_1_2","first-page":"61","volume":"8","year":"2004","unstructured":"Holm, R. 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