{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T14:27:25Z","timestamp":1786976845173,"version":"build-2736575974"},"reference-count":69,"publisher":"Wiley","issue":"9","license":[{"start":{"date-parts":[[2014,1,31]],"date-time":"2014-01-31T00:00:00Z","timestamp":1391126400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Angew Chem Int Ed"],"published-print":{"date-parts":[[2014,2,24]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    A major barrier to understanding the mechanism of nitric oxide reductases (NORs) is the lack of a selective probe of NO binding to the nonheme Fe\n                    <jats:sub>B<\/jats:sub>\n                    center. By replacing the heme in a biosynthetic model of NORs, which structurally and functionally mimics NORs, with isostructural ZnPP, the electronic structure and functional properties of the Fe\n                    <jats:sub>B<\/jats:sub>\n                    nitrosyl complex was probed. This approach allowed observation of the first\n                    <jats:italic>S<\/jats:italic>\n                    =3\/2 nonheme {FeNO}\n                    <jats:sup>7<\/jats:sup>\n                    complex in a protein\u2010based model system of NOR. Detailed spectroscopic and computational studies show that the electronic state of the {FeNO}\n                    <jats:sup>7<\/jats:sup>\n                    complex is best described as a high spin ferrous iron (\n                    <jats:italic>S<\/jats:italic>\n                    =2) antiferromagnetically coupled to an NO radical (\n                    <jats:italic>S<\/jats:italic>\n                    = 1\/2) [Fe\n                    <jats:sup>2+<\/jats:sup>\n                    \u2010NO\n                    <jats:sup>.<\/jats:sup>\n                    ]. The radical nature of the Fe\n                    <jats:sub>B<\/jats:sub>\n                    \u2010bound NO would facilitate N\uf8ffN bond formation by radical coupling with the heme\u2010bound NO. This finding, therefore, supports the proposed\n                    <jats:italic>trans<\/jats:italic>\n                    mechanism of NO reduction by NORs.\n                  <\/jats:p>","DOI":"10.1002\/anie.201308431","type":"journal-article","created":{"date-parts":[[2014,1,31]],"date-time":"2014-01-31T04:58:42Z","timestamp":1391144322000},"page":"2417-2421","source":"Crossref","is-referenced-by-count":38,"title":["Spectroscopic and Computational Study of a Nonheme Iron Nitrosyl Center in a Biosynthetic Model of Nitric Oxide Reductase"],"prefix":"10.1002","volume":"53","author":[{"given":"Saumen","family":"Chakraborty","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julian","family":"Reed","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew","family":"Ross","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark J.","family":"Nilges","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Igor D.","family":"Petrik","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Soumya","family":"Ghosh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sharon","family":"Hammes\u2010Schiffer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J. 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