{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T06:40:42Z","timestamp":1791355242714,"version":"4.3.1"},"reference-count":24,"publisher":"American Chemical Society (ACS)","issue":"35","license":[{"start":{"date-parts":[[2015,8,15]],"date-time":"2015-08-15T00:00:00Z","timestamp":1439596800000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM104543"],"award-info":[{"award-number":["GM104543"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["F32GM111025"],"award-info":[{"award-number":["F32GM111025"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006151","name":"Basic Energy Sciences","doi-asserted-by":"publisher","award":["DE-FG02-09ER46632"],"award-info":[{"award-number":["DE-FG02-09ER46632"]}],"id":[{"id":"10.13039\/100006151","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,9,3]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The two cyanide ligands in the assembled cluster of [FeFe] hydrogenase originate from exogenous l-tyrosine. Using selectively labeled tyrosine substrates, the cyanides were isotopically labeled via a recently developed in vitro maturation procedure allowing advanced electron paramagnetic resonance techniques to probe the electronic structure of the catalytic core of the enzyme. The ratio of the isotropic 13C hyperfine interactions for the two CN\u2013 ligands\u2500a reporter of spin density on their respective coordinating iron ions\u2500collapses from \u22485.8 for the Hox form of hydrogenase to &amp;lt;2 for the CO-inhibited form. Additionally, when the maturation was carried out using [15N]-tyrosine, no features previously ascribed to the nitrogen of the bridging dithiolate ligand were observed suggesting that this bridge is not sourced from tyrosine.<\/jats:p>","DOI":"10.1021\/ja507046w","type":"journal-article","created":{"date-parts":[[2014,8,15]],"date-time":"2014-08-15T21:22:20Z","timestamp":1408137740000},"page":"12237-12240","source":"Crossref","is-referenced-by-count":40,"title":["The Cyanide\nLigands of [FeFe] Hydrogenase: Pulse EPR\nStudies of 13C and 15N-Labeled H-Cluster"],"prefix":"10.1021","volume":"136","author":[{"given":"William K.","family":"Myers","sequence":"first","affiliation":[{"name":"University of California, Davis , , ,","place":["Davis, California, United States, 95616"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Troy A.","family":"Stich","sequence":"additional","affiliation":[{"name":"University of California, Davis , , ,","place":["Davis, California, United States, 95616"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel L. 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