{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T08:08:11Z","timestamp":1791187691827,"version":"4.1.0"},"reference-count":28,"publisher":"American Chemical Society (ACS)","issue":"38","license":[{"start":{"date-parts":[[2015,8,6]],"date-time":"2015-08-06T00:00:00Z","timestamp":1438819200000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100000015","name":"U.S. Department of Energy","doi-asserted-by":"publisher","award":["DE- FG02-10ER16194"],"award-info":[{"award-number":["DE- FG02-10ER16194"]}],"id":[{"id":"10.13039\/100000015","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,9,24]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The organometallic H-cluster at the active site of [FeFe]-hydrogenases is synthesized by three accessory proteins, two of which are radical S-adenosylmethionine enzymes (HydE, HydG) and one of which is a GTPase (HydF). In this work we probed the specific role of H atom abstraction in HydG-catalyzed carbon monoxide and cyanide production from tyrosine. The isotope distributions of 5\u2032-deoxyadenosine and p-cresol were evaluated using deuterium-labeled tyrosine substrates in H2O and D2O. The observation of multiply deuterated 5\u2032-deoxyadenosine and deuterated S-adenosylmethionine when the reaction is carried out in D2O provides evidence for a 5\u2032-deoxyadenosyl radical-mediated abstraction of a hydrogen atom from a solvent-exchangeable position as a reversible event.<\/jats:p>","DOI":"10.1021\/ja504618y","type":"journal-article","created":{"date-parts":[[2014,8,6]],"date-time":"2014-08-06T13:00:07Z","timestamp":1407330007000},"page":"13086-13089","source":"Crossref","is-referenced-by-count":40,"title":["Reversible H Atom Abstraction Catalyzed by the Radical\n                    <i>S<\/i>\n                    -Adenosylmethionine Enzyme HydG"],"prefix":"10.1021","volume":"136","author":[{"given":"Benjamin R.","family":"Duffus","sequence":"first","affiliation":[{"name":"Montana State University , , , ,","place":["Bozeman, Montana, United States, 59717"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shourjo","family":"Ghose","sequence":"additional","affiliation":[{"name":"Montana State University , , , ,","place":["Bozeman, Montana, United States, 59717"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John W.","family":"Peters","sequence":"additional","affiliation":[{"name":"Montana State University , , , ,","place":["Bozeman, Montana, United States, 59717"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joan B.","family":"Broderick","sequence":"additional","affiliation":[{"name":"Montana State University , , , ,","place":["Bozeman, Montana, United States, 59717"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2014,8,6]]},"reference":[{"key":"2026090217144592200_cit1","doi-asserted-by":"crossref","first-page":"4206","DOI":"10.1021\/cr050196r","volume":"107","author":"Vignais","year":"2007","journal-title":"Chem. 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