{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,17]],"date-time":"2026-07-17T11:27:49Z","timestamp":1784287669511,"version":"3.55.0"},"reference-count":40,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,2,1]],"date-time":"2026-02-01T00:00:00Z","timestamp":1769904000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,2,1]],"date-time":"2026-02-01T00:00:00Z","timestamp":1769904000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,11,6]],"date-time":"2026-11-06T00:00:00Z","timestamp":1793923200000},"content-version":"am","delay-in-days":278,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,2,1]],"date-time":"2026-02-01T00:00:00Z","timestamp":1769904000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,2,1]],"date-time":"2026-02-01T00:00:00Z","timestamp":1769904000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,2,1]],"date-time":"2026-02-01T00:00:00Z","timestamp":1769904000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,2,1]],"date-time":"2026-02-01T00:00:00Z","timestamp":1769904000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,2,1]],"date-time":"2026-02-01T00:00:00Z","timestamp":1769904000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100017241","name":"Maryland Advanced Research Computing Center","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100017241","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01GM119374"],"award-info":[{"award-number":["R01GM119374"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R35GM149233"],"award-info":[{"award-number":["R35GM149233"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Inorganic Biochemistry"],"published-print":{"date-parts":[[2026,2]]},"DOI":"10.1016\/j.jinorgbio.2025.113107","type":"journal-article","created":{"date-parts":[[2025,10,15]],"date-time":"2025-10-15T23:43:15Z","timestamp":1760571795000},"page":"113107","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":5,"special_numbering":"C","title":["Examining Pseudohalide (N3, NCS, NCO) Coordination in Nonheme Fe(II) and Fe(III) Complexes"],"prefix":"10.1016","volume":"275","author":[{"given":"Vishal","family":"Yadav","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maxime A.","family":"Siegler","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David P.","family":"Goldberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113107_bb0005","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1021\/acs.chemrev.7b00032","article-title":"Development of halogenase enzymes for use in synthesis","volume":"118","author":"Latham","year":"2018","journal-title":"Chem. Rev."},{"issue":"8","key":"10.1016\/j.jinorgbio.2025.113107_bb0010","doi-asserted-by":"crossref","first-page":"5619","DOI":"10.1021\/acs.chemrev.6b00571","article-title":"Enzymatic halogenation and dehalogenation reactions: pervasive and mechanistically diverse","volume":"117","author":"Agarwal","year":"2017","journal-title":"Chem. Rev."},{"issue":"8","key":"10.1016\/j.jinorgbio.2025.113107_bb0015","doi-asserted-by":"crossref","first-page":"314","DOI":"10.3390\/catal8080314","article-title":"A comparative review on the catalytic mechanism of Nonheme Iron hydroxylases and Halogenases","volume":"8","author":"Timmins","year":"2018","journal-title":"Catalysts"},{"issue":"7082","key":"10.1016\/j.jinorgbio.2025.113107_bb0020","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1038\/nature04544","article-title":"Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis","volume":"440","author":"Blasiak","year":"2006","journal-title":"Nature"},{"issue":"42","key":"10.1016\/j.jinorgbio.2025.113107_bb0025","doi-asserted-by":"crossref","first-page":"17723","DOI":"10.1073\/pnas.0909649106","article-title":"Substrate positioning controls the partition between halogenation and hydroxylation in the aliphatic halogenase, SyrB2","volume":"106","author":"Matthews","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"8","key":"10.1016\/j.jinorgbio.2025.113107_bb0030","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1038\/nchembio.2112","article-title":"Structural basis for halogenation by iron- and 2-oxo-glutarate-dependent enzyme WelO5","volume":"12","author":"Mitchell","year":"2016","journal-title":"Nat. Chem. Biol."},{"issue":"10","key":"10.1016\/j.jinorgbio.2025.113107_bb0035","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1038\/s41589-019-0355-x","article-title":"A family of radical halogenases for the engineering of amino-acid-based products","volume":"15","author":"Neugebauer","year":"2019","journal-title":"Nat. Chem. Biol."},{"issue":"16","key":"10.1016\/j.jinorgbio.2025.113107_bb0040","doi-asserted-by":"crossref","first-page":"2480","DOI":"10.1021\/acs.biochem.3c00248","article-title":"Synergistic binding of the halide and cationic prime substrate of l-lysine 4-Chlorinase, BesD, in both Ferrous and Ferryl States","volume":"62","author":"Slater","year":"2023","journal-title":"Biochemistry"},{"issue":"22","key":"10.1016\/j.jinorgbio.2025.113107_bb0045","doi-asserted-by":"crossref","first-page":"13910","DOI":"10.1021\/acscatal.2c04608","article-title":"Structural insight into the catalytic mechanism of non-Heme Iron Halogenase AdaV in 2\u2032-Chloropentostatin biosynthesis","volume":"12","author":"Zhai","year":"2022","journal-title":"ACS Catal."},{"issue":"17","key":"10.1016\/j.jinorgbio.2025.113107_bb0050","doi-asserted-by":"crossref","first-page":"9443","DOI":"10.1039\/D0CS01551B","article-title":"Halogenases: a palette of emerging opportunities for synthetic biology\u2013synthetic chemistry and C\u2013H functionalisation","volume":"50","author":"Crowe","year":"2021","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.jinorgbio.2025.113107_bb0055","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.cbpa.2018.01.002","article-title":"Halogenases: powerful tools for biocatalysis (mechanisms applications and scope)","volume":"43","author":"Gkotsi","year":"2018","journal-title":"Curr. Opin. Chem. Biol."},{"issue":"6","key":"10.1016\/j.jinorgbio.2025.113107_bb0060","doi-asserted-by":"crossref","first-page":"1659","DOI":"10.1038\/s41596-023-00825-8","article-title":"Click chemistry: a transformative technology in nuclear medicine","volume":"18","author":"Bauer","year":"2023","journal-title":"Nat. Prot."},{"issue":"16","key":"10.1016\/j.jinorgbio.2025.113107_bb0065","doi-asserted-by":"crossref","first-page":"6538","DOI":"10.1039\/D5DT00273G","article-title":"Exploring pseudohalide substitution in \u03b1-cobalt-based layered hydroxides","volume":"54","author":"Diouane","year":"2025","journal-title":"Dalton Trans."},{"issue":"3","key":"10.1016\/j.jinorgbio.2025.113107_bb0070","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1038\/nchembio.1438","article-title":"Direct nitration and azidation of aliphatic carbons by an iron-dependent halogenase","volume":"10","author":"Matthews","year":"2014","journal-title":"Nat. Chem. Biol."},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113107_bb0075","doi-asserted-by":"crossref","first-page":"1867","DOI":"10.1038\/s41467-020-15777-w","article-title":"The chloroalkaloid (\u2212)-acutumine is biosynthesized via a Fe(II)- and 2-oxoglutarate-dependent halogenase in Menispermaceae plants","volume":"11","author":"Kim","year":"2020","journal-title":"Nat. Commun."},{"issue":"36","key":"10.1016\/j.jinorgbio.2025.113107_bb0080","doi-asserted-by":"crossref","first-page":"14477","DOI":"10.1021\/acs.inorgchem.2c02872","article-title":"Non-native anionic ligand binding and reactivity in engineered variants of the Fe(II)- and \u03b1-ketoglutarate-dependent oxygenase, SadA","volume":"61","author":"Chan","year":"2022","journal-title":"Inorg. Chem."},{"issue":"64","key":"10.1016\/j.jinorgbio.2025.113107_bb0085","first-page":"1","article-title":"Cooperative photometallobiocatalysis: nonheme Fe enzyme-catalyzed enantioconvergent radical decarboxylative azidation, thiocyanation, and isocyanation of redox-active esters","volume":"202506361","author":"Zhao","year":"2025","journal-title":"Angew. Chem. Int. Ed."},{"issue":"8","key":"10.1016\/j.jinorgbio.2025.113107_bb0090","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1038\/s44160-024-00536-2","article-title":"Biocatalytic enantioselective C(sp3)\u2013H fluorination enabled by directed evolution of non-haem iron enzymes","volume":"3","author":"Zhao","year":"2024","journal-title":"Nat Synth"},{"issue":"6595","key":"10.1016\/j.jinorgbio.2025.113107_bb0095","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1126\/science.abj2830","article-title":"Directed evolution of nonheme iron enzymes to access abiological radical-relay C(sp3)-H azidation","volume":"376","author":"Rui","year":"2022","journal-title":"Science"},{"issue":"12","key":"10.1016\/j.jinorgbio.2025.113107_bb0100","doi-asserted-by":"crossref","first-page":"1394","DOI":"10.1038\/s41929-024-01257-7","article-title":"Merging photoredox with metalloenzymatic catalysis for enantioselective decarboxylative C(sp3)\u2013N3 and C(sp3)\u2013SCN bond formation","volume":"7","author":"Rui","year":"2024","journal-title":"Nat. Catal."},{"issue":"50","key":"10.1016\/j.jinorgbio.2025.113107_bb0105","doi-asserted-by":"crossref","first-page":"34878","DOI":"10.1021\/jacs.4c14310","article-title":"Biocatalytic generation of Trifluoromethyl radicals by Nonheme Iron enzymes for enantioselective alkene Difunctionalization","volume":"146","author":"Zhang","year":"2024","journal-title":"J. Am. Chem. Soc."},{"issue":"8","key":"10.1016\/j.jinorgbio.2025.113107_bb0110","doi-asserted-by":"crossref","first-page":"958","DOI":"10.1038\/s44160-024-00507-7","article-title":"Engineering non-haem iron enzymes for enantioselective C(sp3)\u2013F bond formation via radical fluorine transfer","volume":"3","author":"Zhao","year":"2024","journal-title":"Nat Synth"},{"issue":"6","key":"10.1016\/j.jinorgbio.2025.113107_bb0115","doi-asserted-by":"crossref","first-page":"2396","DOI":"10.1021\/jacs.6b11995","article-title":"Frontier molecular orbital contributions to chlorination versus hydroxylation selectivity in the non-heme Iron Halogenase SyrB2","volume":"139","author":"Srnec","year":"2017","journal-title":"J. Am. Chem. Soc."},{"issue":"15","key":"10.1016\/j.jinorgbio.2025.113107_bb0120","doi-asserted-by":"crossref","first-page":"5110","DOI":"10.1021\/jacs.6b01151","article-title":"Electronic structure of the ferryl intermediate in the \u03b1-ketoglutarate dependent non-heme Iron Halogenase SyrB2: contributions to H atom abstraction reactivity","volume":"138","author":"Srnec","year":"2016","journal-title":"J. Am. Chem. Soc."},{"issue":"4","key":"10.1016\/j.jinorgbio.2025.113107_bb0125","doi-asserted-by":"crossref","first-page":"2489","DOI":"10.1021\/acscatal.2c06241","volume":"13","year":"2023","journal-title":"ACS Catal."},{"issue":"40","key":"10.1016\/j.jinorgbio.2025.113107_bb0130","doi-asserted-by":"crossref","first-page":"14426","DOI":"10.1021\/ja905206k","article-title":"First-principles study of non-heme Fe(II) halogenase SyrB2 reactivity","volume":"131","author":"Kulik","year":"2009","journal-title":"J. Am. Chem. Soc."},{"issue":"12","key":"10.1016\/j.jinorgbio.2025.113107_bb0135","doi-asserted-by":"crossref","first-page":"9342","DOI":"10.1021\/acscatal.4c02704","article-title":"Conformational isomerization of the Fe(III)\u2013OH species enables selective halogenation in carrier-protein-independent halogenase BesD and hydroxylase-evolved Halogenase","volume":"14","author":"Zhang","year":"2024","journal-title":"ACS Catal."},{"key":"10.1016\/j.jinorgbio.2025.113107_bb0140","doi-asserted-by":"crossref","DOI":"10.3389\/fchem.2018.00513","article-title":"Does substrate positioning affect the selectivity and reactivity in the hectochlorin biosynthesis halogenase?","volume":"6","author":"Timmins","year":"2018","journal-title":"Front. Chem."},{"issue":"7458","key":"10.1016\/j.jinorgbio.2025.113107_bb0145","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1038\/nature12304","article-title":"Elucidation of the Fe(iv)=O intermediate in the catalytic cycle of the halogenase SyrB2","volume":"499","author":"Wong","year":"2013","journal-title":"Nature"},{"issue":"14","key":"10.1016\/j.jinorgbio.2025.113107_bb0150","doi-asserted-by":"crossref","first-page":"3482","DOI":"10.1021\/ja011220v","article-title":"Hydrogen-bond-mediated tuning of the redox potential of the non-heme Fe site of superoxide dismutase","volume":"124","author":"Yikilmaz","year":"2002","journal-title":"J. Am. Chem. Soc."},{"issue":"45","key":"10.1016\/j.jinorgbio.2025.113107_bb0155","doi-asserted-by":"crossref","first-page":"20641","DOI":"10.1021\/jacs.2c07224","article-title":"Nonheme iron(III) azide and iron(III) isothiocyanate complexes: radical rebound reactivity, selectivity, and catalysis","volume":"144","author":"Yadav","year":"2022","journal-title":"J. Am. Chem. Soc."},{"issue":"43","key":"10.1016\/j.jinorgbio.2025.113107_bb0160","doi-asserted-by":"crossref","first-page":"17830","DOI":"10.1021\/acs.inorgchem.3c02617","article-title":"Selective radical transfer in a series of nonheme Iron(III) complexes","volume":"62","author":"Yadav","year":"2023","journal-title":"Inorg. Chem."},{"issue":"26","key":"10.1016\/j.jinorgbio.2025.113107_bb0165","doi-asserted-by":"crossref","first-page":"10148","DOI":"10.1021\/jacs.9b03329","article-title":"Dioxygen-derived nonheme mononuclear FeIII(OH) complex and its reactivity with carbon radicals","volume":"141","author":"Yadav","year":"2019","journal-title":"J. Am. Chem. Soc."},{"issue":"13","key":"10.1016\/j.jinorgbio.2025.113107_bb0170","doi-asserted-by":"crossref","first-page":"5762","DOI":"10.1021\/ic800073t","article-title":"Synthesis, X-ray crystallographic characterization, and electronic structure studies of a di-azide iron(III) complex: implications for the azide adducts of iron(III) superoxide dismutase","volume":"47","author":"Grove","year":"2008","journal-title":"Inorg. Chem."},{"issue":"32","key":"10.1016\/j.jinorgbio.2025.113107_bb0175","doi-asserted-by":"crossref","first-page":"10075","DOI":"10.1021\/jacs.8b04266","article-title":"Hydrogen bonds dictate O2 capture and release within a zinc tripod","volume":"140","author":"Dahl","year":"2018","journal-title":"J. Am. Chem. Soc."},{"issue":"2","key":"10.1016\/j.jinorgbio.2025.113107_bb0180","doi-asserted-by":"crossref","first-page":"985","DOI":"10.1021\/acs.jctc.0c01279","article-title":"Quantitative comparison of experimental and computed IR-spectra extracted from Ab initio molecular dynamics","volume":"17","author":"Esch","year":"2021","journal-title":"J. Chem. Theory Comput."},{"key":"10.1016\/j.jinorgbio.2025.113107_bb0185","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.ica.2012.10.037","article-title":"Bis(isothiocyanato)iron(II) complexes with bithiazole ligands: structure and magnetic studies","volume":"395","author":"Abedi","year":"2013","journal-title":"Inorg. Chim. Acta"},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.113107_bb0190","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1080\/10610270008029805","article-title":"Understanding the peculiarities of azide and thiocyanate binding in proteins: use of the small molecule structural data","volume":"12","author":"Tchertanov","year":"2000","journal-title":"Supramol. Chem."},{"issue":"6","key":"10.1016\/j.jinorgbio.2025.113107_bb0195","doi-asserted-by":"crossref","first-page":"1826","DOI":"10.1021\/ic0487068","article-title":"Spectroscopy of non-heme Iron thiolate complexes: insight into the electronic structure of the low-spin active site of nitrile hydratase","volume":"44","author":"Kennepohl","year":"2005","journal-title":"Inorg. Chem."},{"issue":"9","key":"10.1016\/j.jinorgbio.2025.113107_bb0200","doi-asserted-by":"crossref","first-page":"2176","DOI":"10.1021\/om100106e","article-title":"NMR chemical shifts of trace impurities: common laboratory solvents, organics, and gases in deuterated solvents relevant to the organometallic chemist","volume":"29","author":"Fulmer","year":"2010","journal-title":"Organometallics"}],"container-title":["Journal of Inorganic Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0162013425002880?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0162013425002880?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,6,7]],"date-time":"2026-06-07T08:30:43Z","timestamp":1780821043000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0162013425002880"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2]]},"references-count":40,"alternative-id":["S0162013425002880"],"URL":"https:\/\/doi.org\/10.1016\/j.jinorgbio.2025.113107","relation":{},"ISSN":["0162-0134"],"issn-type":[{"value":"0162-0134","type":"print"}],"subject":[],"published":{"date-parts":[[2026,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Examining Pseudohalide (N3, NCS, NCO) Coordination in Nonheme Fe(II) and Fe(III) Complexes","name":"articletitle","label":"Article Title"},{"value":"Journal of Inorganic Biochemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jinorgbio.2025.113107","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"113107"}}