{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,29]],"date-time":"2026-05-29T23:40:05Z","timestamp":1780098005138,"version":"3.54.0"},"reference-count":76,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,6,1]],"date-time":"2025-06-01T00:00:00Z","timestamp":1748736000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100005415","name":"H\u00e1sk\u00f3li \u00cdslands","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005415","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["bmn.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Current Opinion in Chemical Biology"],"published-print":{"date-parts":[[2025,6]]},"DOI":"10.1016\/j.cbpa.2025.102584","type":"journal-article","created":{"date-parts":[[2025,3,12]],"date-time":"2025-03-12T16:49:49Z","timestamp":1741798189000},"page":"102584","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"special_numbering":"C","title":["Noncytotoxic catalytic enzyme functional mimics including cyanide poisoning antidotes"],"prefix":"10.1016","volume":"86","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4283-6140","authenticated-orcid":false,"given":"Sigridur G.","family":"Suman","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.cbpa.2025.102584_bib1","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/j.cbpa.2015.01.024","article-title":"Approaches to the design of catalytic metallodrugs","volume":"25","author":"Soldevila-Barreda","year":"2015","journal-title":"Curr Opin Chem Biol"},{"key":"10.1016\/j.cbpa.2025.102584_bib2","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.cbpa.2012.01.013","article-title":"The potential of organometallic complexes in medicinal chemistry","volume":"16","author":"Gasser","year":"2012","journal-title":"Curr Opin Chem Biol"},{"key":"10.1016\/j.cbpa.2025.102584_bib3","doi-asserted-by":"crossref","DOI":"10.1016\/j.ica.2021.120754","article-title":"Recent advances in catalytic anticancer drugs: mechanistic investigations and future prospects","volume":"533","author":"Tyagi","year":"2022","journal-title":"Inorg Chim Acta"},{"key":"10.1016\/j.cbpa.2025.102584_bib4","doi-asserted-by":"crossref","DOI":"10.1016\/j.ccr.2023.215230","article-title":"Interweaving catalysis and cancer using Ru- and Os-arene complexes to alter cellular redox state: a structure-activity relationship (SAR) review","volume":"491","author":"Swaminathan","year":"2023","journal-title":"Coord Chem Rev"},{"key":"10.1016\/j.cbpa.2025.102584_bib5","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.cbpa.2014.12.021","article-title":"Transition-metal-mediated uncaging in living human cells\u2014an emerging alternative to photolabile protecting groups","volume":"25","author":"V\u00f6lker","year":"2015","journal-title":"Curr Opin Chem Biol"},{"key":"10.1016\/j.cbpa.2025.102584_bib6","doi-asserted-by":"crossref","DOI":"10.1002\/smll.202000392","article-title":"Artificial metalloenzymes: recent developments and innovations in bioinorganic catalysis","volume":"16","author":"Thompson","year":"2020","journal-title":"Small"},{"key":"10.1016\/j.cbpa.2025.102584_bib7","doi-asserted-by":"crossref","first-page":"12046","DOI":"10.1021\/acs.chemrev.1c01025","article-title":"Catalysis and electron transfer in de novo designed metalloproteins","volume":"122","author":"Koebke","year":"2022","journal-title":"Chem Rev"},{"key":"10.1016\/j.cbpa.2025.102584_bib8","doi-asserted-by":"crossref","DOI":"10.1016\/j.cbpa.2021.102109","article-title":"SOD mimics: from the tool box of the chemists to cellular studies","volume":"67","author":"Policar","year":"2022","journal-title":"Curr Opin Chem Biol"},{"key":"10.1016\/j.cbpa.2025.102584_bib9","doi-asserted-by":"crossref","DOI":"10.1016\/j.ccr.2021.214104","article-title":"Advancement of metal compounds as therapeutic and diagnostic metallodrugs: current frontiers and future perspectives","volume":"445","author":"Yousuf","year":"2021","journal-title":"Coord Chem Rev"},{"key":"10.1016\/j.cbpa.2025.102584_sref10","doi-asserted-by":"crossref","DOI":"10.1002\/anie.202306645","article-title":"Transition metal catalysis in living cells: progress, challenges, and novel supramolecular solutions","volume":"62","author":"James","year":"2023","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2025.102584_sref11","doi-asserted-by":"crossref","first-page":"8911","DOI":"10.1039\/D3CC01380D","article-title":"Distinct chemical factors in hydrolytic reactions catalyzed by metalloenzymes and metal complexes","volume":"59","author":"Serafim","year":"2023","journal-title":"Chem Commun"},{"key":"10.1016\/j.cbpa.2025.102584_sref12","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1021\/acs.joc.2c00956","article-title":"Cyanine-functionalized 2,2\u2032-bipyridine compounds for photocatalytic cancer therapy","volume":"88","author":"Zhu","year":"2023","journal-title":"J Org Chem"},{"key":"10.1016\/j.cbpa.2025.102584_bib13","first-page":"361","article-title":"Chapter Eleven - design and applications of catalytic metallodrugs containing the ATCUN motif","volume":"vol. 75","author":"Yu","year":"2020"},{"key":"10.1016\/j.cbpa.2025.102584_bib14","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1007\/s00775-023-01994-3","article-title":"Targeting cancer lactate metabolism with synergistic combinations of synthetic catalysts and monocarboxylate transporter inhibitors","volume":"28","author":"Bridgewater","year":"2023","journal-title":"J Biol Inorg Chem"},{"key":"10.1016\/j.cbpa.2025.102584_bib15","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1039\/D0CB00150C","article-title":"Transfer hydrogenation catalysis in cells","volume":"2","author":"Banerjee","year":"2021","journal-title":"RSC Chem Biol"},{"key":"10.1016\/j.cbpa.2025.102584_bib16","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.cbpa.2013.01.004","article-title":"Targeted delivery of platinum-based anticancer complexes","volume":"17","author":"Butler","year":"2013","journal-title":"Curr Opin Chem Biol"},{"key":"10.1016\/j.cbpa.2025.102584_bib17","doi-asserted-by":"crossref","first-page":"1890","DOI":"10.1002\/asia.200800149","article-title":"Medicinal organometallic chemistry: designing metal arene complexes as anticancer agents","volume":"3","author":"Peacock","year":"2008","journal-title":"Chem Asian J"},{"key":"10.1016\/j.cbpa.2025.102584_sref18","doi-asserted-by":"crossref","DOI":"10.3390\/ijms24065382","article-title":"Biological consequences of vanadium effects on formation of reactive oxygen species and lipid peroxidation","volume":"24","author":"Aureliano","year":"2023","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.cbpa.2025.102584_sref19","doi-asserted-by":"crossref","first-page":"8747","DOI":"10.1021\/acs.inorgchem.3c00766","article-title":"A series of Ni complexes based on a versatile ATCUN-like tripeptide scaffold to decipher key parameters for superoxide dismutase activity","volume":"62","author":"Domergue","year":"2023","journal-title":"Inorg Chem"},{"key":"10.1016\/j.cbpa.2025.102584_sref20","doi-asserted-by":"crossref","DOI":"10.1016\/j.jinorgbio.2022.112062","article-title":"ROS scavenging of SOD\/CAT mimics probed by EPR and reduction of lipid peroxidation in S. cerevisiae and mouse liver, under severe hydroxyl radical stress condition","volume":"239","author":"Menezes","year":"2023","journal-title":"J Inorg Biochem"},{"key":"10.1016\/j.cbpa.2025.102584_bib21","doi-asserted-by":"crossref","first-page":"4513","DOI":"10.1021\/acs.inorgchem.2c00113","article-title":"Mo(VI) potential metallodrugs: explaining the transport and cytotoxicity by chemical transformations","volume":"61","author":"Mohanty","year":"2022","journal-title":"Inorg Chem"},{"key":"10.1016\/j.cbpa.2025.102584_bib22","doi-asserted-by":"crossref","first-page":"9474","DOI":"10.1002\/anie.202015671","article-title":"In-vitro and in-vivo photocatalytic cancer therapy with biocompatible iridium(III) photocatalysts","volume":"60","author":"Huang","year":"2021","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2025.102584_bib23","doi-asserted-by":"crossref","first-page":"2480","DOI":"10.1002\/cmdc.202100297","article-title":"Metal-based catalytic drug development for next-generation cancer therapy","volume":"16","author":"Fan","year":"2021","journal-title":"ChemMedChem"},{"key":"10.1016\/j.cbpa.2025.102584_bib24","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1007\/s00775-019-01732-8","article-title":"Anticancer activity, DNA binding and cell mechanistic studies of estrogen-functionalised Cu(II) complexes","volume":"25","author":"Barrett","year":"2020","journal-title":"J Biol Inorg Chem"},{"key":"10.1016\/j.cbpa.2025.102584_bib25","doi-asserted-by":"crossref","DOI":"10.1002\/hlca.202300001","article-title":"Ruthenium catalysis in biological habitats","volume":"106","author":"Guti\u00e9rrez-Gonz\u00e1lez","year":"2023","journal-title":"Helv Chim Acta"},{"key":"10.1016\/j.cbpa.2025.102584_sref26","doi-asserted-by":"crossref","first-page":"8756","DOI":"10.1021\/jacs.8b04326","article-title":"Receptor-based artificial metalloenzymes on living human cells","volume":"140","author":"Ghattas","year":"2018","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2025.102584_bib27","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1021\/acs.accounts.0c00031","article-title":"Molecular modeling for artificial metalloenzyme design and optimization","volume":"53","author":"Alonso-Cotchico","year":"2020","journal-title":"Acc Chem Res"},{"key":"10.1016\/j.cbpa.2025.102584_bib28","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1038\/nature19114","article-title":"Directed evolution of artificial metalloenzymes for in vivo metathesis","volume":"537","author":"Jeschek","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.cbpa.2025.102584_sref29","doi-asserted-by":"crossref","first-page":"6424","DOI":"10.1021\/acs.nanolett.3c01186","article-title":"An antibody engineered metalloenzyme for mediating cell\u2013cell communication and activation of immuno- and chemotherapy","volume":"23","author":"Liu","year":"2023","journal-title":"Nano Lett"},{"key":"10.1016\/j.cbpa.2025.102584_bib30","doi-asserted-by":"crossref","first-page":"12446","DOI":"10.1002\/anie.202100369","article-title":"Prodrug activation by gold artificial metalloenzyme-catalyzed synthesis of phenanthridinium derivatives via hydroamination","volume":"60","author":"Chang","year":"2021","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2025.102584_sref31","doi-asserted-by":"crossref","DOI":"10.1021\/jacs.3c13647","article-title":"Intracellular synthesis of indoles enabled by visible-light photocatalysis","author":"D'Avino","year":"2024","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2025.102584_sref32","doi-asserted-by":"crossref","DOI":"10.1016\/j.jinorgbio.2022.111914","article-title":"An artificial metalloprotein with metal-adaptive coordination sites and Ni-dependent quercetinase activity","volume":"235","author":"Beaumet","year":"2022","journal-title":"J Inorg Biochem"},{"key":"10.1016\/j.cbpa.2025.102584_sref33","doi-asserted-by":"crossref","DOI":"10.1016\/j.tchem.2022.100013","article-title":"Enzymatic intermolecular Diels-Alder reactions in synthesis: from nature to design","volume":"2","author":"Gao","year":"2022","journal-title":"Tetrahedron Chem"},{"key":"10.1016\/j.cbpa.2025.102584_bib34","doi-asserted-by":"crossref","DOI":"10.3390\/molecules25194540","article-title":"Synthesis, characterisation and in vitro anticancer activity of catalytically active indole-based half-sandwich complexes","volume":"25","author":"Soldevila-Barreda","year":"2020","journal-title":"Molecules"},{"key":"10.1016\/j.cbpa.2025.102584_bib35","doi-asserted-by":"crossref","first-page":"620","DOI":"10.1016\/0003-2697(78)90790-X","article-title":"Isoelectric points of proteins: a table","volume":"86","author":"Malamud","year":"1978","journal-title":"Anal Biochem"},{"key":"10.1016\/j.cbpa.2025.102584_bib36","doi-asserted-by":"crossref","first-page":"7332","DOI":"10.1002\/anie.201906551","article-title":"Bio-inspired nonheme iron oxidation catalysis: involvement of oxoiron(V) oxidants in cleaving strong C\u2212H bonds","volume":"59","author":"Kal","year":"2020","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2025.102584_bib37","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1186\/s12858-015-0039-4","article-title":"Nickel quercetinase, a \u201cpromiscuous\u201d metalloenzyme: metal incorporation and metal ligand substitution studies","volume":"16","author":"Nianios","year":"2015","journal-title":"BMC Biochem"},{"key":"10.1016\/j.cbpa.2025.102584_bib38","doi-asserted-by":"crossref","first-page":"6974","DOI":"10.1002\/anie.200900942","article-title":"Bioorthogonal chemistry: fishing for selectivity in a sea of functionality","volume":"48","author":"Sletten","year":"2009","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2025.102584_bib39","doi-asserted-by":"crossref","first-page":"5151","DOI":"10.1002\/anie.201002106","article-title":"An artificial metalloenzyme: creation of a designed copper binding site in a thermostable protein","volume":"49","author":"Podtetenieff","year":"2010","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2025.102584_bib40","doi-asserted-by":"crossref","first-page":"17064","DOI":"10.1039\/D2DT02853K","article-title":"The effects of metal cofactors on the reactivity of quercetin 2,4-dioxygenase: synthetic model studies with M(II)-complexes (M = Mn, Co, Ni, Cu, Zn) and assessment of the regulatory factors in catalytic efficacy","volume":"51","author":"Podder","year":"2022","journal-title":"Dalton Trans"},{"key":"10.1016\/j.cbpa.2025.102584_bib41","doi-asserted-by":"crossref","first-page":"130","DOI":"10.3390\/antiox10010130","article-title":"Catalytic antioxidants in the kidney","volume":"10","author":"Hong","year":"2021","journal-title":"Antioxidants"},{"key":"10.1016\/j.cbpa.2025.102584_bib42","first-page":"122","article-title":"On the history of oxidative stress: concept and some aspects of current development","volume":"7","author":"Sies","year":"2018","journal-title":"Curr. Op. Tox."},{"key":"10.1016\/j.cbpa.2025.102584_bib43","doi-asserted-by":"crossref","DOI":"10.1155\/2012\/936486","article-title":"Reactive oxygen species in health and disease","volume":"2012","author":"Alfadda","year":"2012","journal-title":"J Biomed Biotechnol"},{"key":"10.1016\/j.cbpa.2025.102584_sref44","article-title":"Deciphering the metal speciation in low-molecular-weight complexes by IMS-MS: application to the detection of manganese superoxide dismutase mimics in cell lysates","volume":"61","author":"Zoumpoulaki","year":"2022","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2025.102584_bib45","doi-asserted-by":"crossref","first-page":"3905","DOI":"10.1039\/D1QI00542A","article-title":"Rhenium carbonyl complexes bearing methylated triphenylphosphonium cations as antibody-free mitochondria trackers for X-ray fluorescence imaging","volume":"8","author":"Schanne","year":"2021","journal-title":"Inorg Chem Front"},{"key":"10.1016\/j.cbpa.2025.102584_bib46","series-title":"Redox-active therapeutics","first-page":"125","article-title":"Why and how: bio-inspired manganese complexes as SOD mimic","author":"Policar","year":"2016"},{"key":"10.1016\/j.cbpa.2025.102584_sref47","doi-asserted-by":"crossref","DOI":"10.1155\/2022\/3858122","article-title":"Inertness of superoxide dismutase mimics Mn(II) complexes based on an open-chain ligand, bioactivity, and detection in intestinal epithelial cells","volume":"2022","author":"Schanne","year":"2022","journal-title":"Oxid Med Cell Longev"},{"key":"10.1016\/j.cbpa.2025.102584_bib48","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1021\/acs.inorgchem.6b02695","article-title":"A cell-penetrant manganese superoxide dismutase (MnSOD) mimic is able to complement MnSOD and exerts an antiinflammatory effect on cellular and animal models of inflammatory bowel diseases","volume":"56","author":"Mathieu","year":"2017","journal-title":"Inorg Chem"},{"key":"10.1016\/j.cbpa.2025.102584_bib49","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1039\/C9CC07920C","article-title":"An easy-to-implement combinatorial approach involving an activity-based assay for the discovery of a peptidyl copper complex mimicking superoxide dismutase","volume":"56","author":"Vincent","year":"2020","journal-title":"Chem Commun"},{"key":"10.1016\/j.cbpa.2025.102584_sref50","doi-asserted-by":"crossref","first-page":"5476","DOI":"10.3390\/molecules27175476","article-title":"Improvement of peptidyl copper complexes mimicking catalase: a subtle balance between thermodynamic stability and resistance towards H2O2 degradation","volume":"27","author":"Ben Hadj Hammouda","year":"2022","journal-title":"Molecules"},{"key":"10.1016\/j.cbpa.2025.102584_bib51","doi-asserted-by":"crossref","DOI":"10.1016\/j.poly.2022.115879","article-title":"The biocatalytic activity of the \u201clantern-like\u201d binuclear copper complex with trisulfide bridges mimicking SOD metallo-proteins","volume":"221","author":"Caro-Ramirez","year":"2022","journal-title":"Polyhedron"},{"key":"10.1016\/j.cbpa.2025.102584_bib52","doi-asserted-by":"crossref","first-page":"1799","DOI":"10.1351\/pac200880081799","article-title":"Catalytic metallodrugs","volume":"80","author":"Cowan","year":"2008","journal-title":"Pure Appl Chem"},{"key":"10.1016\/j.cbpa.2025.102584_bib53","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1590\/1414-431X20133086","article-title":"Target-directed catalytic metallodrugs","volume":"46","author":"Joyner","year":"2013","journal-title":"Braz J Med Biol Res"},{"key":"10.1016\/j.cbpa.2025.102584_sref54","doi-asserted-by":"crossref","first-page":"12772","DOI":"10.1021\/acs.inorgchem.1c00899","article-title":"A bioinspired NiII superoxide dismutase catalyst designed on an ATCUN-like binding motif","volume":"60","author":"Domergue","year":"2021","journal-title":"Inorg Chem"},{"key":"10.1016\/j.cbpa.2025.102584_bib55","doi-asserted-by":"crossref","DOI":"10.1002\/anie.202409343","article-title":"Outstanding superoxide dismutase catalytic activity of simple peptide-based nickel(II) complexes","volume":"63","author":"Guinard","year":"2024","journal-title":"Angew Chem Int Ed"},{"key":"10.1016\/j.cbpa.2025.102584_bib56","series-title":"Targeted metallo-drugs","first-page":"216","article-title":"Challenges in targeting cyanide poisoning: advantages in exploiting metal complexes in its treatment","volume":"vol. 24","author":"Suman","year":"2023"},{"key":"10.1016\/j.cbpa.2025.102584_bib57","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1016\/S0021-9258(19)42997-9","article-title":"An expanded mechanism for rhodanese catalysis","volume":"249","author":"Schlesinger","year":"1974","journal-title":"J Biol Chem"},{"key":"10.1016\/j.cbpa.2025.102584_bib58","first-page":"359","article-title":"Chemical and clinical aspects of metal-containing antidotes for poisoning by cyanide","volume":"vol. 19","author":"Suman","year":"2019"},{"key":"10.1016\/j.cbpa.2025.102584_bib59","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/0162-0134(86)80075-7","article-title":"Molybdenum in enzymatic and heterogeneous catalysis","volume":"28","author":"Mitchell","year":"1986","journal-title":"J Inorg Biochem"},{"key":"10.1016\/j.cbpa.2025.102584_bib60","doi-asserted-by":"crossref","first-page":"2694","DOI":"10.1016\/S0021-9258(19)85792-7","article-title":"Mechanisms of inactivation of molybdoenzymes by cyanide","volume":"255","author":"Coughlan","year":"1980","journal-title":"J Biol Chem"},{"key":"10.1016\/j.cbpa.2025.102584_bib61","doi-asserted-by":"crossref","first-page":"1892","DOI":"10.1016\/S0021-9258(18)93525-8","article-title":"The mechanism of the rhodanese-catalyzed thiosulfate cyanide reaction","volume":"243","author":"Leininger","year":"1967","journal-title":"J Biol Chem"},{"key":"10.1016\/j.cbpa.2025.102584_bib62","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1080\/10408440802304944","article-title":"Which cyanide antidote?","volume":"39","author":"Hall","year":"2009","journal-title":"Crit Rev Toxicol"},{"key":"10.1016\/j.cbpa.2025.102584_bib63","first-page":"1","article-title":"Dimethyl trisulfide: a novel cyanide countermeasure","author":"Rockwood","year":"2016","journal-title":"Toxicol Ind Health"},{"key":"10.1016\/j.cbpa.2025.102584_bib64","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1006\/faat.1994.1080","article-title":"Encapsulation of rhodanese and organic thiosulfonates by mouse erythrocytes","volume":"23","author":"Petrikovics","year":"1994","journal-title":"Fund Appl Toxicol"},{"key":"10.1016\/j.cbpa.2025.102584_sref65","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijpharm.2021.121260","article-title":"Long-term pharmaceutical stability of liposome-encapsulated methemoglobin as an antidote for cyanide poisoning","volume":"610","author":"Suzuki","year":"2021","journal-title":"Int J Pharm"},{"key":"10.1016\/j.cbpa.2025.102584_sref66","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.jconrel.2021.07.015","article-title":"Liposome-encapsulated methemoglobin as an antidote against cyanide poisoning","volume":"337","author":"Suzuki","year":"2021","journal-title":"J Contr Release"},{"key":"10.1016\/j.cbpa.2025.102584_bib67","doi-asserted-by":"crossref","first-page":"960","DOI":"10.1039\/j19680000960","article-title":"Reactivity differences between haemoglobins. Part VIII. The thermodynamics of the reaction of human methaemoglobins A and C with fluoride, thiocyanate, and cyanide ions. An interpretation of enthalpy changes in terms of hydration","author":"Anusiem","year":"1968","journal-title":"J Chem Soc Inorg Phys Theor"},{"key":"10.1016\/j.cbpa.2025.102584_bib68","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1021\/acs.chemrestox.7b00314","article-title":"A comparison of the cyanide-scavenging capabilities of some cobalt-containing complexes in mice","volume":"31","author":"Cronican","year":"2018","journal-title":"Chem Res Toxicol"},{"key":"10.1016\/j.cbpa.2025.102584_bib69","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1007\/s13181-016-0566-4","article-title":"The vitamin B(12) analog cobinamide is an effective antidote for oral cyanide poisoning","volume":"12","author":"Lee","year":"2016","journal-title":"J Med Toxicol"},{"key":"10.1016\/j.cbpa.2025.102584_sref70","doi-asserted-by":"crossref","first-page":"907","DOI":"10.1021\/acsptsci.2c00093","article-title":"In vitro characterization of a threonine-ligated molybdenyl\u2013sulfide cluster as a putative cyanide poisoning antidote; intracellular distribution, effects on organic osmolyte homeostasis, and induction of cell death","volume":"5","author":"Gretarsdottir","year":"2022","journal-title":"ACS Pharmacol Transl Sci"},{"key":"10.1016\/j.cbpa.2025.102584_sref71","doi-asserted-by":"crossref","first-page":"18190","DOI":"10.1021\/acs.inorgchem.0c02672","article-title":"Water-Soluble \u03b1-amino acid complexes of molybdenum as potential antidotes for cyanide poisoning: synthesis and catalytic studies of threonine, methionine, serine, and leucine complexes","volume":"59","author":"Gretarsdottir","year":"2020","journal-title":"Inorg Chem"},{"key":"10.1016\/j.cbpa.2025.102584_bib72","doi-asserted-by":"crossref","first-page":"5271","DOI":"10.1021\/ja00014a021","volume":"113","author":"Coucouvanis","year":"1991","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.cbpa.2025.102584_bib73","first-page":"1","article-title":"Syntheses, structures, and reactions of binary and tertiary thiomolybdate complexes containing the (O)Mo(sx) and (S)Mo(sx) functional groups (x = 1, 2, 4)","volume":"vol. 45","author":"Coucouvanis","year":"1998"},{"key":"10.1016\/j.cbpa.2025.102584_bib74","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/S0162-0134(00)80050-1","article-title":"Reactions of molybdenum-sulfur compounds with cyanide: chemical evolution and deactivation of molybdoenzymes","volume":"11","author":"Mitchell","year":"1979","journal-title":"J Inorg Biochem"},{"key":"10.1016\/j.cbpa.2025.102584_bib75","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1016\/j.jinorgbio.2016.01.020","article-title":"Cytotoxicity studies of water soluble coordination compounds with a [Mo2O2S2]2+ core","volume":"160","author":"Gretarsdottir","year":"2016","journal-title":"J Inorg Biochem"},{"key":"10.1016\/j.cbpa.2025.102584_bib76","doi-asserted-by":"crossref","first-page":"7644","DOI":"10.1021\/acs.inorgchem.0c00608","article-title":"Reaction chemistry of the syn-[Mo2O2(\u03bc-S)2(S2)(DMF)3] complex with cyanide and catalytic thiocyanate formation","volume":"59","author":"Suman","year":"2020","journal-title":"Inorg Chem"}],"container-title":["Current Opinion in Chemical Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S136759312500016X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S136759312500016X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,6,5]],"date-time":"2025-06-05T22:11:59Z","timestamp":1749161519000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S136759312500016X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,6]]},"references-count":76,"alternative-id":["S136759312500016X"],"URL":"https:\/\/doi.org\/10.1016\/j.cbpa.2025.102584","relation":{},"ISSN":["1367-5931"],"issn-type":[{"value":"1367-5931","type":"print"}],"subject":[],"published":{"date-parts":[[2025,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Noncytotoxic catalytic enzyme functional mimics including cyanide poisoning antidotes","name":"articletitle","label":"Article Title"},{"value":"Current Opinion in Chemical Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cbpa.2025.102584","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"102584"}}