{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,8]],"date-time":"2026-05-08T17:58:57Z","timestamp":1778263137159,"version":"3.51.4"},"reference-count":37,"publisher":"Springer Science and Business Media LLC","issue":"6","license":[{"start":{"date-parts":[[2022,5,5]],"date-time":"2022-05-05T00:00:00Z","timestamp":1651708800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2022,5,5]],"date-time":"2022-05-05T00:00:00Z","timestamp":1651708800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/100000165","name":"Division of Chemistry","doi-asserted-by":"publisher","award":["1904494"],"award-info":[{"award-number":["1904494"]}],"id":[{"id":"10.13039\/100000165","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000165","name":"Division of Chemistry","doi-asserted-by":"publisher","award":["2041047"],"award-info":[{"award-number":["2041047"]}],"id":[{"id":"10.13039\/100000165","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["5P20GM103436"],"award-info":[{"award-number":["5P20GM103436"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["F32GM137461"],"award-info":[{"award-number":["F32GM137461"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["K12GM063651"],"award-info":[{"award-number":["K12GM063651"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["P20GM113117"],"award-info":[{"award-number":["P20GM113117"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01GM127655"],"award-info":[{"award-number":["R01GM127655"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["T32GM008545"],"award-info":[{"award-number":["T32GM008545"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["J Biol Inorg Chem"],"abstract":"<jats:title>Abstract<\/jats:title><jats:p><jats:italic>Pseudomonas aeruginosa<\/jats:italic> is an increasingly antibiotic-resistant pathogen that causes severe lung infections, burn wound infections, and diabetic foot infections. <jats:italic>P. aeruginosa<\/jats:italic> produces the siderophore pyochelin through the use of a non-ribosomal peptide synthetase (NRPS) biosynthetic pathway. Targeting members of siderophore NRPS proteins is one avenue currently under investigation for the development of new antibiotics against antibiotic-resistant organisms. Here, the crystal structure of the pyochelin adenylation domain PchD is reported. The structure was solved to 2.11\u00a0\u00c5 when co-crystallized with the adenylation inhibitor 5\u2032-<jats:italic>O<\/jats:italic>-(N-salicylsulfamoyl)adenosine (salicyl-AMS) and to 1.69\u00a0\u00c5 with a modified version of salicyl-AMS designed to target an active site cysteine (4-cyano-salicyl-AMS). In the structures, PchD adopts the adenylation conformation, similar to that reported for AB3403 from <jats:italic>Acinetobacter baumannii<\/jats:italic>.<\/jats:p>\n                <jats:p><jats:bold>Graphical abstract<\/jats:bold><\/jats:p>","DOI":"10.1007\/s00775-022-01941-8","type":"journal-article","created":{"date-parts":[[2022,5,5]],"date-time":"2022-05-05T18:04:28Z","timestamp":1651773868000},"page":"541-551","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Rational inhibitor design for Pseudomonas aeruginosa salicylate adenylation enzyme PchD"],"prefix":"10.1007","volume":"27","author":[{"given":"Catherine L.","family":"Shelton","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kathleen M.","family":"Meneely","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Trey A.","family":"Ronnebaum","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Annemarie S.","family":"Chilton","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andrew P.","family":"Riley","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Thomas E.","family":"Prisinzano","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2352-2130","authenticated-orcid":false,"given":"Audrey L.","family":"Lamb","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2022,5,5]]},"reference":[{"issue":"8","key":"1941_CR1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1000949","volume":"6","author":"EP Skaar","year":"2010","unstructured":"Skaar EP (2010) The battle for iron between bacterial pathogens and their vertebrate hosts. PLoS Pathog 6(8):e1000949","journal-title":"PLoS Pathog"},{"issue":"11","key":"1941_CR2","doi-asserted-by":"publisher","first-page":"3517","DOI":"10.1128\/JB.00010-09","volume":"191","author":"A Braud","year":"2009","unstructured":"Braud A, Hannauer M, Mislin GL, Schalk IJ (2009) The Pseudomonas aeruginosa pyochelin-iron uptake pathway and its metal specificity. J Bacteriol 191(11):3517\u20133525","journal-title":"J Bacteriol"},{"issue":"11","key":"1941_CR3","doi-asserted-by":"publisher","first-page":"2844","DOI":"10.1111\/j.1462-2920.2011.02556.x","volume":"13","author":"IJ Schalk","year":"2011","unstructured":"Schalk IJ, Hannauer M, Braud A (2011) New roles for bacterial siderophores in metal transport and tolerance. Environ Microbiol 13(11):2844\u20132854","journal-title":"Environ Microbiol"},{"issue":"1","key":"1941_CR4","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1128\/iai.36.1.17-23.1982","volume":"36","author":"CD Cox","year":"1982","unstructured":"Cox CD (1982) Effect of pyochelin on the virulence of Pseudomonas aeruginosa. Infect Immun 36(1):17\u201323","journal-title":"Infect Immun"},{"issue":"9","key":"1941_CR5","doi-asserted-by":"publisher","first-page":"2021","DOI":"10.1128\/iai.55.9.2021-2025.1987","volume":"55","author":"PA Sokol","year":"1987","unstructured":"Sokol PA (1987) Surface expression of ferripyochelin-binding protein is required for virulence of Pseudomonas aeruginosa. Infect Immun 55(9):2021\u20132025","journal-title":"Infect Immun"},{"key":"1941_CR6","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.sbi.2018.01.015","volume":"53","author":"TA Ronnebaum","year":"2018","unstructured":"Ronnebaum TA, Lamb AL (2018) Nonribosomal peptides for iron acquisition: pyochelin biosynthesis as a case study. Curr Opin Struct Biol 53:1\u201311","journal-title":"Curr Opin Struct Biol"},{"issue":"11","key":"1941_CR7","doi-asserted-by":"publisher","first-page":"631","DOI":"10.1016\/S1074-5521(98)90291-5","volume":"5","author":"LE Quadri","year":"1998","unstructured":"Quadri LE, Sello J, Keating TA, Weinreb PH, Walsh CT (1998) Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin. Chem Biol 5(11):631\u2013645","journal-title":"Chem Biol"},{"issue":"10","key":"1941_CR8","doi-asserted-by":"publisher","first-page":"811","DOI":"10.1021\/cb900156h","volume":"4","author":"AM Gulick","year":"2009","unstructured":"Gulick AM (2009) Conformational dynamics in the Acyl-CoA synthetases, adenylation domains of non-ribosomal peptide synthetases, and firefly luciferase. ACS Chem Biol 4(10):811\u2013827","journal-title":"ACS Chem Biol"},{"issue":"7585","key":"1941_CR9","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1038\/nature16163","volume":"529","author":"EJ Drake","year":"2016","unstructured":"Drake EJ, Miller BR, Shi C, Tarrasch JT, Sundlov JA, Allen CL et al (2016) Structures of two distinct conformations of holo-non-ribosomal peptide synthetases. Nature 529(7585):235\u2013238","journal-title":"Nature"},{"key":"1941_CR10","volume-title":"Antibiotic Resistance Threats in the United States, 2019","author":"CDC","year":"2019","unstructured":"CDC (2019) Antibiotic Resistance Threats in the United States, 2019. US Department of Health and Human Services, Atlanta, GA"},{"issue":"8","key":"1941_CR11","doi-asserted-by":"publisher","first-page":"1054","DOI":"10.1016\/j.bbapap.2015.05.001","volume":"1854","author":"AL Lamb","year":"2015","unstructured":"Lamb AL (2015) Breaking a pathogen\u2019s iron will: Inhibiting siderophore production as an antimicrobial strategy. Biochim Biophys Acta 1854(8):1054\u20131070","journal-title":"Biochim Biophys Acta"},{"issue":"9","key":"1941_CR12","doi-asserted-by":"publisher","first-page":"903","DOI":"10.1002\/cbic.200300666","volume":"4","author":"R Finking","year":"2003","unstructured":"Finking R, Neumuller A, Solsbacher J, Konz D, Kretzschmar G, Schweitzer M et al (2003) Aminoacyl adenylate substrate analogues for the inhibition of adenylation domains of nonribosomal peptide synthetases. ChemBioChem 4(9):903\u2013906","journal-title":"ChemBioChem"},{"issue":"1","key":"1941_CR13","doi-asserted-by":"publisher","first-page":"29","DOI":"10.1038\/nchembio706","volume":"1","author":"JA Ferreras","year":"2005","unstructured":"Ferreras JA, Ryu J-S, Di Lello F, Tan DS, Quadri LE (2005) Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis. Nat Chem Biol 1(1):29\u201332","journal-title":"Nat Chem Biol"},{"issue":"1","key":"1941_CR14","doi-asserted-by":"publisher","first-page":"31","DOI":"10.1021\/jm051060o","volume":"49","author":"RV Somu","year":"2006","unstructured":"Somu RV, Boshoff H, Qiao C, Bennett EM, Barry CE 3rd, Aldrich CC (2006) Rationally designed nucleoside antibiotics that inhibit siderophore biosynthesis of Mycobacterium tuberculosis. J Med Chem 49(1):31\u201334","journal-title":"J Med Chem"},{"issue":"26","key":"1941_CR15","doi-asserted-by":"publisher","first-page":"7623","DOI":"10.1021\/jm061068d","volume":"49","author":"RV Somu","year":"2006","unstructured":"Somu RV, Wilson DJ, Bennett EM, Boshoff HI, Celia L, Beck BJ et al (2006) Antitubercular nucleosides that inhibit siderophore biosynthesis: SAR of the glycosyl domain. J Med Chem 49(26):7623\u20137635","journal-title":"J Med Chem"},{"issue":"21","key":"1941_CR16","doi-asserted-by":"publisher","first-page":"4707","DOI":"10.1021\/ol0617289","volume":"8","author":"J Vannada","year":"2006","unstructured":"Vannada J, Bennett EM, Wilson DJ, Boshoff HI, Barry CE 3rd, Aldrich CC (2006) Design, synthesis, and biological evaluation of beta-ketosulfonamide adenylation inhibitors as potential antitubercular agents. Org Lett 8(21):4707\u20134710","journal-title":"Org Lett"},{"issue":"24","key":"1941_CR17","doi-asserted-by":"publisher","first-page":"6080","DOI":"10.1021\/jm070905o","volume":"50","author":"C Qiao","year":"2007","unstructured":"Qiao C, Gupte A, Boshoff HI, Wilson DJ, Bennett EM, Somu RV et al (2007) 5\u2019-O-[(N-acyl)sulfamoyl]adenosines as antitubercular agents that inhibit MbtA: an adenylation enzyme required for siderophore biosynthesis of the mycobactins. J Med Chem 50(24):6080\u20136094","journal-title":"J Med Chem"},{"issue":"23","key":"1941_CR18","doi-asserted-by":"publisher","first-page":"7495","DOI":"10.1021\/jm8008037","volume":"51","author":"A Gupte","year":"2008","unstructured":"Gupte A, Boshoff HI, Wilson DJ, Neres J, Labello NP, Somu RV et al (2008) Inhibition of siderophore biosynthesis by 2-triazole substituted analogues of 5\u2019-O-[N-(salicyl)sulfamoyl]adenosine: antibacterial nucleosides effective against Mycobacterium tuberculosis. J Med Chem 51(23):7495\u20137507","journal-title":"J Med Chem"},{"issue":"17","key":"1941_CR19","doi-asserted-by":"publisher","first-page":"5349","DOI":"10.1021\/jm800567v","volume":"51","author":"J Neres","year":"2008","unstructured":"Neres J, Labello NP, Somu RV, Boshoff HI, Wilson DJ, Vannada J et al (2008) Inhibition of siderophore biosynthesis in Mycobacterium tuberculosis with nucleoside bisubstrate analogues: structure-activity relationships of the nucleobase domain of 5\u2019-O-[N-(salicyl)sulfamoyl]adenosine. J Med Chem 51(17):5349\u20135370","journal-title":"J Med Chem"},{"issue":"15","key":"1941_CR20","doi-asserted-by":"publisher","first-page":"7470","DOI":"10.1021\/jo400976f","volume":"78","author":"CA Engelhart","year":"2013","unstructured":"Engelhart CA, Aldrich CC (2013) Synthesis of chromone, quinolone, and benzoxazinone sulfonamide nucleosides as conformationally constrained inhibitors of adenylating enzymes required for siderophore biosynthesis. J Org Chem 78(15):7470\u20137481","journal-title":"J Org Chem"},{"issue":"10","key":"1941_CR21","doi-asserted-by":"publisher","first-page":"4835","DOI":"10.1021\/acs.joc.5b00550","volume":"80","author":"S Dawadi","year":"2015","unstructured":"Dawadi S, Viswanathan K, Boshoff HI, Barry CE 3rd, Aldrich CC (2015) Investigation and conformational analysis of fluorinated nucleoside antibiotics targeting siderophore biosynthesis. J Org Chem 80(10):4835\u20134850","journal-title":"J Org Chem"},{"issue":"14","key":"1941_CR22","doi-asserted-by":"publisher","first-page":"5459","DOI":"10.1021\/acs.jmedchem.5b00391","volume":"58","author":"KM Nelson","year":"2015","unstructured":"Nelson KM, Viswanathan K, Dawadi S, Duckworth BP, Boshoff HI, Barry CE 3rd et al (2015) Synthesis and Pharmacokinetic Evaluation of Siderophore Biosynthesis Inhibitors for Mycobacterium tuberculosis. J Med Chem 58(14):5459\u20135475","journal-title":"J Med Chem"},{"issue":"4","key":"1941_CR23","doi-asserted-by":"publisher","first-page":"386","DOI":"10.1021\/acsmedchemlett.8b00090","volume":"9","author":"S Dawadi","year":"2018","unstructured":"Dawadi S, Boshoff HIM, Park SW, Schnappinger D, Aldrich CC (2018) Conformationally constrained cinnolinone nucleoside analogues as siderophore biosynthesis inhibitors for tuberculosis. ACS Med Chem Lett 9(4):386\u2013391","journal-title":"ACS Med Chem Lett"},{"issue":"42","key":"1941_CR24","doi-asserted-by":"publisher","first-page":"22315","DOI":"10.1074\/jbc.M116.744532","volume":"291","author":"O Vergnolle","year":"2016","unstructured":"Vergnolle O, Xu H, Tufariello JM, Favrot L, Malek AA, Jacobs WR Jr et al (2016) Post-translational acetylation of MbtA modulates Mycobacterial siderophore biosynthesis. J Biol Chem 291(42):22315\u201322326","journal-title":"J Biol Chem"},{"issue":"Pt 2","key":"1941_CR25","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1107\/S0907444909047337","volume":"D66","author":"W Kabsch","year":"2010","unstructured":"Kabsch W (2010) XDS. Acta Crystallogr D Biol Crystallogr D66(Pt 2):125\u2013132","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"issue":"Pt 4","key":"1941_CR26","doi-asserted-by":"publisher","first-page":"658","DOI":"10.1107\/S0021889807021206","volume":"40","author":"AJ McCoy","year":"2007","unstructured":"McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC, Read RJ (2007) Phaser crystallographic software. J Appl Crystallogr 40(Pt 4):658\u2013674","journal-title":"J Appl Crystallogr"},{"issue":"Pt 2","key":"1941_CR27","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1107\/S0907444909052925","volume":"66","author":"PD Adams","year":"2010","unstructured":"Adams PD, Afonine PV, Bunkoczi G, Chen VB, Davis IW, Echols N et al (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213\u2013221","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"issue":"19","key":"1941_CR28","doi-asserted-by":"publisher","first-page":"12120","DOI":"10.1073\/pnas.182156699","volume":"99","author":"JJ May","year":"2002","unstructured":"May JJ, Kessler N, Marahiel MA, Stubbs MT (2002) Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases. Proc Natl Acad Sci USA 99(19):12120\u201312125","journal-title":"Proc Natl Acad Sci USA"},{"issue":"Pt 12 Pt 1","key":"1941_CR29","first-page":"2126","volume":"D60","author":"P Emsley","year":"2004","unstructured":"Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Cryst D60(Pt 12 Pt 1):2126\u20132132","journal-title":"Acta Cryst"},{"key":"1941_CR30","doi-asserted-by":"crossref","unstructured":"Afonine PV, Grosse-Kunstleve RW, Echols N, Headd JJ, Moriarty NW, Mustyakimov M, et al. (2012) Towards automated crystallographic structure refinement with phenix refine. Acta Crystallogr D Biol Crystallogr 68(4):352\u201367.","DOI":"10.1107\/S0907444912001308"},{"issue":"Pt 10","key":"1941_CR31","doi-asserted-by":"publisher","first-page":"1074","DOI":"10.1107\/S0907444909029436","volume":"65","author":"NW Moriarty","year":"2009","unstructured":"Moriarty NW, Grosse-Kunstleve RW, Adams PD (2009) electronic Ligand Builder and Optimization Workbench (eLBOW): a tool for ligand coordinate and restraint generation. Acta Crystallogr D Biol Crystallogr 65(Pt 10):1074\u20131080","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"issue":"Pt 8","key":"1941_CR32","doi-asserted-by":"publisher","first-page":"915","DOI":"10.1107\/S0907444906017161","volume":"62","author":"TC Terwilliger","year":"2006","unstructured":"Terwilliger TC, Klei H, Adams PD, Moriarty NW, Cohn JD (2006) Automated ligand fitting by core-fragment fitting and extension into density. Acta Crystallogr D Biol Crystallogr 62(Pt 8):915\u2013922","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"issue":"Pt 1","key":"1941_CR33","doi-asserted-by":"publisher","first-page":"101","DOI":"10.1107\/S0907444906046233","volume":"63","author":"TC Terwilliger","year":"2007","unstructured":"Terwilliger TC, Adams PD, Moriarty NW, Cohn JD (2007) Ligand identification using electron-density map correlations. Acta Crystallogr D Biol Crystallogr 63(Pt 1):101\u2013107","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"issue":"Pt 1","key":"1941_CR34","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1107\/S0907444909042073","volume":"66","author":"VB Chen","year":"2010","unstructured":"Chen VB, Arendall WB 3rd, Headd JJ, Keedy DA, Immormino RM, Kapral GJ et al (2010) MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66(Pt 1):12\u201321","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"issue":"Pt 12 Pt 1","key":"1941_CR35","doi-asserted-by":"publisher","first-page":"2256","DOI":"10.1107\/S0907444904026460","volume":"60","author":"E Krissinel","year":"2004","unstructured":"Krissinel E, Henrick K (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2256\u20132268","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"1941_CR36","doi-asserted-by":"crossref","unstructured":"Zaitseva J, Meneely KM, Lamb AL. Structure of Escherichia coli malate dehydrogenase at 1.45 A resolution. Acta Crystallogr Sect F 2009;65(Pt 9):866\u20139.","DOI":"10.1107\/S1744309109032217"},{"issue":"4","key":"1941_CR37","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1038\/nrd3410","volume":"10","author":"J Singh","year":"2011","unstructured":"Singh J, Petter RC, Baillie TA, Whitty A (2011) The resurgence of covalent drugs. Nat Rev Drug Discov 10(4):307\u2013317","journal-title":"Nat Rev Drug Discov"}],"container-title":["JBIC Journal of Biological Inorganic Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00775-022-01941-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s00775-022-01941-8\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00775-022-01941-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,9,13]],"date-time":"2022-09-13T08:22:08Z","timestamp":1663057328000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s00775-022-01941-8"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,5,5]]},"references-count":37,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2022,9]]}},"alternative-id":["1941"],"URL":"https:\/\/doi.org\/10.1007\/s00775-022-01941-8","relation":{},"ISSN":["1432-1327"],"issn-type":[{"value":"1432-1327","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,5,5]]},"assertion":[{"value":"20 February 2022","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"21 April 2022","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"5 May 2022","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no conflict of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}}]}}