{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,29]],"date-time":"2026-10-29T20:38:53Z","timestamp":1793306333467,"version":"4.5.0"},"reference-count":61,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,9,1]],"date-time":"2025-09-01T00:00:00Z","timestamp":1756684800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,9,1]],"date-time":"2025-09-01T00:00:00Z","timestamp":1756684800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,4,21]],"date-time":"2025-04-21T00:00:00Z","timestamp":1745193600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001665","name":"French National Research Agency","doi-asserted-by":"publisher","award":["ANR-23-07\\u20130002CE-01"],"award-info":[{"award-number":["ANR-23-07\\u20130002CE-01"]}],"id":[{"id":"10.13039\/501100001665","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":[[2025,9]]},"DOI":"10.1016\/j.jinorgbio.2025.112924","type":"journal-article","created":{"date-parts":[[2025,4,19]],"date-time":"2025-04-19T11:05:07Z","timestamp":1745060707000},"page":"112924","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"special_numbering":"C","title":["Lanthanide(III)-dependent hydration of the methanol dehydrogenase cofactor, pyrroloquinoline quinone"],"prefix":"10.1016","volume":"270","author":[{"given":"Camille","family":"Blanc","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lauriane","family":"Oriol","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thayalan","family":"Rajeshkumar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Bijani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charles-Louis","family":"Serpentini","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicolas","family":"Giraud","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laurent","family":"Maron","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christelle","family":"Hureau","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emilie","family":"Mathieu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"6","key":"10.1016\/j.jinorgbio.2025.112924_bb0005","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1039\/c0nj00969e","article-title":"Rare earths: jewels for functional materials of the future","volume":"35","author":"Eliseeva","year":"2011","journal-title":"New J. Chem."},{"issue":"20","key":"10.1016\/j.jinorgbio.2025.112924_bb0010","doi-asserted-by":"crossref","first-page":"10083","DOI":"10.1021\/acs.inorgchem.6b00919","article-title":"Lanthanide chemistry: from coordination in chemical complexes shaping our technology to coordination in enzymes shaping bacterial metabolism","volume":"55","author":"Martinez-Gomez","year":"2016","journal-title":"Inorg. Chem."},{"issue":"6237","key":"10.1016\/j.jinorgbio.2025.112924_bb0015","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1126\/science.aaa9091","article-title":"Just Add Lanthanides","volume":"348","author":"Skovran","year":"2015","journal-title":"Science"},{"issue":"8","key":"10.1016\/j.jinorgbio.2025.112924_bb0020","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1007\/s11274-016-2088-2","article-title":"Lanthanides: new life metals?","volume":"32","author":"Chistoserdova","year":"2016","journal-title":"World J. Microbiol. Biotechnol."},{"issue":"37","key":"10.1016\/j.jinorgbio.2025.112924_bb0025","doi-asserted-by":"crossref","first-page":"12795","DOI":"10.1002\/anie.201904090","article-title":"Essential and ubiquitous: the emergence of lanthanide metallobiochemistry","volume":"58","author":"Daumann","year":"2019","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.jinorgbio.2025.112924_bb0030","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.cbpa.2018.09.019","article-title":"Role of rare earth elements in methanol oxidation","volume":"49","author":"Picone","year":"2019","journal-title":"Curr. Opin. Chem. Biol."},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.112924_bb0035","article-title":"The biochemistry of lanthanide acquisition, trafficking, and utilization","volume":"1868","author":"Featherston","year":"2021","journal-title":"Biochim. Biophys. Acta BBA - Mol. Cell Res."},{"issue":"7988","key":"10.1016\/j.jinorgbio.2025.112924_bb0040","doi-asserted-by":"crossref","first-page":"876","DOI":"10.1038\/d41586-023-03611-4","article-title":"Microbial miners take on rare-earth metals","volume":"623","author":"Dance","year":"2023","journal-title":"Nature"},{"issue":"5","key":"10.1016\/j.jinorgbio.2025.112924_bb0045","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1016\/j.tibtech.2023.10.011","article-title":"Engineering biomaterials for the recovery of rare earth elements","volume":"42","author":"Ye","year":"2024","journal-title":"Trends Biotechnol."},{"issue":"17","key":"10.1016\/j.jinorgbio.2025.112924_bb0050","doi-asserted-by":"crossref","first-page":"2184","DOI":"10.1007\/s00018-004-4156-2","article-title":"Lanthanide-binding peptides and the enzymes that might have been","volume":"61","author":"Lim","year":"2004","journal-title":"Cell. Mol. Life Sci. CMLS"},{"issue":"6","key":"10.1016\/j.jinorgbio.2025.112924_bb0055","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1016\/j.jbiosc.2011.01.015","article-title":"Molecular structure and gene analysis of ce3+-induced methanol dehydrogenase of bradyrhizobium Sp. MAFF211645","volume":"111","author":"Fitriyanto","year":"2011","journal-title":"J. Biosci. Bioeng."},{"issue":"5","key":"10.1016\/j.jinorgbio.2025.112924_bb0060","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1016\/j.jbiosc.2010.12.017","article-title":"Molecular structure of La3+-induced methanol dehydrogenase-like protein in methylobacterium radiotolerans","volume":"111","author":"Hibi","year":"2011","journal-title":"J. Biosci. Bioeng."},{"issue":"11","key":"10.1016\/j.jinorgbio.2025.112924_bb0065","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0050480","article-title":"A catalytic role of XoxF1 as La3+-dependent methanol dehydrogenase in methylobacterium extorquens strain AM1","volume":"7","author":"Nakagawa","year":"2012","journal-title":"PLoS One"},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.112924_bb0070","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1111\/1462-2920.12249","article-title":"Rare earth metals are essential for methanotrophic life in volcanic mudpots","volume":"16","author":"Pol","year":"2014","journal-title":"Environ. Microbiol."},{"issue":"14","key":"10.1016\/j.jinorgbio.2025.112924_bb0075","doi-asserted-by":"crossref","first-page":"6163","DOI":"10.1007\/s00253-014-5766-8","article-title":"PQQ-dependent methanol dehydrogenases: rare-earth elements make a difference","volume":"98","author":"Keltjens","year":"2014","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.jinorgbio.2025.112924_bb0080","doi-asserted-by":"crossref","DOI":"10.1007\/s00775-021-01852-0","article-title":"Bioinorganic insights of the PQQ-dependent alcohol dehydrogenases","author":"Sarmiento-Pav\u00eda","year":"2021","journal-title":"JBIC J. Biol. Inorg. Chem."},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.112924_bb0085","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1038\/s41467-022-28102-4","article-title":"Bio-inspired lanthanum-ortho-quinone catalysis for aerobic alcohol oxidation: semi-quinone anionic radical as redox ligand","volume":"13","author":"Zhang","year":"2022","journal-title":"Nat. Commun."},{"issue":"4","key":"10.1016\/j.jinorgbio.2025.112924_bb0090","doi-asserted-by":"crossref","first-page":"2162","DOI":"10.1021\/acscatal.3c05428","article-title":"Aerobic alcohol oxidation with a cerium\u2013phenanthrolinedione complex: a mimic of lanthanide-based methanol dehydrogenase","volume":"14","author":"Shen","year":"2024","journal-title":"ACS Catal."},{"issue":"33","key":"10.1016\/j.jinorgbio.2025.112924_bb0095","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2405836121","article-title":"Structure-driven development of a biomimetic rare earth artificial metalloprotein","volume":"121","author":"Thompson","year":"2024","journal-title":"Proc. Natl. Acad. Sci."},{"issue":"5725","key":"10.1016\/j.jinorgbio.2025.112924_bb0100","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1038\/280843a0","article-title":"A novel coenzyme from bacterial primary alcohol dehydrogenases","volume":"280","author":"Salisbury","year":"1979","journal-title":"Nature"},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.112924_bb0105","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1111\/j.1432-1033.1980.tb04711.x","article-title":"Structure and activity of the prosthetic group of methanol dehydrogenase","volume":"108","author":"Duine","year":"1980","journal-title":"Eur. J. Biochem."},{"issue":"3","key":"10.1016\/j.jinorgbio.2025.112924_bb0110","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/S1389-1723(00)80002-X","article-title":"The PQQ story","volume":"88","author":"Duine","year":"1999","journal-title":"J. Biosci. Bioeng."},{"issue":"3","key":"10.1016\/j.jinorgbio.2025.112924_bb0115","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/0302-4598(90)80012-8","article-title":"Voltammetric and spectroscopic studies of pyrroloquinoline quinone coenzyme under neutral and basic conditions","volume":"23","author":"Kano","year":"1990","journal-title":"Bioelectrochem. Bioenerg."},{"issue":"2","key":"10.1016\/j.jinorgbio.2025.112924_bb0120","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/0302-4598(90)85021-9","article-title":"Voltammetric determination of acid dissociation constants of pyrroloquinoline quinone and its reduced form under acidic conditions","volume":"24","author":"Kano","year":"1990","journal-title":"Bioelectrochem. Bioenerg."},{"issue":"16","key":"10.1016\/j.jinorgbio.2025.112924_bb0125","doi-asserted-by":"crossref","first-page":"12242","DOI":"10.1021\/acscatal.4c02319","article-title":"Redox properties of pyrroloquinoline quinone in pyranose dehydrogenase measured by direct electron transfer","volume":"14","author":"Takeda","year":"2024","journal-title":"ACS Catal."},{"issue":"29","key":"10.1016\/j.jinorgbio.2025.112924_bb0130","doi-asserted-by":"crossref","first-page":"7271","DOI":"10.1021\/ja9813663","article-title":"Electrochemical behavior and characterization of semiquinone radical anion species of coenzyme PQQ in aprotic organic media","volume":"120","author":"Itoh","year":"1998","journal-title":"J. Am. Chem. Soc."},{"issue":"22","key":"10.1016\/j.jinorgbio.2025.112924_bb0135","doi-asserted-by":"crossref","first-page":"9960","DOI":"10.1021\/ja00075a012","article-title":"C-4 and C-5 Adducts of Cofactor PQQ (Pyrroloquinolinequinone). Model studies directed toward the action of quinoprotein methanol dehydrogenase","volume":"115","author":"Itoh","year":"1993","journal-title":"J. Am. Chem. Soc."},{"issue":"2","key":"10.1016\/j.jinorgbio.2025.112924_bb0140","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1111\/j.1432-1033.1981.tb06415.x","article-title":"Characterization of the second prosthetic group in methanol dehydrogenase from hyphomicrobium X","volume":"118","author":"Duine","year":"1981","journal-title":"Eur. J. Biochem."},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.112924_bb0145","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1111\/j.1432-1033.1982.tb06652.x","article-title":"Covalent addition of H2O, enzyme substrates and activators to pyrrolo-quinoline quinone, the coenzyme of quinoproteins","volume":"125","author":"Dekker","year":"1982","journal-title":"Eur. J. Biochem."},{"issue":"25","key":"10.1016\/j.jinorgbio.2025.112924_bb0150","doi-asserted-by":"crossref","first-page":"15397","DOI":"10.1039\/D2CP00311B","article-title":"Studies of pyrroloquinoline quinone species in solution and in lanthanide-dependent methanol dehydrogenases","volume":"24","author":"Danaf","year":"2022","journal-title":"Phys. Chem. Chem. Phys."},{"issue":"1","key":"10.1016\/j.jinorgbio.2025.112924_bb0155","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/S1570-9639(03)00042-6","article-title":"The structure and mechanism of methanol dehydrogenase","volume":"1647","author":"Anthony","year":"2003","journal-title":"Biochim. Biophys. Acta BBA - Proteins Proteomics"},{"issue":"2","key":"10.1016\/j.jinorgbio.2025.112924_bb0160","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1021\/ja963366d","article-title":"Modeling of the chemistry of quinoprotein methanol dehydrogenase. oxidation of methanol by calcium complex of coenzyme PQQ via addition\u2212elimination mechanism","volume":"119","author":"Itoh","year":"1997","journal-title":"J. Am. Chem. Soc."},{"issue":"7","key":"10.1016\/j.jinorgbio.2025.112924_bb0165","doi-asserted-by":"crossref","first-page":"2109","DOI":"10.1002\/chem.200601123","article-title":"The preferred reaction path for the oxidation of methanol by PQQ-containing methanol dehydrogenase: addition\u2013elimination versus hydride-transfer mechanism","volume":"13","author":"Leopoldini","year":"2007","journal-title":"Chem. Eur. J."},{"issue":"2","key":"10.1016\/j.jinorgbio.2025.112924_bb0170","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1073\/pnas.98.2.432","article-title":"Catalytic mechanism of quinoprotein methanol dehydrogenase: a theoretical and x-Ray crystallographic investigation","volume":"98","author":"Zheng","year":"2001","journal-title":"Proc. Natl. Acad. Sci."},{"issue":"3","key":"10.1016\/j.jinorgbio.2025.112924_bb0175","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1073\/pnas.0610126104","article-title":"Mechanism of methanol oxidation by quinoprotein methanol dehydrogenase","volume":"104","author":"Zhang","year":"2007","journal-title":"Proc. Natl. Acad. Sci."},{"issue":"9","key":"10.1016\/j.jinorgbio.2025.112924_bb0180","doi-asserted-by":"crossref","first-page":"3359","DOI":"10.1021\/jacs.0c11414","article-title":"Mechanism of pyrroloquinoline quinone-dependent hydride transfer chemistry from spectroscopic and high-resolution X-ray structural studies of the methanol dehydrogenase from methylococcus capsulatus (Bath)","volume":"143","author":"Chan","year":"2021","journal-title":"J. Am. Chem. Soc."},{"issue":"36","key":"10.1016\/j.jinorgbio.2025.112924_bb0185","doi-asserted-by":"crossref","first-page":"8652","DOI":"10.1002\/chem.201700381","article-title":"How can methanol dehydrogenase from methylacidiphilum fumariolicum work with the alien ceiii ion in the active center? A theoretical study","volume":"23","author":"Prejan\u00f2","year":"2017","journal-title":"Chem. Eur. J."},{"issue":"4","key":"10.1016\/j.jinorgbio.2025.112924_bb0190","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1021\/jacs.7b12318","article-title":"Functional synthetic model for the lanthanide-dependent quinoid alcohol dehydrogenase active site","volume":"140","author":"McSkimming","year":"2018","journal-title":"J. Am. Chem. Soc."},{"issue":"31","key":"10.1016\/j.jinorgbio.2025.112924_bb0195","doi-asserted-by":"crossref","first-page":"10463","DOI":"10.1039\/C8DT01238E","article-title":"Impact of the lanthanide contraction on the activity of a lanthanide-dependent methanol dehydrogenase \u2013 a kinetic and DFT study","volume":"47","author":"Lumpe","year":"2018","journal-title":"Dalton Trans."},{"issue":"11","key":"10.1016\/j.jinorgbio.2025.112924_bb0200","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1002\/cbic.201800130","article-title":"Similar but not the same: first kinetic and structural analyses of a methanol dehydrogenase containing a europium ion in the active site","volume":"19","author":"Jahn","year":"2018","journal-title":"ChemBioChem"},{"key":"10.1016\/j.jinorgbio.2025.112924_bb0205","article-title":"Assessing lanthanide-dependent methanol dehydrogenase activity: the assay matters","author":"Phi","year":"2024","journal-title":"ChemBioChem"},{"issue":"31","key":"10.1016\/j.jinorgbio.2025.112924_bb0210","article-title":"Minor actinides can replace essential lanthanides in bacterial life**","volume":"62","author":"Singer","year":"2023","journal-title":"Angew. Chem. Int. Ed."},{"issue":"18","key":"10.1016\/j.jinorgbio.2025.112924_bb0215","doi-asserted-by":"crossref","first-page":"2360","DOI":"10.1002\/cbic.201900184","article-title":"Biochemical and structural characterization of XoxG and XoxJ and their roles in lanthanide-dependent methanol dehydrogenase activity","volume":"20","author":"Featherston","year":"2019","journal-title":"ChemBioChem"},{"issue":"4","key":"10.1016\/j.jinorgbio.2025.112924_bb0220","doi-asserted-by":"crossref","first-page":"1743","DOI":"10.1002\/chem.201405159","article-title":"DFT study of the active site of the XoxF-type natural, cerium-dependent methanol dehydrogenase enzyme","volume":"21","author":"Bogart","year":"2015","journal-title":"Chem. Eur. J."},{"issue":"39","key":"10.1016\/j.jinorgbio.2025.112924_bb0225","doi-asserted-by":"crossref","first-page":"21979","DOI":"10.1039\/C9CP03953H","article-title":"Lanthanide-induced conformational change of methanol dehydrogenase involving coordination change of cofactor pyrroloquinoline quinone","volume":"21","author":"Tsushima","year":"2019","journal-title":"Phys. Chem. Chem. Phys."},{"issue":"49","key":"10.1016\/j.jinorgbio.2025.112924_bb0230","doi-asserted-by":"crossref","first-page":"11334","DOI":"10.1002\/chem.202001855","article-title":"How lanthanide ions affect the addition\u2013elimination step of methanol dehydrogenases","volume":"26","author":"Prejan\u00f2","year":"2020","journal-title":"Chem. Eur. J."},{"key":"10.1016\/j.jinorgbio.2025.112924_bb0235","article-title":"The earlier the better: structural analysis and separation of lanthanides with pyrroloquinoline quinone","author":"Lumpe","year":"2020","journal-title":"Chem. Eur. J."},{"issue":"12","key":"10.1016\/j.jinorgbio.2025.112924_bb0240","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1107\/S2053229620014278","article-title":"Crystal structure of a Calcium(II)\u2013Pyrrolo\u00adquinoline Quinone (PQQ) complex outside a protein environment","volume":"76","author":"Lumpe","year":"2020","journal-title":"Acta Crystallogr. Sect. C Struct. Chem."},{"issue":"22","key":"10.1016\/j.jinorgbio.2025.112924_bb0245","doi-asserted-by":"crossref","first-page":"12794","DOI":"10.1039\/D0CP00989J","article-title":"The Effect of weighted averages when determining the speciation and structure\u2013property relationships of Europium(III) Dipicolinate complexes","volume":"22","author":"Nawrocki","year":"2020","journal-title":"Phys. Chem. Chem. Phys."},{"issue":"13","key":"10.1016\/j.jinorgbio.2025.112924_bb0250","doi-asserted-by":"crossref","first-page":"8432","DOI":"10.1021\/acs.inorgchem.9b00568","article-title":"Studies of redox cofactor pyrroloquinoline quinone and its interaction with lanthanides(III) and calcium(II)","volume":"58","author":"Lumpe","year":"2019","journal-title":"Inorg. Chem."},{"issue":"18","key":"10.1016\/j.jinorgbio.2025.112924_bb0255","doi-asserted-by":"crossref","first-page":"6562","DOI":"10.1021\/bi9800092","article-title":"Model studies on calcium-containing quinoprotein alcohol dehydrogenases. catalytic role of Ca2+ for the oxidation of alcohols by coenzyme PQQ (4,5-Dihydro-4,5-Dioxo-1H-Pyrrolo[2,3-f]Quinoline-2,7,9-Tricarboxylic Acid)","volume":"37","author":"Itoh","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.jinorgbio.2025.112924_bb0260","doi-asserted-by":"crossref","DOI":"10.1016\/j.ccr.2019.213146","article-title":"The chemical consequences of the gradual decrease of the ionic radius along the Ln-series","volume":"406","author":"Peters","year":"2020","journal-title":"Coord. Chem. Rev."},{"issue":"10","key":"10.1016\/j.jinorgbio.2025.112924_bb0265","doi-asserted-by":"crossref","first-page":"4572","DOI":"10.1021\/ic200260r","article-title":"Revised ionic radii of lanthanoid(III) ions in aqueous solution","volume":"50","author":"D\u2019Angelo","year":"2011","journal-title":"Inorg. Chem."},{"issue":"5","key":"10.1016\/j.jinorgbio.2025.112924_bb0270","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1107\/S0567739476001551","article-title":"Revised effective ionic radii and systematic studies of interatomic distances in halides and chalcogenides","volume":"32","author":"Shannon","year":"1976","journal-title":"Acta Crystallogr. Sect. A"},{"issue":"24","key":"10.1016\/j.jinorgbio.2025.112924_bb0275","doi-asserted-by":"crossref","first-page":"5752","DOI":"10.1021\/ja953943i","article-title":"Calcium ion coordination: a comparison with that of beryllium, magnesium, and zinc","volume":"118","author":"Katz","year":"1996","journal-title":"J. Am. Chem. Soc."},{"issue":"3","key":"10.1016\/j.jinorgbio.2025.112924_bb0280","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1021\/ja001533a","article-title":"Hydration of the calcium ion. An EXAFS, large-angle X-Ray scattering, and molecular dynamics simulation study","volume":"123","author":"Jalilehvand","year":"2001","journal-title":"J. Am. Chem. Soc."},{"issue":"15","key":"10.1016\/j.jinorgbio.2025.112924_bb0285","doi-asserted-by":"crossref","first-page":"1604","DOI":"10.1016\/j.ccr.2012.03.023","article-title":"Charge transfer excited states sensitization of lanthanide emitting from the visible to the Near-Infra-Red","volume":"256","author":"D\u2019Al\u00e9o","year":"2012","journal-title":"Coord. Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2025.112924_bb0290","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ccr.2015.02.015","article-title":"Interpretation of Europium(III) Spectra","volume":"295","author":"Binnemans","year":"2015","journal-title":"Coord. Chem. Rev."},{"issue":"6","key":"10.1016\/j.jinorgbio.2025.112924_bb0295","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1021\/cr00104a002","article-title":"Application of two-dimensional NMR to kinetics of chemical exchange","volume":"90","author":"Perrin","year":"1990","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jinorgbio.2025.112924_bb0300","article-title":"An Introduction to one- and two-dimensional lineshape analysis of chemically exchanging systems","volume":"16\u201317","author":"Waudby","year":"2023","journal-title":"J. Magn. Reson. Open"},{"issue":"30","key":"10.1016\/j.jinorgbio.2025.112924_bb0305","doi-asserted-by":"crossref","first-page":"7140","DOI":"10.1021\/jp0010278","article-title":"Do f electrons play a role in the lanthanide\u2212ligand bonds? A DFT study of Ln(NR2)3; R = H, SiH3","volume":"104","author":"Maron","year":"2000","journal-title":"J. Phys. Chem. A"}],"container-title":["Journal of Inorganic Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0162013425001047?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0162013425001047?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,7,17]],"date-time":"2025-07-17T08:33:08Z","timestamp":1752741188000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0162013425001047"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,9]]},"references-count":61,"alternative-id":["S0162013425001047"],"URL":"https:\/\/doi.org\/10.1016\/j.jinorgbio.2025.112924","relation":{},"ISSN":["0162-0134"],"issn-type":[{"value":"0162-0134","type":"print"}],"subject":[],"published":{"date-parts":[[2025,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Lanthanide(III)-dependent hydration of the methanol dehydrogenase cofactor, pyrroloquinoline quinone","name":"articletitle","label":"Article Title"},{"value":"Journal of Inorganic Biochemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jinorgbio.2025.112924","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Authors. Published by Elsevier Inc.","name":"copyright","label":"Copyright"}],"article-number":"112924"}}