{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T10:03:06Z","timestamp":1777629786597,"version":"3.51.4"},"reference-count":40,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[2020,3,1]],"date-time":"2020-03-01T00:00:00Z","timestamp":1583020800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,3,1]],"date-time":"2020-03-01T00:00:00Z","timestamp":1583020800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2020,3,1]],"date-time":"2020-03-01T00:00:00Z","timestamp":1583020800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2020,3,1]],"date-time":"2020-03-01T00:00:00Z","timestamp":1583020800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2020,3,1]],"date-time":"2020-03-01T00:00:00Z","timestamp":1583020800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2020,3,1]],"date-time":"2020-03-01T00:00:00Z","timestamp":1583020800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2020,3,1]],"date-time":"2020-03-01T00:00:00Z","timestamp":1583020800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["SH87\/1-1"],"award-info":[{"award-number":["SH87\/1-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004189","name":"Max-Planck-Gesellschaft","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004189","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004543","name":"China Scholarship Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004543","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100007769","name":"Max-Planck-Institut f\u00fcr Terrestrische Mikrobiologie","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100007769","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003398","name":"Shanxi Scholarship Council of China","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003398","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2020,3]]},"DOI":"10.1016\/j.jmb.2020.01.042","type":"journal-article","created":{"date-parts":[[2020,2,13]],"date-time":"2020-02-13T02:20:18Z","timestamp":1581560418000},"page":"2042-2054","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":8,"title":["The Hydride Transfer Process in NADP-dependent Methylene-tetrahydromethanopterin Dehydrogenase"],"prefix":"10.1016","volume":"432","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4115-284X","authenticated-orcid":false,"given":"Gangfeng","family":"Huang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3382-8969","authenticated-orcid":false,"given":"Tristan","family":"Wagner","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ulrike","family":"Demmer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Eberhard","family":"Warkentin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ulrich","family":"Ermler","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1872-8705","authenticated-orcid":false,"given":"Seigo","family":"Shima","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2020.01.042_bib1","doi-asserted-by":"crossref","first-page":"2359","DOI":"10.1128\/JB.00029-13","article-title":"Elucidation of the role of the methylene-tetrahydromethanopterin dehydrogenase MtdA in the tetrahydromethanopterin-dependent oxidation pathway in Methylobacterium extorquens AM1","volume":"195","author":"Martinez-Gomez","year":"2013","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.jmb.2020.01.042_bib2","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1126\/science.281.5373.99","article-title":"C1 transfer enzymes and coenzymes linking methylotrophic Bacteria and methanogenic Archaea","volume":"281","author":"Chistoserdova","year":"1998","journal-title":"Science"},{"key":"10.1016\/j.jmb.2020.01.042_bib3","doi-asserted-by":"crossref","first-page":"5750","DOI":"10.1128\/JB.181.18.5750-5757.1999","article-title":"Distribution of tetrahydromethanopterin-dependent enzymes in methylotrophic bacteria and phylogeny of methenyl tetrahydromethanopterin cyclohydrolases","volume":"181","author":"Vorholt","year":"1999","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.jmb.2020.01.042_bib4","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1146\/annurev.bi.59.070190.002035","article-title":"Unusual coenzymes of methanogenesis","volume":"59","author":"Dimarco","year":"1990","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jmb.2020.01.042_bib5","doi-asserted-by":"crossref","first-page":"3431","DOI":"10.1111\/1462-2920.12475","article-title":"A\u00a0reversed genetic approach reveals the coenzyme specificity and other catalytic properties of three enzymes putatively involved in anaerobic oxidation of methane with sulfate","volume":"16","author":"Kojima","year":"2014","journal-title":"Environ. Microbiol."},{"key":"10.1016\/j.jmb.2020.01.042_bib6","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1007\/BF00425174","article-title":"Function of methanofuran, tetrahydromethanopterin, and coenzyme-F420 in Archaeoglobus-Fulgidus","volume":"152","author":"M\u00f6ller-Zinkhan","year":"1989","journal-title":"Arch. Microbiol."},{"key":"10.1016\/j.jmb.2020.01.042_bib7","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1007\/s00203-004-0714-0","article-title":"Tetrahydrofolate-specific enzymes in Methanosarcina barkeri and growth dependence of this methanogenic archaeon on folic acid or p-aminobenzoic acid","volume":"182","author":"Buchenau","year":"2004","journal-title":"Arch. Microbiol."},{"key":"10.1016\/j.jmb.2020.01.042_bib8","doi-asserted-by":"crossref","first-page":"5351","DOI":"10.1128\/JB.180.20.5351-5356.1998","article-title":"The NADP-dependent methylene tetrahydromethanopterin dehydrogenase in Methylobacterium extorquens AM1","volume":"180","author":"Vorholt","year":"1998","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.jmb.2020.01.042_bib9","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/S0014-5793(01)02306-7","article-title":"Re-face stereospecificity of NADP dependent methylenetetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1 as determined by NMR spectroscopy","volume":"494","author":"Hagemeier","year":"2001","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jmb.2020.01.042_bib10","doi-asserted-by":"crossref","first-page":"3031","DOI":"10.1021\/cr9500601","article-title":"Reactions with molecular hydrogen in microorganisms: evidence for a purely organic hydrogenation catalyst","volume":"96","author":"Thauer","year":"1996","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jmb.2020.01.042_bib11","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1016\/S0969-2126(02)00802-X","article-title":"Structure of methylene-tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1","volume":"10","author":"Ermler","year":"2002","journal-title":"Structure"},{"key":"10.1016\/j.jmb.2020.01.042_bib12","doi-asserted-by":"crossref","first-page":"9917","DOI":"10.1002\/anie.201006255","article-title":"Iron-chromophore circular dichroism of [Fe]-hydrogenase: the conformational change required for H2 activation","volume":"49","author":"Shima","year":"2010","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.jmb.2020.01.042_bib13","doi-asserted-by":"crossref","first-page":"Pr41","DOI":"10.1021\/cr1001035","article-title":"Update 1 of: tunneling and dynamics in enzymatic hydride transfer","volume":"110","author":"Nagel","year":"2010","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jmb.2020.01.042_bib14","doi-asserted-by":"crossref","first-page":"6241","DOI":"10.1074\/jbc.RA117.000149","article-title":"Structural basis for the catalytic mechanism and a-ketoglutarate cooperativity of glutamate dehydrogenase","volume":"293","author":"Prakash","year":"2018","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jmb.2020.01.042_bib15","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1038\/12307","article-title":"A\u00a0productive NADP+ binding mode of ferredoxin-NADP+ reductase revealed by protein engineering and crystallographic studies","volume":"6","author":"Deng","year":"1999","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.jmb.2020.01.042_bib16","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1002\/1439-7633(20010803)2:7\/8<530::AID-CBIC530>3.0.CO;2-0","article-title":"Re-face stereospecificity of methylenetetrahydromethanopterin and methylenetetrahydrofolate dehydrogenases is predetermined by intrinsic properties of the substrate","volume":"2","author":"Bartoschek","year":"2001","journal-title":"Chembiochem"},{"key":"10.1016\/j.jmb.2020.01.042_bib17","doi-asserted-by":"crossref","first-page":"13712","DOI":"10.1074\/jbc.M412320200","article-title":"How an enzyme binds the C1 carrier tetrahydromethanopterin - structure of the tetrahydromethanopterin-dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1","volume":"280","author":"Acharya","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jmb.2020.01.042_bib18","doi-asserted-by":"crossref","first-page":"3762","DOI":"10.1046\/j.1432-1327.2000.01413.x","article-title":"Characterization of a second methylene tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1","volume":"267","author":"Hagemeier","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jmb.2020.01.042_bib19","doi-asserted-by":"crossref","first-page":"3218","DOI":"10.1021\/bi982719d","article-title":"Enzymatic H-transfer requires vibration-driven extreme tunneling","volume":"38","author":"Basran","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2020.01.042_bib20","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1146\/annurev-biochem-051710-133623","article-title":"Hydrogen tunneling links protein dynamics to enzyme catalysis","volume":"82","author":"Klinman","year":"2013","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jmb.2020.01.042_bib21","doi-asserted-by":"crossref","first-page":"3930","DOI":"10.1111\/j.1742-4658.2009.07121.x","article-title":"Structural and mechanistic aspects of flavoproteins: probes of hydrogen tunnelling","volume":"276","author":"Hay","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/j.jmb.2020.01.042_bib22","doi-asserted-by":"crossref","first-page":"30775","DOI":"10.1039\/C5CP00614G","article-title":"Nuclear quantum tunnelling in enzymatic reactions-an enzymologist's perspective","volume":"17","author":"Johannissen","year":"2015","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.jmb.2020.01.042_bib23","series-title":"The Theory of Rate Processes: the kinetics of chemical reactions, viscosity, diffusion and electrochemical phenomena","author":"Gladstone","year":"1941"},{"key":"10.1016\/j.jmb.2020.01.042_bib24","doi-asserted-by":"crossref","first-page":"3302","DOI":"10.1111\/febs.14190","article-title":"High-resolution studies of hydride transfer in the ferredoxin:NADP+ reductase superfamily","volume":"284","author":"Kean","year":"2017","journal-title":"FEBS J."},{"key":"10.1016\/j.jmb.2020.01.042_bib25","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/j.jmb.2008.06.083","article-title":"Catalytic cycle of human glutathione reductase near 1 \u00c5 resolution","volume":"382","author":"Berkholz","year":"2008","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jmb.2020.01.042_bib26","doi-asserted-by":"crossref","first-page":"978","DOI":"10.1016\/j.str.2017.05.002","article-title":"Mechanism-informed refinement reveals altered substrate-binding mode for catalytically competent nitroreductase","volume":"25","author":"Pitsawong","year":"2017","journal-title":"Structure"},{"key":"10.1016\/j.jmb.2020.01.042_bib27","doi-asserted-by":"crossref","first-page":"1452","DOI":"10.1002\/anie.200805502","article-title":"Barrier compression enhances an enzymatic hydrogen-transfer reaction","volume":"48","author":"Hay","year":"2009","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.jmb.2020.01.042_bib28","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1016\/S0022-2836(03)00949-5","article-title":"Coenzyme F420 dependent methylenetetrahydromethanopterin dehydrogenase (Mtd) from Methanopyrus kandleri: a methanogenic enzyme with an unusual quaternary structure","volume":"332","author":"Hagemeier","year":"2003","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jmb.2020.01.042_bib29","doi-asserted-by":"crossref","first-page":"10098","DOI":"10.1021\/bi901104d","article-title":"Structural basis of the hydride transfer mechanism in F420-dependent methylenetetrahydromethanopterin dehydrogenase","volume":"48","author":"Ceh","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2020.01.042_bib30","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/S0076-6879(01)31069-8","article-title":"Tetrahydromethanopterin-specific enzymes from Methanopyrus kandleri","volume":"331","author":"Shima","year":"2001","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jmb.2020.01.042_bib31","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1038\/s41929-019-0289-4","article-title":"The atomic-resolution crystal structure of activated [Fe]-hydrogenase","volume":"2","author":"Huang","year":"2019","journal-title":"Nat. Catal."},{"key":"10.1016\/j.jmb.2020.01.042_bib32","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1107\/S0907444910048675","article-title":"iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM","volume":"67","author":"Battye","year":"2011","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/j.jmb.2020.01.042_bib33","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"Xds","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/j.jmb.2020.01.042_bib34","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1107\/S0907444913000061","article-title":"How good are my data and what is the resolution?","volume":"69","author":"Evans","year":"2013","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/j.jmb.2020.01.042_bib35","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1107\/S0021889897006766","article-title":"MOLREP: an automated program for molecular replacement","volume":"30","author":"Vagin","year":"1997","journal-title":"J.\u00a0Appl. Crystallogr."},{"key":"10.1016\/j.jmb.2020.01.042_bib36","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J.\u00a0Appl. Crystallogr."},{"key":"10.1016\/j.jmb.2020.01.042_bib37","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum-likelihood method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/j.jmb.2020.01.042_bib38","series-title":"BUSTER Version 2.10.1","author":"Bricogne","year":"2016"},{"key":"10.1016\/j.jmb.2020.01.042_bib39","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1107\/S0021889810015608","article-title":"phenix.model_vs_data: a high-level tool for the calculation of crystallographic model and data statistics","volume":"43","author":"Afonine","year":"2010","journal-title":"J.\u00a0Appl. Crystallogr."},{"key":"10.1016\/j.jmb.2020.01.042_bib40","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002228362030108X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002228362030108X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T02:39:05Z","timestamp":1777430345000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S002228362030108X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,3]]},"references-count":40,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2020,3]]}},"alternative-id":["S002228362030108X"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2020.01.042","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2020,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The Hydride Transfer Process in NADP-dependent Methylene-tetrahydromethanopterin Dehydrogenase","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2020.01.042","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}