{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T13:24:42Z","timestamp":1787059482913,"version":"build-2736575974"},"reference-count":60,"publisher":"American Chemical Society (ACS)","issue":"16","license":[{"start":{"date-parts":[[2026,8,5]],"date-time":"2026-08-05T00:00:00Z","timestamp":1785888000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,8,5]],"date-time":"2026-08-05T00:00:00Z","timestamp":1785888000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,8,5]],"date-time":"2026-08-05T00:00:00Z","timestamp":1785888000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/100007586","name":"Aix-Marseille Universit?","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/100007586","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010663","name":"H2020 European Research Council","doi-asserted-by":"publisher","award":["101229565"],"award-info":[{"award-number":["101229565"]}],"id":[{"id":"10.13039\/100010663","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-23-CE44-0023"],"award-info":[{"award-number":["ANR-23-CE44-0023"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009708","name":"Novo Nordisk Fonden","doi-asserted-by":"publisher","award":["NNF20OC0064747"],"award-info":[{"award-number":["NNF20OC0064747"]}],"id":[{"id":"10.13039\/501100009708","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,8,18]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Auxiliary activity family 7 (AA7) oxidoreductases are fungal flavoenzymes that catalyze the C1 oxidation of diverse oligosaccharides coupled to the reduction of molecular oxygen (oxidase activity) or organic molecules (dehydrogenase activity). These enzymes are predominantly derived from Ascomycota, with a smaller, less-explored fraction from Basidiomycota and Oomycota plant pathogens. Moreover, AA7 members are promising biocatalysts for the selective oxidation of carbohydrates, which is an enduring challenge in catalysis. However, the sequence space of AA7 enzymes remains largely uncharted, particularly within basidiomycota members, and the molecular determinants shaping substrate selectivity remain ill-defined. Focusing on the basidiomycete maize pathogen Ustilago maydis, we explored the boundaries of the AA7 sequence space by identifying and characterizing two enzymes, UmAA7A and UmAA7B, that are divergent from hitherto described members. We found that UmAA7s oxidize both chitooligosaccharides (CHOS) and their deacetylated forms (dCHOS) in an acetylation-site-dependent manner. The X-ray crystal structure of UmAA7A, sequence, and structural comparisons with a model of UmAA7B and other known CHOS-active AA7s, combined with docking analyses on CHOS and dCHOS, revealed specific active-site residues behind this unprecedented substrate specificity. Moreover, a previously not reported combination of a bicovalently tethered FAD and an atypical arrangement of residues at re-side of the FAD cofactor was associated with a mainly dehydrogenase activity profile, contrasting the majority of oxidases in AA7. Altogether, this work reveals the enzymatic oxidation of dCHOS, extending the substrate scope of AA7s and laying the biochemical foundation for uncovering their biological functions during plant infection.<\/jats:p>","DOI":"10.1021\/acs.biochem.6c00454","type":"journal-article","created":{"date-parts":[[2026,8,5]],"date-time":"2026-08-05T21:02:22Z","timestamp":1785963742000},"page":"2617-2628","source":"Crossref","is-referenced-by-count":0,"title":["A Pair of FAD-Dependent\nCarbohydrate Oxidases from\nthe Corn Smut Pathogen\n                    <i>Ustilago maydis<\/i>\n                    Oxidize Chitosan Oligomers"],"prefix":"10.1021","volume":"65","author":[{"given":"Roseline Assiah","family":"Yao","sequence":"first","affiliation":[{"name":"INRAE, Aix Marseille Univ, BBF, Biodiversite\u0301 et Biotechnologie Fongiques , ,","place":["Marseille, France, 13009"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Simone","family":"Turella","sequence":"additional","affiliation":[{"name":"Technical University of Denmark , , ,","place":["Lyngby, Denmark, DK-2800"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sanchari","family":"Banerjee","sequence":"additional","affiliation":[{"name":"Technical University of Denmark , , ,","place":["Lyngby, Denmark, DK-2800"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sara","family":"Vujakovic","sequence":"additional","affiliation":[{"name":"University of British Columbia , , , ,","place":["Vancouver, British Columbia, Canada, V6T 1Z4"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sacha","family":"Grisel","sequence":"additional","affiliation":[{"name":"INRAE, Aix Marseille Univ, BBF, Biodiversite\u0301 et Biotechnologie Fongiques , ,","place":["Marseille, France, 13009"]},{"name":"INRAE, Aix Marseille Univ, 3PE , ,","place":["Marseille, France, 13009"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mireille","family":"Haon","sequence":"additional","affiliation":[{"name":"INRAE, Aix Marseille Univ, BBF, Biodiversite\u0301 et Biotechnologie Fongiques , ,","place":["Marseille, France, 13009"]},{"name":"INRAE, Aix Marseille Univ, 3PE , ,","place":["Marseille, France, 13009"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bastien","family":"Annic","sequence":"additional","affiliation":[{"name":"INRAE, UR1268 BIA , ,","place":["Nantes, France, 44300"]},{"name":"INRAE, PROBE Research Infrastructure, BIBS Facility , ,","place":["Nantes, France, 44300"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4767-6940","authenticated-orcid":true,"given":"David","family":"Ropartz","sequence":"additional","affiliation":[{"name":"INRAE, UR1268 BIA , ,","place":["Nantes, France, 44300"]},{"name":"INRAE, PROBE Research Infrastructure, BIBS Facility , ,","place":["Nantes, France, 44300"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthias","family":"Kretschmer","sequence":"additional","affiliation":[{"name":"University of British Columbia , , , ,","place":["Vancouver, British Columbia, Canada, V6T 1Z4"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jens Preben","family":"Morth","sequence":"additional","affiliation":[{"name":"Technical University of Denmark , , ,","place":["Lyngby, Denmark, DK-2800"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Guy","family":"Berrin","sequence":"additional","affiliation":[{"name":"INRAE, Aix Marseille Univ, BBF, Biodiversite\u0301 et Biotechnologie Fongiques , ,","place":["Marseille, France, 13009"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4240-6976","authenticated-orcid":true,"given":"James","family":"Kronstad","sequence":"additional","affiliation":[{"name":"University of British Columbia , , , ,","place":["Vancouver, British Columbia, Canada, V6T 1Z4"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8250-1842","authenticated-orcid":true,"given":"Maher","family":"Abou Hachem","sequence":"additional","affiliation":[{"name":"Technical University of Denmark , , ,","place":["Lyngby, Denmark, DK-2800"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8354-3892","authenticated-orcid":true,"given":"Bastien","family":"Bissaro","sequence":"additional","affiliation":[{"name":"INRAE, Aix Marseille Univ, BBF, Biodiversite\u0301 et Biotechnologie Fongiques , ,","place":["Marseille, France, 13009"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,8,5]]},"reference":[{"key":"2026081808121634400_cit1","doi-asserted-by":"publisher","DOI":"10.1016\/j.biotechadv.2020.107634","article-title":"The Vast Repertoire of Carbohydrate Oxidases: An Overview","volume":"51","author":"Savino","year":"2021","journal-title":"Biotechnol. Adv."},{"issue":"D1","key":"2026081808121634400_cit2","doi-asserted-by":"publisher","first-page":"D571","DOI":"10.1093\/nar\/gkab1045","article-title":"The Carbohydrate-Active\nEnzyme Database: Functions\nand Literature","volume":"50","author":"Drula","year":"2022","journal-title":"Nucleic Acids Res."},{"issue":"1","key":"2026081808121634400_cit3","doi-asserted-by":"publisher","DOI":"10.1186\/1754-6834-6-41","article-title":"Expansion\nof the Enzymatic Repertoire of the CAZy Database to Integrate Auxiliary\nRedox Enzymes","volume":"6","author":"Levasseur","year":"2013","journal-title":"Biotechnol. Biofuels"},{"issue":"1","key":"2026081808121634400_cit4","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1016\/0167-4838(91)90439-7","article-title":"Purification\nand Characterization of a Novel Glucooligosaccharide Oxidase from Acremonium strictum T1","volume":"1118","author":"Lin","year":"1991","journal-title":"Biochim.\nBiophys. Acta, Protein Struct. Mol. Enzymol."},{"issue":"25","key":"2026081808121634400_cit5","doi-asserted-by":"publisher","first-page":"4905","DOI":"10.1016\/j.febslet.2007.09.019","article-title":"Changing\nthe Substrate Specificity\nof a Chitooligosaccharide Oxidase from Fusarium graminearum by Model-Inspired Site-Directed Mutagenesis","volume":"581","author":"Heuts","year":"2007","journal-title":"FEBS Lett."},{"issue":"45","key":"2026081808121634400_cit6","doi-asserted-by":"publisher","first-page":"23709","DOI":"10.1074\/jbc.M116.741173","article-title":"Discovery of a Xylooligosaccharide\nOxidase from Myceliophthora thermophila C1","volume":"291","author":"Ferrari","year":"2016","journal-title":"J. Biol. Chem."},{"issue":"1","key":"2026081808121634400_cit7","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-025-58668-8","article-title":"Enzymatic Oxidation of Galacturonides\nfrom Pectin Breakdown Contributes to Stealth Infection by Oomycota\nPhytopathogens","volume":"16","author":"Turella","year":"2025","journal-title":"Nat. Commun."},{"issue":"1","key":"2026081808121634400_cit8","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-22372-0","article-title":"Discovery of Fungal Oligosaccharide-Oxidising Flavo-Enzymes\nwith Previously Unknown Substrates, Redox-Activity Profiles and Interplay\nwith LPMOs","volume":"12","author":"Haddad Momeni","year":"2021","journal-title":"Nat. Commun."},{"issue":"1","key":"2026081808121634400_cit9","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-025-64189-1","article-title":"Oomycetes Manipulate\nPlant Innate Immunity through Galacturonide Oxidases","volume":"16","author":"Welsh","year":"2025","journal-title":"Nat. Commun."},{"key":"2026081808121634400_cit10","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1016\/j.carres.2017.05.010","article-title":"Fungal Secretomics\nto Probe the Biological\nFunctions of Lytic Polysaccharide Monooxygenases","volume":"448","author":"Berrin","year":"2017","journal-title":"Carbohydr. Res."},{"issue":"46","key":"2026081808121634400_cit11","doi-asserted-by":"publisher","first-page":"38831","DOI":"10.1074\/jbc.M506078200","article-title":"Crystal Structure\nof Glucooligosaccharide\nOxidase from Acremonium Strictum: A Novel Flavinylation of 6-S-Cysteinyl,\n8\u03b1-N1-Histidyl FAD","volume":"280","author":"Huang","year":"2005","journal-title":"J. Biol. Chem."},{"issue":"1","key":"2026081808121634400_cit12","doi-asserted-by":"publisher","DOI":"10.1186\/1754-6834-6-148","article-title":"Xylo- and Cello-Oligosaccharide Oxidation\nby Gluco-Oligosaccharide Oxidase from Sarocladium strictum and Variants with Reduced Substrate Inhibition","volume":"6","author":"Vuong","year":"2013","journal-title":"Biotechnol. Biofuels"},{"issue":"7115","key":"2026081808121634400_cit13","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1038\/nature05248","article-title":"Insights from the Genome of the Biotrophic Fungal Plant\nPathogen Ustilago maydis","volume":"444","author":"Ka\u0308mper","year":"2006","journal-title":"Nature"},{"issue":"6598","key":"2026081808121634400_cit14","doi-asserted-by":"publisher","first-page":"1187","DOI":"10.1126\/science.abo2401","article-title":"Organic Acids\nand Glucose Prime Late-Stage\nFungal Biotrophy in Maize","volume":"376","author":"Kretschmer","year":"2022","journal-title":"Science"},{"issue":"6","key":"2026081808121634400_cit15","doi-asserted-by":"publisher","first-page":"639","DOI":"10.1007\/s00438-004-1085-6","article-title":"A H2O2-Producing Glyoxal Oxidase Is Required for Filamentous\nGrowth and Pathogenicity in Ustilago maydis","volume":"272","author":"Leuthner","year":"2005","journal-title":"Mol. Genet. Genomics"},{"issue":"23","key":"2026081808121634400_cit16","doi-asserted-by":"publisher","DOI":"10.1101\/2022.09.16.508353","article-title":"The Maize\nPathogen Ustilago maydis Secretes Glycoside\nHydrolases and\nCarbohydrate Oxidases Directed towards Components of the Fungal Cell\nWall","volume":"88","author":"Reyre","year":"2022","journal-title":"Appl. Environ. Microbiol."},{"key":"2026081808121634400_cit17","doi-asserted-by":"publisher","DOI":"10.1128\/aem.00573-23","article-title":"The Ustilago maydis AA10 LPMO Is Active on Fungal Cell\nWall Chitin","volume":"89","author":"Yao","year":"2023","journal-title":"Appl. Environ. Microbiol."},{"issue":"2","key":"2026081808121634400_cit18","doi-asserted-by":"publisher","DOI":"10.1007\/s10529-026-03721-9","article-title":"Oligosaccharide\nOxidase for the Enzymatic Synthesis of Glucosaminic Acids","volume":"48","author":"Raji","year":"2026","journal-title":"Biotechnol. Lett."},{"issue":"13","key":"2026081808121634400_cit19","doi-asserted-by":"publisher","first-page":"1658","DOI":"10.1093\/bioinformatics\/btl158","article-title":"Cd-Hit: A Fast Program\nfor Clustering and Comparing\nLarge Sets of Protein or Nucleotide Sequences","volume":"22","author":"Li","year":"2006","journal-title":"Bioinformatics"},{"issue":"W1","key":"2026081808121634400_cit20","doi-asserted-by":"publisher","first-page":"W521","DOI":"10.1093\/nar\/gkae241","article-title":"The EMBL-EBI Job Dispatcher\nSequence Analysis Tools Framework in 2024","volume":"52","author":"Madeira","year":"2024","journal-title":"Nucleic\nAcids Res."},{"issue":"W1","key":"2026081808121634400_cit21","doi-asserted-by":"publisher","first-page":"W232","DOI":"10.1093\/nar\/gkw256","article-title":"W-IQ-TREE: A Fast\nOnline Phylogenetic Tool for Maximum Likelihood Analysis","volume":"44","author":"Trifinopoulos","year":"2016","journal-title":"Nucleic Acids Res."},{"issue":"W1","key":"2026081808121634400_cit22","doi-asserted-by":"publisher","first-page":"W78","DOI":"10.1093\/nar\/gkae268","article-title":"Interactive Tree of\nLife (ITOL) v6: Recent Updates to the Phylogenetic\nTree Display and Annotation Tool","volume":"52","author":"Letunic","year":"2024","journal-title":"Nucleic Acids\nRes."},{"key":"2026081808121634400_cit23","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2015.01002","article-title":"Recombinant Protein Production Facility for Fungal\nBiomass-Degrading Enzymes Using the Yeast Pichia pastoris","volume":"6","author":"Haon","year":"2015","journal-title":"Front. Microbiol."},{"issue":"10","key":"2026081808121634400_cit24","doi-asserted-by":"publisher","first-page":"863","DOI":"10.1021\/cbe.4c00125","article-title":"Design of\nPlastic Binding Lytic Polysaccharide\nMonooxygenases via Modular Engineering","volume":"1","author":"Munzone","year":"2024","journal-title":"Chem\nBio Eng."},{"issue":"14","key":"2026081808121634400_cit25","doi-asserted-by":"publisher","first-page":"2059","DOI":"10.1002\/rcm.5060","article-title":"Performance Evaluation\non a Wide Set of Matrix-Assisted Laser Desorption Ionization Matrices\nfor the Detection of Oligosaccharides in a High-Throughput Mass Spectrometric\nScreening of Carbohydrate Depolymerizing Enzymes","volume":"25","author":"Ropartz","year":"2011","journal-title":"Rapid Commun. Mass Spectrom."},{"issue":"6","key":"2026081808121634400_cit26","doi-asserted-by":"publisher","first-page":"1022","DOI":"10.1107\/S0021889897006766","article-title":"MOLREP: An\nAutomated Program for Molecular Replacement","volume":"30","author":"Vagin","year":"1997","journal-title":"J. Appl. Crystallogr."},{"issue":"5","key":"2026081808121634400_cit27","doi-asserted-by":"publisher","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The\nCCP4 Suite: Programs for Protein Crystallography","volume":"50","author":"Collaborative Computational Project, Number 4.","year":"1994","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"key":"2026081808121634400_cit28","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview\nof the CCP4 Suite and Current Developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"key":"2026081808121634400_cit29","doi-asserted-by":"publisher","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement\nof Macromolecular Structures\nby the Maximum-Likelihood Method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr.,\nSect. D: Biol. Crystallogr."},{"issue":"12\nI","key":"2026081808121634400_cit30","doi-asserted-by":"publisher","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: Model-Building Tools for Molecular\nGraphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr., Sect. D: Biol.\nCrystallogr."},{"issue":"4","key":"2026081808121634400_cit31","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and\nDevelopment\nof Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"issue":"2","key":"2026081808121634400_cit32","doi-asserted-by":"publisher","first-page":"892","DOI":"10.1021\/acs.jctc.5b00834","article-title":"Vina-Carb:\nImproving Glycosidic Angles during Carbohydrate Docking","volume":"12","author":"Nivedha","year":"2016","journal-title":"J. Chem. Theory Comput."},{"issue":"8","key":"2026081808121634400_cit33","doi-asserted-by":"publisher","first-page":"1529","DOI":"10.1016\/j.bpj.2017.03.011","article-title":"NMRbox: A Resource\nfor Biomolecular NMR Computation","volume":"112","author":"Maciejewski","year":"2017","journal-title":"Biophys. J."},{"issue":"2","key":"2026081808121634400_cit34","doi-asserted-by":"publisher","first-page":"300","DOI":"10.1105\/tpc.17.00764","article-title":"The Biotrophic\nDevelopment of Ustilago maydis Studied\nby RNA-Seq Analysis","volume":"30","author":"Lanver","year":"2018","journal-title":"Plant Cell"},{"issue":"1","key":"2026081808121634400_cit35","doi-asserted-by":"publisher","DOI":"10.1186\/1471-2164-13-57","article-title":"Post-Genomic Analyses\nof Fungal Lignocellulosic\nBiomass Degradation Reveal the Unexpected Potential of the Plant Pathogen Ustilago maydis","volume":"13","author":"Couturier","year":"2012","journal-title":"BMC Genomics"},{"key":"2026081808121634400_cit36","doi-asserted-by":"crossref","unstructured":"Gupta, R.; Brunak, S. In  Prediction of Glycosylation\nacross the Human Proteome and the Correlation to Protein Function, Pac. Symp. Biocomput., 2002; pp 310\u2013322.","DOI":"10.1142\/9789812799623_0029"},{"issue":"10","key":"2026081808121634400_cit37","doi-asserted-by":"publisher","first-page":"1478","DOI":"10.1038\/emboj.2013.79","article-title":"Precision Mapping of the Human O-GalNAc Glycoproteome\nthrough SimpleCell Technology","volume":"32","author":"Steentoft","year":"2013","journal-title":"EMBO J."},{"issue":"2","key":"2026081808121634400_cit38","doi-asserted-by":"publisher","DOI":"10.1128\/mBio.03419-20","article-title":"Chitosan and Chitin Deacetylase Activity Are Necessary\nfor Development and Virulence of Ustilago maydis","volume":"12","author":"Rizzi","year":"2021","journal-title":"mBio"},{"issue":"3","key":"2026081808121634400_cit39","doi-asserted-by":"publisher","first-page":"658","DOI":"10.1021\/ja01318a036","article-title":"The Determination of\nEnzyme Dissociation Constants","volume":"56","author":"Lineweaver","year":"1934","journal-title":"J. Am. Chem.\nSoc."},{"issue":"6001","key":"2026081808121634400_cit40","doi-asserted-by":"publisher","first-page":"219","DOI":"10.1126\/science.1192231","article-title":"An Oxidative Enzyme Boosting the\nEnzymatic Conversion of Recalcitrant Polysaccharides","volume":"330","author":"Vaaje-Kolstad","year":"2010","journal-title":"Science"},{"key":"2026081808121634400_cit41","doi-asserted-by":"publisher","first-page":"292","DOI":"10.1016\/j.abb.2008.01.027","article-title":"The\nGrowing VAO Flavoprotein Family","volume":"474","author":"Leferink","year":"2008","journal-title":"Arch. Biochem.\nBiophys."},{"issue":"3","key":"2026081808121634400_cit42","doi-asserted-by":"publisher","first-page":"126","DOI":"10.1016\/S0968-0004(99)01533-9","article-title":"Flavoenzymes: Diverse Catalysts with Recurrent Features","volume":"25","author":"Fraaije","year":"2000","journal-title":"Trends Biochem. Sci."},{"key":"2026081808121634400_cit43","doi-asserted-by":"publisher","first-page":"1742","DOI":"10.1021\/acs.chemrev.7b00650","article-title":"Same Substrate, Many\nReactions: Oxygen Activation in\nFlavoenzymes","volume":"118","author":"Romero","year":"2018","journal-title":"Chem. Rev."},{"issue":"16","key":"2026081808121634400_cit44","doi-asserted-by":"publisher","first-page":"3060","DOI":"10.1111\/febs.13212","article-title":"Rationally\nEngineered Flavin-Dependent Oxidase Reveals Steric Control of Dioxygen\nReduction","volume":"282","author":"Zafred","year":"2015","journal-title":"FEBS J."},{"issue":"2","key":"2026081808121634400_cit45","doi-asserted-by":"publisher","first-page":"1046","DOI":"10.1021\/acscatal.4c05944","article-title":"Dehydrogenase versus\nOxidase Function: The Interplay\nbetween Substrate Binding and Flavin Microenvironment","volume":"15","author":"Guerriere","year":"2025","journal-title":"ACS Catal."},{"key":"2026081808121634400_cit46","doi-asserted-by":"publisher","first-page":"88","DOI":"10.1016\/j.abb.2017.06.023","article-title":"The Family\nof Berberine Bridge Enzyme-like\nEnzymes: A Treasure-Trove of Oxidative Reactions","volume":"632","author":"Daniel","year":"2017","journal-title":"Arch. Biochem. Biophys."},{"issue":"1","key":"2026081808121634400_cit47","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1042\/bj20031813","article-title":"Catalytic\nReaction of Cytokinin Dehydrogenase: Preference for Quinones as Electron\nAcceptors","volume":"380","author":"Fre\u0301bortova\u0301","year":"2004","journal-title":"Biochem. 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