{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,27]],"date-time":"2026-02-27T02:45:18Z","timestamp":1772160318350,"version":"3.50.1"},"reference-count":35,"publisher":"Wiley","issue":"21","license":[{"start":{"date-parts":[[2023,8,11]],"date-time":"2023-08-11T00:00:00Z","timestamp":1691712000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100012914","name":"Vidyasirimedhi Institute of Science and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012914","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2023,11]]},"abstract":"<jats:p>\n                    The dimethyl sulfone monooxygenase system is a two\u2010component flavoprotein, catalyzing the monooxygenation of dimethyl sulfone (DMSO\n                    <jats:sub>2<\/jats:sub>\n                    ) by oxidative cleavage producing methanesulfinate and formaldehyde. The reductase component (DMSR) is a flavoprotein with FMN as a cofactor, catalyzing flavin reduction using NADH. The monooxygenase (DMSMO) uses reduced flavin from the reductase and oxygen for substrate monooxygenation. DMSMO can bind to FMN and FMNH\n                    <jats:sup>\u2212<\/jats:sup>\n                    with a\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>d<\/jats:sub>\n                    of 17.4\u2009\u00b1\u20090.9\u2009\u03bc\n                    <jats:sc>m<\/jats:sc>\n                    and 4.08\u2009\u00b1\u20090.8\u2009\u03bc\n                    <jats:sc>m<\/jats:sc>\n                    , respectively. The binding of FMN to DMSMO is required prior to binding DMSO\n                    <jats:sub>2<\/jats:sub>\n                    . This also applies to the fast binding of reduced FMN to DMSMO followed by DMSO\n                    <jats:sub>2<\/jats:sub>\n                    . Substituting reduced DMSR with FMNH\n                    <jats:sup>\u2212<\/jats:sup>\n                    demonstrated the same oxidation kinetics, indicating that FMNH\n                    <jats:sup>\u2212<\/jats:sup>\n                    from DMSR was transferred to DMSMO. The oxidation of FMNH\n                    <jats:sup>\u2212<\/jats:sup>\n                    :DMSMO, with and without DMSO\n                    <jats:sub>2<\/jats:sub>\n                    did not generate any flavin adducts for monooxygenation. Therefore, H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    is likely to be the reactive agent to attack the substrate. The H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    assay results demonstrated production of H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    from the oxidation of FMNH\n                    <jats:sup>\u2212<\/jats:sup>\n                    :DMSMO, whereas H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    was not detected in the presence of DMSO\n                    <jats:sub>2<\/jats:sub>\n                    , confirming H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    utilization. The rate constant for methanesulfinate formation determined from rapid quenched flow and the rate constant for flavin oxidation were similar, indicating that H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    rapidly reacts with DMSO\n                    <jats:sub>2<\/jats:sub>\n                    , with flavin oxidation as the rate\u2010limiting step. This is the first report of the kinetic mechanisms of both components using rapid kinetics and of a method for methanesulfinate detection using LC\u2013MS.\n                  <\/jats:p>","DOI":"10.1111\/febs.16916","type":"journal-article","created":{"date-parts":[[2023,7,31]],"date-time":"2023-07-31T06:59:00Z","timestamp":1690786740000},"page":"5171-5195","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Reaction mechanism and kinetics of the two\u2010component flavoprotein dimethyl sulfone monooxygenase system: Using hydrogen peroxide for monooxygenation and substrate cleavage"],"prefix":"10.1111","volume":"290","author":[{"ORCID":"https:\/\/orcid.org\/0009-0001-8756-580X","authenticated-orcid":false,"given":"Montisa","family":"Mangkalee","sequence":"first","affiliation":[{"name":"Department of Chemistry, Faculty of Science Chulalongkorn University  Bangkok Thailand"},{"name":"Research Unit in Integrative 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