{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tucci FJ"],"funding":["U.S. Department of Health &amp; Human Services | NIH | Office of Extramural Research, National Institutes of Health","NIEHS NIH HHS","NCI NIH HHS","NIGMS NIH HHS","U.S. Department of Health &amp; Human Services | National Institutes of Health","National Science Foundation"],"pagination":["1194-1204"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10766429"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["6(12)"],"pubmed_abstract":["Nature's primary methane-oxidizing enzyme, the membrane-bound particulate methane monooxygenase (pMMO), catalyzes the oxidation of methane to methanol. pMMO activity requires copper, and decades of structural and spectroscopic studies have sought to identify the active site among three candidates: the Cu<sub>B</sub>, Cu<sub>C</sub>, and Cu<sub>D</sub> sites. Challenges associated with the isolation of active pMMO have hindered progress toward locating its catalytic center. However, reconstituting pMMO into native lipid nanodiscs stabilizes its structure and recovers its activity. Here, these active samples were incubated with 2,2,2,-trifluoroethanol (TFE), a product analog that serves as a readily visualized active-site probe. Interactions of TFE with the Cu<sub>D</sub> site were observed "],"journal":["Nature catalysis"],"pubmed_title":["Product analog binding identifies the copper active site of particulate methane monooxygenase."],"pmcid":["PMC10766429"],"funding_grant_id":["T32 GM008382","F31 ES034283","MCB-1908587","F31ES034283","P30 CA060553","U24 GM129539","R35 GM118035","T32GM008382","T32 GM105538","R01 GM111097","R01GM111097","R35GM118035"],"pubmed_authors":["Tucci FJ","Hoffman BM","Rosenzweig AC","Jodts RJ"],"additional_accession":[]},"is_claimable":false,"name":"Product analog binding identifies the copper active site of particulate methane monooxygenase.","description":"Nature's primary methane-oxidizing enzyme, the membrane-bound particulate methane monooxygenase (pMMO), catalyzes the oxidation of methane to methanol. pMMO activity requires copper, and decades of structural and spectroscopic studies have sought to identify the active site among three candidates: the Cu<sub>B</sub>, Cu<sub>C</sub>, and Cu<sub>D</sub> sites. Challenges associated with the isolation of active pMMO have hindered progress toward locating its catalytic center. However, reconstituting pMMO into native lipid nanodiscs stabilizes its structure and recovers its activity. Here, these active samples were incubated with 2,2,2,-trifluoroethanol (TFE), a product analog that serves as a readily visualized active-site probe. Interactions of TFE with the Cu<sub>D</sub> site were observed ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Dec","modification":"2026-04-17T13:20:01.431Z","creation":"2025-04-06T15:08:31.149Z"},"accession":"S-EPMC10766429","cross_references":{"pubmed":["38187819"],"doi":["10.1038/s41929-023-01051-x"]}}