{"corpus_id":18159473,"paper_sha":"9923be5815abbd5c43911a57dbe53a8d2a1c64a7","doi":"10.1126/SCIENCE.282.5395.1877","arxiv_id":null,"pmid":9836635,"pmcid":null,"mag_id":2142337964,"dblp_id":null,"acl_id":null,"title":"Single-molecule enzymatic dynamics.","year":1998,"publication_date":"1998-12-04","venue":"Science","journal":{"name":"Science","pages":"\n          1877-82\n        ","volume":"282 5395"},"journal_issn":null,"journal_title":null,"publication_types":["JournalArticle"],"pubmed_pub_types":["Journal Article","Research Support, Non-U.S. Gov't","Research Support, U.S. Gov't, Non-P.H.S."],"s2_fields_of_study":["Biology","Medicine","Chemistry"],"reference_count":53,"citation_count":1298,"influential_citation_count":25,"is_open_access":false,"arxiv_categories":null,"arxiv_license":null,"arxiv_journal_ref":null,"mesh_headings":[{"d":"Binding Sites","mj":false,"ui":"D001665"},{"d":"Brevibacterium","mj":false,"qs":[{"q":"enzymology","mj":false,"ui":"Q000201"}],"ui":"D001951"},{"d":"Cholesterol","mj":false,"qs":[{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D002784"},{"d":"Cholesterol Oxidase","mj":false,"qs":[{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D002789"},{"d":"Flavin-Adenine Dinucleotide","mj":false,"qs":[{"q":"metabolism","mj":true,"ui":"Q000378"}],"ui":"D005182"},{"d":"Kinetics","mj":false,"ui":"D007700"},{"d":"Microscopy, Fluorescence","mj":false,"ui":"D008856"},{"d":"Oxidation-Reduction","mj":false,"ui":"D010084"},{"d":"Probability","mj":false,"ui":"D011336"},{"d":"Spectrometry, Fluorescence","mj":false,"ui":"D013050"},{"d":"Stochastic Processes","mj":false,"ui":"D013269"}],"chemicals":[{"n":"Flavin-Adenine Dinucleotide","ui":"D005182","reg":"146-14-5"},{"n":"Cholesterol","ui":"D002784","reg":"97C5T2UQ7J"},{"n":"Cholesterol Oxidase","ui":"D002789","reg":"EC 1.1.3.6"}],"comments_corrections":null,"source_flags":5,"s2_open_access_pdf_url":null,"s2_open_access_landing_url":null,"s2_open_access_license":null,"s2_open_access_status":null,"pmc_open_access_pdf_url":null,"pmc_open_access_landing_url":null,"pmc_open_access_license":null,"pmc_open_access_status":null,"unpaywall_open_access_pdf_url":null,"unpaywall_open_access_landing_url":null,"unpaywall_open_access_license":null,"unpaywall_open_access_status":null,"abstract":"Enzymatic turnovers of single cholesterol oxidase molecules were observed in real time by monitoring the emission from the enzyme's fluorescent active site, flavin adenine dinucleotide (FAD). Statistical analyses of single-molecule trajectories revealed a significant and slow fluctuation in the rate of cholesterol oxidation by FAD. The static disorder and dynamic disorder of reaction rates, which are essentially indistinguishable in ensemble-averaged experiments, were determined separately by the real-time single-molecule approach. A molecular memory phenomenon, in which an enzymatic turnover was not independent of its previous turnovers because of a slow fluctuation of protein conformation, was evidenced by spontaneous spectral fluctuation of FAD.","claims":[{"public_id":"cl_7a15f340b3404f21a00b7f76c3530748","status":"active","text":"A molecular memory phenomenon was evidenced, in which enzymatic turnover depended on previous turnovers because of a slow fluctuation of protein conformation.","confidence":0.94,"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["extraction"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"url":"https://sah.borca.ai/claims/cl_7a15f340b3404f21a00b7f76c3530748"},{"public_id":"cl_85eb76eef39db35ce474e0f24ce3341b","status":"active","text":"Single cholesterol oxidase turnovers were observed in real time by monitoring emission from the fluorescent active site flavin adenine 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