{"corpus_id":20316719,"paper_sha":"3289eaee88d3944c69a176ca6901ccadbae56be1","doi":"10.1016/s0021-9258(19)42510-6","arxiv_id":null,"pmid":4369125,"pmcid":null,"mag_id":1598187616,"dblp_id":null,"acl_id":null,"title":"Reduced nicotinamide adenine dinucleotide cytochrome o reductase associated with cytochrome o purified from Vitreoscilla. Evidence for an intermediate oxygenated form of cytochrome o.","year":1974,"publication_date":"1974-07-10","venue":"Journal of Biological Chemistry","journal":{"name":"The Journal of biological chemistry","pages":"\n          4257-60\n        ","volume":"249 13"},"journal_issn":null,"journal_title":null,"publication_types":["JournalArticle"],"pubmed_pub_types":["Journal Article"],"s2_fields_of_study":["Biology","Medicine","Chemistry"],"reference_count":0,"citation_count":65,"influential_citation_count":1,"is_open_access":false,"arxiv_categories":null,"arxiv_license":null,"arxiv_journal_ref":null,"mesh_headings":[{"d":"Bacteria","mj":false,"qs":[{"q":"enzymology","mj":true,"ui":"Q000201"}],"ui":"D001419"},{"d":"Carbon Monoxide","mj":false,"ui":"D002248"},{"d":"Chemical Precipitation","mj":false,"ui":"D011232"},{"d":"Chromatography, DEAE-Cellulose","mj":false,"ui":"D002848"},{"d":"Chromatography, Gel","mj":false,"ui":"D002850"},{"d":"Cytochrome Reductases","mj":false,"qs":[{"q":"analysis","mj":true,"ui":"Q000032"}],"ui":"D003579"},{"d":"Cytochromes","mj":false,"qs":[{"q":"isolation & purification","mj":true,"ui":"Q000302"}],"ui":"D003580"},{"d":"Molecular Conformation","mj":false,"ui":"D008968"},{"d":"NAD","mj":false,"ui":"D009243"},{"d":"Oxidation-Reduction","mj":false,"ui":"D010084"},{"d":"Oxygen","mj":true,"ui":"D010100"},{"d":"Spectrophotometry","mj":false,"ui":"D013053"},{"d":"Sulfites","mj":false,"ui":"D013447"}],"chemicals":[{"n":"Cytochromes","ui":"D003580","reg":"0"},{"n":"Sulfites","ui":"D013447","reg":"0"},{"n":"NAD","ui":"D009243","reg":"0U46U6E8UK"},{"n":"Carbon Monoxide","ui":"D002248","reg":"7U1EE4V452"},{"n":"Cytochrome Reductases","ui":"D003579","reg":"EC 1.6.2.-"},{"n":"Oxygen","ui":"D010100","reg":"S88TT14065"}],"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":"Abstract Cytochrome o, purified from Vitreoscilla sp., Murray strain 389, has a carbon monoxide difference spectrum with absorption maxima at 569, 535, and 419 nm. This spectrum resembles closely the carbon monoxide difference spectrum of whole cell suspensions of Vitreoscilla. The reduction of cytochrome o by NADH is catalyzed by a component(s) present in purified preparations of the cytochrome, and this NADH-cytochrome o reductase activity could be assayed in these preparations aerobically by following the absorbancy increase at 420 nm on the addition of NADH. Aerobic difference spectra of cytochrome o solutions, (NADH) minus (untreated), have absorption maxima at 577, 544, and 420 nm, and this spectrum is believed to represent the formation of an \"oxygenated\" form of reduced cytochrome o. Difference spectra of cytochrome o, that has been chemically reduced by excess sodium dithionite, have absorption maxima at 560 and 435 nm, which presumably are the absorption maxima characteristic of the reduced, but not oxygenated, form of cytochrome o. Chromatography of cytochrome o on Sephadex G-100 and DEAE-cellulose resulted in purification of cytochrome o and NADH-cytochrome o reductase, but separation of the reductase activity from the cytochrome was not achieved. Reductase activity with cytochrome o as acceptor was separated chromatographically from reductase activity with 2,6-dichlorophenolindophenol as acceptor. Oxygen uptake of purified fractions on the addition of NADH was associated primarily with NADH-cytochrome o reductase activity.","claims":[{"public_id":"cl_8aa1ac11abe557f5259b2d5db21888da","status":"active","text":"Aerobic difference spectra after NADH addition show maxima at 577, 544, and 420 nm and are interpreted as evidence for an intermediate oxygenated form of reduced cytochrome o.","confidence":0.95,"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_8aa1ac11abe557f5259b2d5db21888da"},{"public_id":"cl_182129e48f9958fd7cbf46924b0c203d","status":"active","text":"Chemical reduction with excess sodium dithionite yields a cytochrome o spectrum with maxima at 560 and 435 nm, consistent with a reduced but non-oxygenated form.","confidence":0.93,"contributors":[{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous 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420 nm after NADH addition.","confidence":0.96,"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_2ca19f01ff768901da8d50d8e7910f86"},{"public_id":"cl_9ac787c1b6334b822d25a97ed9f24981","status":"active","text":"Purified cytochrome o from Vitreoscilla sp. shows a carbon monoxide difference spectrum with absorption maxima at 569, 535, and 419 nm, closely matching the spectrum of whole-cell suspensions.","confidence":0.97,"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_9ac787c1b6334b822d25a97ed9f24981"}],"concepts":[{"public_id":"co_0029e420b924ba247d3c45f00807465f","status":"active","name":"aerobic difference spectra","description":"Difference spectra recorded under aerobic conditions before and after 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