{"title":"亚砷酸盐与鸡肝黄嘌呤脱氢酶钼中心的相互作用","authors":"Jean L. Johnson, K.V. Rajagopalan","doi":"10.1016/S0006-3061(00)80278-1","DOIUrl":null,"url":null,"abstract":"<div><p>Inactivation of chicken liver xanthine dehydrogenase by arsenite is reflected in the molybdenum electron paramagnetic resonance signal at <em>g</em> = 1.97. The arsenite spectrum shows additional splittings and considerable broadening yet remains comparable to the native in total intensity. Further subtle alterations of the molybdenum signal of arsenite-treated enzyme are seen in the presence of purine-type substrates or inhibitors.</p></div>","PeriodicalId":9177,"journal":{"name":"Bioinorganic chemistry","volume":"8 5","pages":"Pages 439-444"},"PeriodicalIF":0.0000,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0006-3061(00)80278-1","citationCount":"13","resultStr":"{\"title\":\"The Interaction of Arsenite with the Molybdenum Center of Chicken Liver Xanthine Dehydrogenase\",\"authors\":\"Jean L. Johnson, K.V. Rajagopalan\",\"doi\":\"10.1016/S0006-3061(00)80278-1\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Inactivation of chicken liver xanthine dehydrogenase by arsenite is reflected in the molybdenum electron paramagnetic resonance signal at <em>g</em> = 1.97. The arsenite spectrum shows additional splittings and considerable broadening yet remains comparable to the native in total intensity. Further subtle alterations of the molybdenum signal of arsenite-treated enzyme are seen in the presence of purine-type substrates or inhibitors.</p></div>\",\"PeriodicalId\":9177,\"journal\":{\"name\":\"Bioinorganic chemistry\",\"volume\":\"8 5\",\"pages\":\"Pages 439-444\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1978-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0006-3061(00)80278-1\",\"citationCount\":\"13\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bioinorganic chemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0006306100802781\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioinorganic chemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0006306100802781","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The Interaction of Arsenite with the Molybdenum Center of Chicken Liver Xanthine Dehydrogenase
Inactivation of chicken liver xanthine dehydrogenase by arsenite is reflected in the molybdenum electron paramagnetic resonance signal at g = 1.97. The arsenite spectrum shows additional splittings and considerable broadening yet remains comparable to the native in total intensity. Further subtle alterations of the molybdenum signal of arsenite-treated enzyme are seen in the presence of purine-type substrates or inhibitors.
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