{"title":"硫酸腺苷酸还原酶对硫酸盐还原菌脱硫弧菌的作用机理研究。","authors":"H D Peck, R Bramlett, D V Der Vartanian","doi":"10.1515/znb-1972-0928","DOIUrl":null,"url":null,"abstract":"The roles of enzyme-bound FAD and non-heme iron in the mechanism of adenylyl sulfate reductase have been investigated by inhibitor studies, stopped-flow techniques and EPR spectroscopy. The results indicate that the non-heme iron found in the purified reductase is catalytically active and that the turnover number of the enzyme-bound FAD is identical with the maximum turnover number for the enzyme.","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 9","pages":"1084-6"},"PeriodicalIF":0.0000,"publicationDate":"1972-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-0928","citationCount":"4","resultStr":"{\"title\":\"On the mechanism of adenylyl sulfate reductase for the sulfate-reducing bacterium, Desulfovibrio vulgaris.\",\"authors\":\"H D Peck, R Bramlett, D V Der Vartanian\",\"doi\":\"10.1515/znb-1972-0928\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The roles of enzyme-bound FAD and non-heme iron in the mechanism of adenylyl sulfate reductase have been investigated by inhibitor studies, stopped-flow techniques and EPR spectroscopy. The results indicate that the non-heme iron found in the purified reductase is catalytically active and that the turnover number of the enzyme-bound FAD is identical with the maximum turnover number for the enzyme.\",\"PeriodicalId\":78857,\"journal\":{\"name\":\"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie\",\"volume\":\"27 9\",\"pages\":\"1084-6\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1972-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1515/znb-1972-0928\",\"citationCount\":\"4\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1515/znb-1972-0928\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1515/znb-1972-0928","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
On the mechanism of adenylyl sulfate reductase for the sulfate-reducing bacterium, Desulfovibrio vulgaris.
The roles of enzyme-bound FAD and non-heme iron in the mechanism of adenylyl sulfate reductase have been investigated by inhibitor studies, stopped-flow techniques and EPR spectroscopy. The results indicate that the non-heme iron found in the purified reductase is catalytically active and that the turnover number of the enzyme-bound FAD is identical with the maximum turnover number for the enzyme.
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