{"title":"甲酸脱氢酶的一些性质。","authors":"T Höpner, A Trautwein","doi":"10.1515/znb-1972-0923","DOIUrl":null,"url":null,"abstract":"The enzyme was anaerobically isolated and was characterized as a flavoprotein containing at least 1 FMN, 5-8 Fe and 7-8 moles labile sulfide per mole (M. W. appr. 300.000). It catalyzes the oxidation of formate by NAD, O2 (forming H2O2) and dyes and the oxidation of NADH by O2 (forming Η2Ο2) and dyes. It is irreversibly inhibited by formate.","PeriodicalId":78857,"journal":{"name":"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie","volume":"27 9","pages":"1075-6"},"PeriodicalIF":0.0000,"publicationDate":"1972-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1972-0923","citationCount":"13","resultStr":"{\"title\":\"Some properties of formate dehydrogenase.\",\"authors\":\"T Höpner, A Trautwein\",\"doi\":\"10.1515/znb-1972-0923\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The enzyme was anaerobically isolated and was characterized as a flavoprotein containing at least 1 FMN, 5-8 Fe and 7-8 moles labile sulfide per mole (M. W. appr. 300.000). It catalyzes the oxidation of formate by NAD, O2 (forming H2O2) and dyes and the oxidation of NADH by O2 (forming Η2Ο2) and dyes. It is irreversibly inhibited by formate.\",\"PeriodicalId\":78857,\"journal\":{\"name\":\"Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie\",\"volume\":\"27 9\",\"pages\":\"1075-6\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1972-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1515/znb-1972-0923\",\"citationCount\":\"13\",\"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-1972-0923\",\"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-1972-0923","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The enzyme was anaerobically isolated and was characterized as a flavoprotein containing at least 1 FMN, 5-8 Fe and 7-8 moles labile sulfide per mole (M. W. appr. 300.000). It catalyzes the oxidation of formate by NAD, O2 (forming H2O2) and dyes and the oxidation of NADH by O2 (forming Η2Ο2) and dyes. It is irreversibly inhibited by formate.
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