{"title":"用SVD分析模拟和真实数据,重新检验o2与完全还原的细胞色素aa3的结合。","authors":"R W Hendler, R I Shrager","doi":"10.1002/iub.7510450521","DOIUrl":null,"url":null,"abstract":"<p><p>Using new time-resolved multichannel experimental and simulated data, analyzed by SVD, it is concluded that the second order binding rate constant for O2-binding to fully reduced mammalian cytochrome aa3 is approximately five times higher than the currently accepted value of approximately 1.5 x 10(8) M-1 s-1.</p>","PeriodicalId":8770,"journal":{"name":"Biochemistry and molecular biology international","volume":"45 5","pages":"1031-45"},"PeriodicalIF":0.0000,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/iub.7510450521","citationCount":"2","resultStr":"{\"title\":\"O2-binding to fully reduced cytochrome aa3 reexamined using SVD analysis of simulated and real data.\",\"authors\":\"R W Hendler, R I Shrager\",\"doi\":\"10.1002/iub.7510450521\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Using new time-resolved multichannel experimental and simulated data, analyzed by SVD, it is concluded that the second order binding rate constant for O2-binding to fully reduced mammalian cytochrome aa3 is approximately five times higher than the currently accepted value of approximately 1.5 x 10(8) M-1 s-1.</p>\",\"PeriodicalId\":8770,\"journal\":{\"name\":\"Biochemistry and molecular biology international\",\"volume\":\"45 5\",\"pages\":\"1031-45\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1002/iub.7510450521\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemistry and molecular biology international\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1002/iub.7510450521\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemistry and molecular biology international","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1002/iub.7510450521","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 2
摘要
利用新的时间分辨多通道实验和模拟数据,通过SVD分析,得出o2与完全还原的哺乳动物细胞色素aa3结合的二级结合速率常数比目前公认的约1.5 x 10(8) M-1 s-1高约5倍。
O2-binding to fully reduced cytochrome aa3 reexamined using SVD analysis of simulated and real data.
Using new time-resolved multichannel experimental and simulated data, analyzed by SVD, it is concluded that the second order binding rate constant for O2-binding to fully reduced mammalian cytochrome aa3 is approximately five times higher than the currently accepted value of approximately 1.5 x 10(8) M-1 s-1.