{"title":"pH为7时酶催化反应表观平衡常数的计算","authors":"Robert A. Alberty","doi":"10.1016/S0307-4412(99)00064-3","DOIUrl":null,"url":null,"abstract":"<div><p>Apparent equilibrium constants <em>K</em>′ of biochemical reactions at pH 7 and standard apparent reduction potentials of half reactions at pH 7 can be calculated using a table of standard transformed Gibbs energies of formation Δ<sub>f</sub><em>G</em>′<sup>0</sup> at pH 7. A table is provided for 136 reactants at 25°C, pH 7, and ionic strengths of 0, 0.10, and 0.25 M. Examples are given to illustrate the use of the table.</p></div>","PeriodicalId":80258,"journal":{"name":"Biochemical education","volume":"28 1","pages":"Pages 12-17"},"PeriodicalIF":0.0000,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0307-4412(99)00064-3","citationCount":"0","resultStr":"{\"title\":\"Calculating apparent equilibrium constants of enzyme-catalyzed reactions at pH 7\",\"authors\":\"Robert A. Alberty\",\"doi\":\"10.1016/S0307-4412(99)00064-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Apparent equilibrium constants <em>K</em>′ of biochemical reactions at pH 7 and standard apparent reduction potentials of half reactions at pH 7 can be calculated using a table of standard transformed Gibbs energies of formation Δ<sub>f</sub><em>G</em>′<sup>0</sup> at pH 7. A table is provided for 136 reactants at 25°C, pH 7, and ionic strengths of 0, 0.10, and 0.25 M. Examples are given to illustrate the use of the table.</p></div>\",\"PeriodicalId\":80258,\"journal\":{\"name\":\"Biochemical education\",\"volume\":\"28 1\",\"pages\":\"Pages 12-17\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2000-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0307-4412(99)00064-3\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemical education\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0307441299000643\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemical education","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0307441299000643","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Calculating apparent equilibrium constants of enzyme-catalyzed reactions at pH 7
Apparent equilibrium constants K′ of biochemical reactions at pH 7 and standard apparent reduction potentials of half reactions at pH 7 can be calculated using a table of standard transformed Gibbs energies of formation ΔfG′0 at pH 7. A table is provided for 136 reactants at 25°C, pH 7, and ionic strengths of 0, 0.10, and 0.25 M. Examples are given to illustrate the use of the table.
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