生物物理学. 评论“极端电场在酮固醇异构酶活性部位推动催化反应”。
BIOPHYSICS. Comment on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".
机构信息
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA.
Department of Chemistry and Biochemistry, California State University Long Beach, Long Beach, CA 90840, USA.
出版信息
Science. 2015 Aug 28;349(6251):936. doi: 10.1126/science.aab1584. Epub 2015 Aug 27.
Fried et al. (Reports, 19 December 2014, p. 1510) demonstrated a strong correlation between reaction rate and the carbonyl stretching frequency of a product analog bound to ketosteroid isomerase oxyanion hole mutants and concluded that the active-site electric field provides 70% of catalysis. Alternative comparisons suggest a smaller contribution, relative to the corresponding solution reaction, and highlight the importance of atomic-level descriptions.
弗里德等人（1914 年 12 月 19 日，第 1510 页报道）证明了反应速率与结合到酮甾体异构酶氧阴离子穴突变体的产物类似物的羰基伸缩频率之间存在很强的相关性，并得出结论，活性位点电场提供了 70%的催化作用。其他比较表明，与相应的溶液反应相比，电场的贡献相对较小，这凸显了原子水平描述的重要性。
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