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BIOPHYSICS. Comment on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".生物物理学。对“极端电场助力酮甾类异构酶活性位点的催化作用”的评论。
Science. 2015 Aug 28;349(6251):936. doi: 10.1126/science.aab0095. Epub 2015 Aug 27.
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BIOPHYSICS. Comment on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".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”。
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Extreme electric fields power catalysis in the active site of ketosteroid isomerase.极强电场助力酮甾体异构酶活性位点的催化作用。
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BIOPHYSICS. Response to Comments on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".生物物理学。对《极端电场助力酮甾类异构酶活性位点催化作用》评论的回应
Science. 2015 Aug 28;349(6251):936. doi: 10.1126/science.aab1627. Epub 2015 Aug 27.

本文引用的文献

1
Extreme electric fields power catalysis in the active site of ketosteroid isomerase.极强电场助力酮甾体异构酶活性位点的催化作用。
Science. 2014 Dec 19;346(6216):1510-4. doi: 10.1126/science.1259802.
2
Ground state destabilization from a positioned general base in the ketosteroid isomerase active site.定位在酮甾体异构酶活性部位的通用碱基使基态失稳。
Biochemistry. 2013 Feb 12;52(6):1074-81. doi: 10.1021/bi301348x. Epub 2013 Jan 30.
3
Dissecting the paradoxical effects of hydrogen bond mutations in the ketosteroid isomerase oxyanion hole.剖析酮甾体异构酶氧阴离子穴中氢键突变的矛盾效应。
Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):1960-5. doi: 10.1073/pnas.0911168107. Epub 2010 Jan 11.
4
Detection of large pKa perturbations of an inhibitor and a catalytic group at an enzyme active site, a mechanistic basis for catalytic power of many enzymes.
J Biol Chem. 2000 Dec 29;275(52):41100-6. doi: 10.1074/jbc.M007561200.
5
Solvation, reorganization energy, and biological catalysis.溶剂化、重组能与生物催化
J Biol Chem. 1998 Oct 9;273(41):26257-60. doi: 10.1074/jbc.273.41.26257.

生物物理学。对“极端电场助力酮甾类异构酶活性位点的催化作用”的评论。

BIOPHYSICS. Comment on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".

作者信息

Chen Deliang, Savidge Tor

机构信息

Jiangxi Key Laboratory of Organo-Pharmaceutical Chemistry, Gannan Normal University, Jiangxi 341000, China.

Department of Pathology and Immunology, Baylor College of Medicine, Houston, TX 77030, USA. Department of Pathology, Texas Children's Hospital, Houston, TX 77030, USA.

出版信息

Science. 2015 Aug 28;349(6251):936. doi: 10.1126/science.aab0095. Epub 2015 Aug 27.

DOI:10.1126/science.aab0095
PMID:26315427
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4797066/
Abstract

Fried et al. (Reports, 19 December 2014, p. 1510) demonstrate electric field-dependent acceleration of biological catalysis using ketosteroid isomerase as a prototypic example. These findings were not extended to aqueous solution because water by itself has field fluctuations that are too large and fast to provide a catalytic effect. Given physiological context, when water electrostatic interactions are considered, electric fields play a less important role in the catalysis.

摘要

弗里德等人（《报告》，2014年12月19日，第1510页）以酮甾体异构酶作为典型示例，证明了生物催化存在电场依赖性加速作用。这些发现并未扩展到水溶液中，因为水自身存在的场波动过大且过快，无法产生催化作用。考虑到生理环境，当考虑水的静电相互作用时，电场在催化过程中所起的作用较小。