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Science. 2015 Aug 28;349(6251):936. doi: 10.1126/science.aab1584. Epub 2015 Aug 27.

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

Author information

1
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA.
2
Department of Chemistry and Biochemistry, California State University Long Beach, Long Beach, CA 90840, USA.
3
Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA. herschla@stanford.edu.

Abstract

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.

PMID:
26315426
DOI:
10.1126/science.aab1584
[Indexed for MEDLINE]
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