title: BIOPHYSICS. Comment on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".
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.
authors: Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA.
authors: Aditya
authors: A
authors: Natarajan
authors: Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA.
authors: Filip
authors: F
authors: Yabukarski
authors: Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA.
authors: Vandana
authors: V
authors: Lamba
authors: Department of Chemistry and Biochemistry, California State University Long Beach, Long Beach, CA 90840, USA.
authors: Jason P
authors: JP
authors: Schwans
authors: Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA.
authors: Fanny
authors: F
authors: Sunden
authors: Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, USA. herschla@stanford.edu.
authors: Daniel
authors: D
authors: Herschlag
mesh_terms: D007664:Ketosteroids / Q000378:metabolism*; D055672:Static Electricity; D013251:Steroid Isomerases / Q000737:chemistry*
chemical_list: D007664:Ketosteroids; D013251:Steroid Isomerases