An expanded genetic code for probing the role of electrostatics in enzyme catalysis by vibrational Stark spectroscopy

Publication date: Available online 14 February 2017
Source:Biochimica et Biophysica Acta (BBA) - General Subjects
Author(s): Jan-Stefan Völler, Hernan Biava, Peter Hildebrandt, Nediljko Budisa
BackgroundTo find experimental validation for electrostatic interactions essential for catalytic reactions represents a challenge due to practical limitations in assessing electric fields within protein structures.Scope of reviewThis review examines the applications of non-canonical amino acids (ncAAs) as genetically encoded probes for studying the role of electrostatic interactions in enzyme catalysis.Major conclusionsncAAs constitute sensitive spectroscopic probes to detect local electric fields by exploiting the vibrational Stark effect (VSE) and thus have the potential to map the protein electrostatics.General significanceMapping the electrostatics in proteins will improve our understanding of natural catalytic processes and, in beyond, will be helpful for biocatalyst engineering. This article is part of a Special Issue entitled “Biochemistry of Synthetic Biology - Recent Developments” Guest Editor: Dr. Ilka Heinemann and Dr. Patrick O'Donoghue.

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