Jan-Stefan Völler1, Hernan Biava2, Peter Hildebrandt3, Nediljko Budisa4. 1. Department of Chemistry, Technische Universität Berlin, Müller-Breslau-Strasse 10, D-10623 Berlin, Germany. Electronic address: jan.voeller@85mail.com. 2. Department of Chemistry, Technische Universität Berlin, Müller-Breslau-Strasse 10, D-10623 Berlin, Germany; Department of Chemistry, Technische Universität Berlin, Straße des 17. Juni 135, D-10623 Berlin, Germany. 3. Department of Chemistry, Technische Universität Berlin, Straße des 17. Juni 135, D-10623 Berlin, Germany. Electronic address: hildebrandt@chem.tu-berlin.de. 4. Department of Chemistry, Technische Universität Berlin, Müller-Breslau-Strasse 10, D-10623 Berlin, Germany. Electronic address: budisa@chem.tu-berlin.de.
Abstract
BACKGROUND: To 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 REVIEW: This 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 CONCLUSIONS: ncAAs 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 SIGNIFICANCE: Mapping 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.
BACKGROUND: To 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 REVIEW: This 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 CONCLUSIONS: ncAAs 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 SIGNIFICANCE: Mapping 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.
Authors: Jacek Kozuch; Samuel H Schneider; Chu Zheng; Zhe Ji; Richard T Bradshaw; Steven G Boxer Journal: J Phys Chem B Date: 2021-04-26 Impact factor: 2.991