An expanded genetic code for probing the role of electrostatics in enzyme catalysis by vibrational Stark spectroscopy
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. This review examines the applications of non-canonical amino acids (ncAAs) as genetically encod...
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| Published in | Biochimica et biophysica acta. General subjects Vol. 1861; no. 11; pp. 3053 - 3059 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
01.11.2017
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| Abstract | 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.
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.
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.
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.
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•Enzyme electrostatics have a great impact on catalytic reactions.•Strong evidence for this concept is provided on the basis of VSS.•Genetically encoded VSE-active ncAAs substantially broaden the potential of VSS.•VSS with ncAAs enables studying the role of global electrostatics in biocatalysis. |
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| AbstractList | 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.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.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.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. 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. 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. 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. 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. 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. 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. 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. 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. [Display omitted] •Enzyme electrostatics have a great impact on catalytic reactions.•Strong evidence for this concept is provided on the basis of VSS.•Genetically encoded VSE-active ncAAs substantially broaden the potential of VSS.•VSS with ncAAs enables studying the role of global electrostatics in biocatalysis. 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.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.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.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.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.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.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.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. |
| Author | Völler, Jan-Stefan Hildebrandt, Peter Budisa, Nediljko Biava, Hernan |
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| Keywords | Non-canonical amino acids Vibrational Stark spectroscopy Enzyme catalysis Enzyme electrostatics Electric fields |
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Phys. Chem. B doi: 10.1021/jp301054e – volume: 11 year: 2015 ident: 10.1016/j.bbagen.2017.02.009_bb0305 article-title: Secondary structure across the bacterial Transcriptome reveals versatile roles in mRNA regulation and function publication-title: PLoS Genet. doi: 10.1371/journal.pgen.1005613 |
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| Snippet | To find experimental validation for electrostatic interactions essential for catalytic reactions represents a challenge due to practical limitations in... |
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| SubjectTerms | amino acids biocatalysts Catalysis catalytic activity electric field Electric fields electrostatic interactions Enzyme catalysis Enzyme electrostatics Genetic Code Molecular Dynamics Simulation Non-canonical amino acids Protein Engineering - methods proteins Proteins - chemistry Proteins - genetics Proteins - metabolism spectroscopy Spectrum Analysis - methods Static Electricity synthetic biology Vibration Vibrational Stark spectroscopy |
| Title | An expanded genetic code for probing the role of electrostatics in enzyme catalysis by vibrational Stark spectroscopy |
| URI | https://dx.doi.org/10.1016/j.bbagen.2017.02.009 https://www.ncbi.nlm.nih.gov/pubmed/28229928 https://www.proquest.com/docview/1871554470 https://www.proquest.com/docview/2000341060 |
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