The relationship between redox enzyme activity and electrochemical potential—cellular and mechanistic implications from protein film electrochemistry
| Autor: | Sophie J. Marritt, David J. Richardson, Andrew J. Gates, Chun Yip To, James Mann, Andrew G. Mayes, Julea N. Butt, Gemma L. Kemp |
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| Rok vydání: | 2011 |
| Předmět: |
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Molecular General Physics and Astronomy Electrochemistry Nitrate Reductase Redox Catalysis Structure-Activity Relationship Physical and Theoretical Chemistry Electrochemical potential chemistry.chemical_classification Nitrates biology Substrate (chemistry) Electrochemical Techniques Enzyme assay Enzymes Kinetics Enzyme chemistry Biochemistry Paracoccus pantotrophus Biocatalysis biology.protein Biophysics Oxidation-Reduction Function (biology) |
| Zdroj: | Physical Chemistry Chemical Physics. 13:7720 |
| ISSN: | 1463-9084 1463-9076 |
| Popis: | In protein film electrochemistry a redox protein of interest is studied as an electroactive film adsorbed on an electrode surface. For redox enzymes this configuration allows quantification of the relationship between catalytic activity and electrochemical potential. Considered as a function of enzyme environment, i.e., pH, substrate concentration etc., the activity-potential relationship provides a fingerprint of activity unique to a given enzyme. Here we consider the nature of the activity-potential relationship in terms of both its cellular impact and its origin in the structure and catalytic mechanism of the enzyme. We propose that the activity-potential relationship of a redox enzyme is tuned to facilitate cellular function and highlight opportunities to test this hypothesis through computational, structural, biochemical and cellular studies. |
| Databáze: | OpenAIRE |
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