Is Trehalose an Effective Quenching Agent of
| Autor: | Stephen P. Cramer, Leland B. Gee, Christie H. Dapper, William E. Newton, Aubrey D. Scott |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Ethylene Disaccharide Reaction intermediate 010402 general chemistry Photochemistry 01 natural sciences Article law.invention Inorganic Chemistry 03 medical and health sciences chemistry.chemical_compound law Materials Chemistry Organic chemistry Physical and Theoretical Chemistry Electron paramagnetic resonance biology Nitrogenase biology.organism_classification Trehalose 0104 chemical sciences 030104 developmental biology chemistry Azotobacter vinelandii Ethylene glycol |
| Zdroj: | Inorganica chimica acta. 453 |
| ISSN: | 0020-1693 |
| Popis: | H(2)-evolution assays, plus EPR and FTIR spectroscopies, using CO-inhibited Azotobacter vinelandii Mo-nitrogenase have shown that the disaccharide trehalose is an effective quenching agent of enzymatic turnover and also stabilizes the reaction intermediates formed. Complete inhibition of H(2)-evolution activity was achieved at 1.5 M trehalose, which compares favorably to the requirement for 10 M ethylene glycol to achieve similar inhibition. Reaction-intermediate stabilization was demonstrated by monitoring the EPR spectrum of the ‘hi-CO’ form of CO-inhibited N(2)ase, which did not change during 1 hr after trehalose quenching. Similarly, in situ photolysis with FTIR monitoring of ‘hi-CO’ resulted in the same 1973 and 1681 cm(−1) signals as observed previously in ethylene glycol-quenched systems. [a] These results clearly show that 1.5 M trehalose is an effective quench and stabilization agent for Mo-N(2)ase studies. Possible applications are discussed. |
| Databáze: | OpenAIRE |
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