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• W3192571275 endingPage "7782" @default.
• W3192571275 startingPage "7777" @default.
• W3192571275 abstract "Enzyme catalysis achieves tremendous rate accelerations. Enzyme reaction centers provide a constraint geometry that preferentially binds an activated form of the substrate and thus lowers the energy barrier. However, this transition state picture neglects the flexibility of proteins and its role in enzymatic catalysis. Especially for proton transfer reactions, it has been suggested that motions of the protein modulate the donor–acceptor distance and prepare a tunneling-ready state. We report the detection of frequency fluctuations of an azide anion (N3–) bound in the active site of the protein carbonic anhydrase II, where a low-frequency mode of the protein has been proposed to facilitate proton transfer over two water molecules during the catalyzed reaction. 2D-IR spectroscopy resolves an underdamped low-frequency mode at about 1 THz (30 cm–1). We find its frequency to be viscosity- and temperature-dependent and to decrease by 6 cm–1 between 230 and 320 K, reporting the softening of the mode’s potential." @default.
• W3192571275 created "2021-08-16" @default.
• W3192571275 creator A5046001985 @default.
• W3192571275 creator A5055324791 @default.
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• W3192571275 date "2021-08-10" @default.
• W3192571275 modified "2023-09-23" @default.
• W3192571275 title "Temperature-Dependent Low-Frequency Modes in the Active Site of Bovine Carbonic Anhydrase II Probed by 2D-IR Spectroscopy" @default.
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• W3192571275 doi "https://doi.org/10.1021/acs.jpclett.1c01453" @default.
• W3192571275 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34374547" @default.
• W3192571275 hasPublicationYear "2021" @default.
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