ArticleThe journal of physical chemistry. B2009
Exploring the molecular origins of protein dynamics in the active site of human carbonic anhydrase II.
Article in The journal of physical chemistry. B, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Oscillatory Active-site Motions Correlate with Kinetic Isotope Effects in Formate Dehydrogenase.ACS catalysis · 2019Article
- Site-Specific 1D and 2D IR Spectroscopy to Characterize the Conformations and Dynamics of Protein Molecular Recognition.The journal of physical chemistry. B · 2019Article
- Article
- Ultrafast infrared spectroscopy reveals water-mediated coherent dynamics in an enzyme active site.Chemical science · 2015Article
- Relationship of femtosecond-picosecond dynamics to enzyme-catalyzed H-transfer.Topics in current chemistry · 2013Review
- Ribonuclease S dynamics measured using a nitrile label with 2D IR vibrational echo spectroscopy.The journal of physical chemistry. B · 2012Article
- 3-picolyl azide adenine dinucleotide as a probe of femtosecond to picosecond enzyme dynamics.The journal of physical chemistry. B · 2012Article
- Two-dimensional IR spectroscopy of protein dynamics using two vibrational labels: a site-specific genetically encoded unnatural amino acid and an active site ligand.The journal of physical chemistry. B · 2011Article
- Two-dimensional infrared spectroscopy of azido-nicotinamide adenine dinucleotide in water.The Journal of chemical physics · 2011Article
- Modulating Accidental Fermi Resonance: What a Difference a Neutron Makes.The journal of physical chemistry letters · 2011Article
- Characterization of azido-NAD+ to assess its potential as a two-dimensional infrared probe of enzyme dynamics.Analytical biochemistry · 2010Article
- Characterizing the dynamics of functionally relevant complexes of formate dehydrogenase.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
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6 authors.
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Abstract
We present three-pulse vibrational echo measurements of azide ion bound to the active site Zn of human carbonic anhydrase II (HCA II) and of two separate active-site mutants Thr199 --> Ala (T199A) and Leu198 --> Phe (L198F). Because structural motions of the protein active site influence the frequency of bound ligands, the differences in the time scales of the frequency-frequency correlation functions (FFCFs) obtained from global fits to each set of data allow us to make inferences about the time scales of the active site dynamics of HCA II. Surprisingly, the deletion of a potential electrostatic interaction in results in very little change in the FFCF, but the insertion of the bulky phenylalanine ring in causes much faster dynamics. We conclude that the fast, sub-picosecond time scale in the correlation function is attributable to hydrogen bond dynamics, and the slow, apparently static contribution is due to the conformational flexibility of Zn-bound azide in the active site.
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