ArticleProceedings of the National Academy of Sciences of the United States of America2007
Dissection of complex protein dynamics in human thioredoxin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Dynamic Equilibrium between the Fluorescent State of Tryptophan and Its Cation-Electron Ion Pair Governs Triplet State Population.Journal of the American Chemical Society · 2025Article
- Hydrogen deuterium exchange defines catalytically linked regions of protein flexibility in the catecholProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Dynamics and mechanisms of DNA repair by photolyase.Physical chemistry chemical physics : PCCP · 2015Review
- Picosecond-resolved fluorescence studies of substrate and cofactor-binding domain mutants in a thermophilic alcohol dehydrogenase uncover an extended network of communication.Journal of the American Chemical Society · 2014Article
- Article
- Picosecond-resolved fluorescent probes at functionally distinct tryptophans within a thermophilic alcohol dehydrogenase: relationship of temperature-dependent changes in fluorescence to catalysis.The journal of physical chemistry. B · 2014Article
- Mode-specific reorganization energies and ultrafast solvation dynamics of Tryptophan from Raman line-shape analysis.Biophysical journal · 2013Article
- Validation of response function construction and probing heterogeneous protein hydration by intrinsic tryptophan.The journal of physical chemistry. B · 2012Article
- Femtosecond conical intersection dynamics of tryptophan in proteins and validation of slowdown of hydration layer dynamics.Journal of the American Chemical Society · 2012Article
- Ultrafast dynamics of nonequilibrium electron transfer in photoinduced redox cycle: solvent mediation and conformation flexibility.The journal of physical chemistry. B · 2012Article
- Molecular dynamics modeling of the sub-THz vibrational absorption of thioredoxin from E. coli.Journal of molecular modeling · 2012Article
- Hydration studies on the archaeal protein Sso7d using NMR measurements and MD simulations.BMC structural biology · 2011Article
- Crystal structure of the human thioredoxin reductase-thioredoxin complex.Nature communications · 2011Article
- Thiol/Disulfide redox switches in the regulation of heme binding to proteins.Antioxidants & redox signaling · 2011Review
- Mapping solvation dynamics at the function site of flavodoxin in three redox states.Journal of the American Chemical Society · 2010Article
- Ultrafast solvation dynamics at binding and active sites of photolyases.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state.The Journal of biological chemistry · 2009Article
- Mapping hydration dynamics around a protein surface.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report our direct study of complex protein dynamics in human thioredoxin by dissecting into elementary processes and determining their relevant time scales. By combining site-directed mutagenesis with femtosecond spectroscopy, we have distinguished four partly time-overlapped dynamical processes at the active site of thioredoxin. Using intrinsic tryptophan as a molecular probe and from mutation studies, we ascertained the negligible contribution to solvation by protein sidechains and observed that the hydration dynamics at the active site occur in 0.47-0.67 and 10.8-13.2 ps. With reduced and oxidized states, we determined the electron-transfer quenching dynamics between excited tryptophan and a nearby disulfide bond in 10-17.5 ps for three mutants. A robust dynamical process in 95-114 ps, present in both redox states and all mutants regardless of neighboring charged, polar, and hydrophobic residues around the probe, is attributed to the charge transfer reaction with its adjacent peptide bond. Site-directed mutations also revealed the electronic quenching dynamics by an aspartate residue at a hydrogen bond distance in 275-615 ps. The local rotational dynamics determined by the measurement of anisotropy changes with time unraveled a relatively rigid local configuration but implies that the protein fluctuates on the time scale of longer than nanoseconds. These results elucidate the temporal evolution of hydrating water motions, electron-transfer reactions, and local protein fluctuations at the active site, and show continuously synergistic dynamics of biological function over wide time scales.
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