ArticleJournal of the American Chemical Society2010
Mapping solvation dynamics at the function site of flavodoxin in three redox states.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed.
- Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography.Nature chemistry · 2024Article
- Ultrafast Dynamics and Catalytic Mechanism of Fatty Acid Photodecarboxylase.Angewandte Chemie (International ed. in English) · 2022Article
- Roles of Ferredoxin-NADPAntioxidants (Basel, Switzerland) · 2022Review
- The nature of proton-coupled electron transfer in a blue light using flavin domain.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Revealing the origin of multiphasic dynamic behaviors in cyanobacteriochrome.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Origin of Ultrafast Multiphasic Dynamics in Photoisomerization of Bacteriophytochrome.The journal of physical chemistry letters · 2020Article
- Effects of nonequilibrium fluctuations on ultrafast short-range electron transfer dynamics.Nature communications · 2020Article
- Nonequilibrium dynamics of photoinduced forward and backward electron transfer reactions.The Journal of chemical physics · 2020Article
- Short-Range Electron Transfer in Reduced Flavodoxin: Ultrafast Nonequilibrium Dynamics Coupled with Protein Fluctuations.The journal of physical chemistry letters · 2018Article
- Role of a Conserved Tyrosine Residue in the FMN-Heme Interdomain Electron Transfer in Inducible Nitric Oxide Synthase.The journal of physical chemistry. A · 2016Article
- Mutants of Cytochrome P450 Reductase Lacking Either Gly-141 or Gly-143 Destabilize Its FMN Semiquinone.The Journal of biological chemistry · 2016Article
- 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
- 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
- Dynamic Determination of Active-Site Reactivity in Semiquinone Photolyase by the Cofactor Photoreduction.The journal of physical chemistry letters · 2014Article
- Femtosecond dynamics of short-range protein electron transfer in flavodoxin.Biochemistry · 2013Article
- Direct probing of solvent accessibility and mobility at the binding interface of polymerase (Dpo4)-DNA complex.The journal of physical chemistry. A · 2013Article
- Determining complete electron flow in the cofactor photoreduction of oxidized photolyase.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Ultrafast real-time visualization of active site flexibility of flavoenzyme thymidylate synthase ThyX.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Flavoproteins are unique redox coenzymes, and the dynamic solvation at their function sites is critical to the understanding of their electron-transfer properties. Here, we report our complete characterization of the function-site solvation of holoflavodoxin in three redox states and of the binding-site solvation of apoflavodoxin. Using intrinsic flavin cofactor and tryptophan residue as the local optical probes with two site-specific mutations, we observed distinct ultrafast solvation dynamics at the function site in the three states and at the related recognition site of the cofactor, ranging from a few to hundreds of picoseconds. The initial ultrafast motion in 1-2.6 ps reflects the local water-network relaxation around the shallow, solvent-exposed function site. The second relaxation in 20-40 ps results from the coupled local water-protein fluctuation. The third dynamics in hundreds of picoseconds is from the intrinsic fluctuation of the loose loops flanking the cofactor at the function site. These solvation dynamics with different amplitudes well correlate with the redox states from the oxidized form, to the more rigid semiquinone and to the much looser hydroquinone. This observation of the redox control of local protein conformation plasticity and water network flexibility is significant, and such an intimate relationship is essential to the biological function of interprotein electron transfer.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.