ArticleThe journal of physical chemistry. B2010
On the origin of fluorescence in bacteriophytochrome infrared fluorescent proteins.
Article in The journal of physical chemistry. B, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Modulation of biliverdin dynamics and spectral properties by Sandercyanin.RSC advances · 2022Article
- UV-trained and metal-enhanced fluorescence of biliverdin and biliverdin nanoparticles.Nanoscale · 2021Article
- mRhubarb: Engineering of monomeric, red-shifted, and brighter variants of iRFP using structure-guided multi-site mutagenesis.Scientific reports · 2019Article
- Fluorescence enhancement of a ligand-activated fluorescent protein induced by collective noncovalent interactions.Chemical science · 2018Article
- Blue protein with red fluorescence.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Removal of Chromophore-Proximal Polar Atoms Decreases Water Content and Increases Fluorescence in a Near Infrared Phytofluor.Frontiers in molecular biosciences · 2015Article
- Atomic force microscopy of red-light photoreceptors using peakforce quantitative nanomechanical property mapping.Journal of visualized experiments : JoVE · 2014Article
- Structure-guided engineering enhances a phytochrome-based infrared fluorescent protein.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Tsien et al. (Science, 2009, 324, 804-807) recently reported the creation of the first infrared fluorescent protein (IFP). It was engineered from bacterial phytochrome by removing the PHY and histidine kinase-related domains, by optimizing the protein to prevent dimerization, and by limiting the biliverdins conformational freedom, especially around its D ring. We have used database analyses and molecular dynamics simulations with freely rotating chromophoric dihedrals in order to model the dihedral freedom available to the biliverdin D ring in the excited state and to show that the tetrapyrrole ligands in phytochromes are flexible and can adopt many conformations; however, their conformational space is limited/defined by the chemospatial characteristics of the protein cavity. Our simulations confirm that the reduced accessibility to conformations geared to an excited state proton transfer may be responsible for the fluorescence in IFP, just as has been suggested by Kennis et al. (Proc. Natl. Acad. Sci. U.S.A., 2010, 107, 9170-9175) for fluorescent bacteriophytochrome from Rhodopseudomonas palustris.
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.