ArticleBiophysical journal2004
Recording of blue light-induced energy and volume changes within the wild-type and mutated phot-LOV1 domain from Chlamydomonas reinhardtii.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025Review
- Machine Learning-Assisted Engineering of Light, Oxygen, Voltage Photoreceptor Adduct Lifetime.JACS Au · 2023Article
- Arguments for an additional long-lived intermediate in the photocycle of the full-length aureochrome 1c receptor: A time-resolved small-angle X-ray scattering study.Structural dynamics (Melville, N.Y.) · 2019Article
- Glutamine Amide Flip Elicits Long Distance Allosteric Responses in the LOV Protein Vivid.Journal of the American Chemical Society · 2017Article
- The dark recovery rate in the photocycle of the bacterial photoreceptor YtvA is affected by the cellular environment and by hydration.PloS one · 2014Article
- Photosensitivity of kinase activation by blue light involves the lifetime of a cysteinyl-flavin adduct intermediate, S390, in the photoreaction cycle of the LOV2 domain in phototropin, a plant blue light receptor.The Journal of biological chemistry · 2012Article
- Signals of LOV1: a computer simulation study on the wildtype LOV1-domain of Chlamydomonas reinhardtii and its mutants.Journal of molecular modeling · 2012Article
- A LOV protein modulates the physiological attributes of Xanthomonas axonopodis pv. citri relevant for host plant colonization.PloS one · 2012Article
- Effect of computational methodology on the conformational dynamics of the protein photosensor LOV1 from Chlamydomonas reinhardtii.Journal of chemical biology · 2011Article
- Structural basis of photosensitivity in a bacterial light-oxygen-voltage/helix-turn-helix (LOV-HTH) DNA-binding protein.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Kinetics of conformational changes of the FKF1-LOV domain upon photoexcitation.Biophysical journal · 2010Article
- Article
- Primary reactions of the LOV2 domain of phototropin studied with ultrafast mid-infrared spectroscopy and quantum chemistry.Biophysical journal · 2009Article
- A conserved glutamine plays a central role in LOV domain signal transmission and its duration.Biochemistry · 2008Article
- A blue light inducible two-component signal transduction system in the plant pathogen Pseudomonas syringae pv. tomato.Biophysical journal · 2008Article
- NTP-binding properties of the blue-light receptor YtvA and effects of the E105L mutation.European biophysics journal : EBJ · 2007Article
- Conformational switching in the fungal light sensor Vivid.Science (New York, N.Y.) · 2007Article
- Dynamic switching mechanisms in LOV1 and LOV2 domains of plant phototropins.Biophysical journal · 2006Article
- Kinetic measurement of transient dimerization and dissociation reactions of Arabidopsis phototropin 1 LOV2 domain.Biophysical journal · 2006Article
- When light falls in LOV: a quantum mechanical/molecular mechanical study of photoexcitation in Phot-LOV1 of Chlamydomonas reinhardtii.The journal of physical chemistry. B · 2005Article
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3 authors.
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Abstract
The time-resolved thermodynamics of the flavin mononucleotide (FMN)-binding LOV1 domain of Chlamydomonas reinhardtii phot (phototropin homolog) was studied by means of laser-induced optoacoustic spectroscopy. In the wild-type protein the early red-shifted intermediate LOV(715) exhibits a small volume contraction, DeltaV(715) = -1.50 ml/mol, with respect to the parent state. LOV(715) decays within few micro s into the covalent FMN-Cys-57 adduct LOV(390), that shows a larger contraction, DeltaV(390) = -8.8 ml/mol, suggesting a loss of entropy and conformational flexibility. The high energy content of LOV(390), E(390) = 180 kJ/mol, ensures the driving force for the completion of the photocycle and points to a strained photoreceptor conformation. In the LOV-C57S mutated protein the photoadduct is not formed and DeltaV(390) is undetected. Large effects on the measured DeltaVs are observed in the photochemically competent R58K and R58K/D31Q mutated proteins, with DeltaV(390) = -2.0 and -1.9 ml/mol, respectively, and DeltaV(715) approximately 0. The D31Q and D31N substitutions exhibit smaller but well-detectable effects. These results show that the photo-induced volume changes involve the protein region comprising Arg-58, which tightly interacts with the FMN phosphate group.
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