ArticleBiophysical journal2005
The phot LOV2 domain and its interaction with LOV1.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Article
- Protein Electrostatics Tune the Singlet-Triplet Energy Gap in Natural and Engineered Phototropin Light-Oxygen-Voltage (LOV) Domains.Journal of the American Chemical Society · 2026Article
- Red Shift in the Absorption Spectrum of Phototropin LOV1 upon the Formation of a Semiquinone Radical: Reconstructing the Orbital Architecture.The journal of physical chemistry. B · 2024Article
- Modulation of Phototropin Signalosome with Artificial Illumination Holds Great Potential in the Development of Climate-Smart Crops.Current genomics · 2021Review
- Tailored flavoproteins acting as light-driven spin machines pump nuclear hyperpolarization.Scientific reports · 2020Article
- Resonance energy transfer sensitises and monitors in situ switching of LOV2-based optogenetic actuators.Nature communications · 2020Article
- New Light on the Mechanism of Phototransduction in Phototropin.Biochemistry · 2020Article
- In-cell infrared difference spectroscopy of LOV photoreceptors reveals structural responses to light altered in living cells.The Journal of biological chemistry · 2020Article
- Nuclear spin-hyperpolarization generated in a flavoprotein under illumination: experimental field-dependence and theoretical level crossing analysis.Scientific reports · 2019Article
- Differential UVR8 Signal across the Stem Controls UV-B-Induced Inflorescence Phototropism.The Plant cell · 2019Article
- 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
- A simple optogenetic MAPK inhibitor design reveals resonance between transcription-regulating circuitry and temporally-encoded inputs.Nature communications · 2017Article
- Molecular mechanism of phototropin light signaling.Journal of plant research · 2016Review
- Regulation of neural gene transcription by optogenetic inhibition of the RE1-silencing transcription factor.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A critical element of the light-induced quaternary structural changes in YtvA-LOV.Protein science : a publication of the Protein Society · 2015Article
- Light-induced conformational changes of LOV1 (light oxygen voltage-sensing domain 1) and LOV2 relative to the kinase domain and regulation of kinase activity in Chlamydomonas phototropin.The Journal of biological chemistry · 2014Article
- The Neurospora photoreceptor VIVID exerts negative and positive control on light sensing to achieve adaptation.Molecular systems biology · 2013Article
- News about cryptochrome photoreceptors in algae.Plant signaling & behavior · 2013Article
- Phototropin influence on eyespot development and regulation of phototactic behavior in Chlamydomonas reinhardtii.The Plant cell · 2012Article
- A flavin binding cryptochrome photoreceptor responds to both blue and red light in Chlamydomonas reinhardtii.The Plant cell · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phot proteins are homologs of the blue-light receptor phototropin. We report a comparative study of the photocycles of the isolated, light-sensitive domains LOV1 and LOV2 from Chlamydomonas reinhardtii phot protein, as well as the construct LOV1/2 containing both domains. Transient absorption measurements revealed a short lifetime of the LOV2-wt triplet state (500 ns), but a long lifetime (287 micros) of the triplet in the mutant LOV2-C250S, in which the reactive cysteine is replaced by serine. For LOV1, in comparison, corresponding numbers of 800 ns and 4 micros for the two conformers in LOV1-wt, and 27 micros for LOV1-C57S have been reported. The triplet decay kinetics in the mixed domains LOV1/2-wt, LOV1/2-C57S, and LOV1/2-C250S can be analyzed as the superposition of the behavior of the corresponding single domains. The situation is different for the slow, thermal reaction of the photoadduct back to the dark form. Whereas the individual domains LOV1 and LOV2 show two decay components, the double domains LOV1/2-C57S and LOV1/2-C250S both show only a single component. The interaction of the two domains does therefore not manifest itself during the lifetime of the triplet states, but changes the decay behavior of the adduct states.
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