ArticleThe Journal of biological chemistry2008
Light-induced hydrogen bonding pattern and driving force of electron transfer in AppA BLUF domain photoreceptor.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 26 citations in OpenAlex.
- Unraveling the Photoactivation Mechanism of a Light-Activated Adenylyl Cyclase Using Ultrafast Spectroscopy Coupled with Unnatural Amino Acid Mutagenesis.ACS chemical biology · 2022Article
- 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
- A proposal for a dipole-generated BLUF domain mechanism.Frontiers in molecular biosciences · 2015Article
- Revealing the functional states in the active site of BLUF photoreceptors from electrochromic shift calculations.The journal of physical chemistry. B · 2014Article
- Biochemistry and theory of proton-coupled electron transfer.Chemical reviews · 2014Review
- BLUF domain function does not require a metastable radical intermediate state.Journal of the American Chemical Society · 2014Article
- Redox modulation of flavin and tyrosine determines photoinduced proton-coupled electron transfer and photoactivation of BLUF photoreceptors.The Journal of biological chemistry · 2012Article
- Protein conformational gating of enzymatic activity in xanthine oxidoreductase.Journal of the American Chemical Society · 2012Article
- Structural refinement of a key tryptophan residue in the BLUF photoreceptor AppA by ultraviolet resonance Raman spectroscopy.Biophysical journal · 2010Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The AppA BLUF (blue light sensing using FAD) domain from Rhodobacter sphaeroides serves as a blue light-sensing photoreceptor. The charge separation process between Tyr-21 and flavin plays an important role in the light signaling state by transforming the dark state conformation to the light state one. By solving the linearized Poisson-Boltzmann equation, I calculated E(m) for Tyr-21, flavin, and redox-active Trp-104 and revealed the electron transfer (ET) driving energy. Rotation of the Gln-63 side chain that converts protein conformation from the dark state to the light state is responsible for the decrease of 150 mV in E(m) for Tyr-21, leading to the significantly larger ET driving energy in the light state conformation. The pK(a) values of protonation for flavin anions are essentially the same in both dark and light state crystal structures. In contrast to the ET via Tyr-21, formation of the W state results in generation of only the dark state conformation (even if the initial conformation is in the light state); this could explain why Trp-104-mediated ET deactivates the light-sensing yield and why the activity of W104A mutant is similar to that of the light-adapted native BLUF.
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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.