ArticleBiophysical journal2010
Structural refinement of a key tryptophan residue in the BLUF photoreceptor AppA by ultraviolet resonance Raman spectroscopy.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Probing the Signal Transduction Mechanism of the Light-Activated Adenylate Cyclase OaPAC Using Unnatural Amino Acid Mutagenesis.ACS chemical biology · 2025Article
- Lung cancer diagnosis through extracellular vesicle analysis using label-free surface-enhanced Raman spectroscopy coupled with machine learning.Theranostics · 2025Article
- Time-resolved diffusion reveals photoreactions of BLUF proteins with similar functional domains.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Review
- Structural Basis for the Regulation of Biofilm Formation and Iron Uptake inACS infectious diseases · 2020Article
- Light-induced chromophore and protein responses and mechanical signal transduction of BLUF proteins.Biophysical reviews · 2018Review
- Evidence for Tautomerisation of Glutamine in BLUF Blue Light Receptors by Vibrational Spectroscopy and Computational Chemistry.Scientific reports · 2016Article
- A proposal for a dipole-generated BLUF domain mechanism.Frontiers in molecular biosciences · 2015Article
- Photochemistry of flavoprotein light sensors.Nature chemical biology · 2014Review
- Revealing the functional states in the active site of BLUF photoreceptors from electrochromic shift calculations.The journal of physical chemistry. B · 2014Article
- Article
- Site-specific protein dynamics in communication pathway from sensor to signaling domain of oxygen sensor protein, HemAT-Bs: Time-resolved Ultraviolet Resonance Raman Study.The Journal of biological chemistry · 2012Article
- Tripping the light fantastic: blue-light photoreceptors as examples of environmentally modulated protein-protein interactions.Biochemistry · 2011Review
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3 authors.
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Abstract
The flavin-adenine-dinucleotide-binding BLUF domain constitutes a new class of blue-light receptors, and the N-terminal domain of AppA is a representative of this family. The BLUF domain is of special interest because it uses a rigid flavin rather than an isomerizable chromophore, such as a rhodopsin or phytochrome, for its light-activation process. Crystal and solution structures of several BLUF domains were recently obtained, and their overall structures are consistent. However, there is a key ambiguity regarding the position of a conserved tryptophan (Trp-104 in AppA), in that this residue was found either close to flavin (Trp(in) conformation) or exposed to the solvent (Trp(out) conformation). The location of Trp-104 is a crucial factor in understanding the photocycle mechanism of BLUF domains, because this residue has been shown to play an essential role in the activation of AppA. In this study, we demonstrated a Trp(in) conformation for the BLUF domain of AppA through direct observation of the vibrational spectrum of Trp-104 by ultraviolet resonance Raman spectroscopy, and also observed light-induced conformational and environmental changes in Trp-104. This study provides a structural basis for future investigations of the photocycle mechanism of BLUF proteins.
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