Structural refinement of a key tryptophan residue in the BLUF photoreceptor AppA by ultraviolet resonance Raman spectroscopy.

No abstract is available for this paper.

• Publication year

  2010

• Venue

  Biophysical Journal

• Publication date

  2010-05-05

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/j.bpj.2010.01.007PMID 20441759PMCID PMC2862157
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Spectroscopic studies of the AppA BLUF domain from Rhodobacter sphaeroides: addressing movement of tryptophan 104 in the signaling state.

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• Light-induced Hydrogen Bonding Pattern and Driving Force of Electron Transfer in AppA BLUF Domain Photoreceptor*

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• On the signaling mechanism and the absence of photoreversibility in the AppA BLUF domain.

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• Hydrogen bond switching among flavin and amino acid side chains in the BLUF photoreceptor observed by ultrafast infrared spectroscopy.

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• FTIR study on the hydrogen bond structure of a key tyrosine residue in the flavin-binding blue light sensor TePixD from Thermosynechococcus elongatus.

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• On the role of aromatic side chains in the photoactivation of BLUF domains.

  2007cited by this paper
• The critical role of a hydrogen bond between Gln63 and Trp104 in the blue-light sensing BLUF domain that controls AppA activity.

  2007influential reference
• Ultrafast structural dynamics in BLUF domains: transient infrared spectroscopy of AppA and its mutants.

  2007cited by this paper
• Crystal structures of the Synechocystis photoreceptor Slr1694 reveal distinct structural states related to signaling.

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  2006cited by this paper
• On the mechanism of activation of the BLUF domain of AppA.

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  2005cited by this paper
• Tryptophan at position 104 is involved in transforming light signal into changes of beta-sheet structure for the signaling state in the BLUF domain of AppA.

  2005cited by this paper
• Primary intermediate in the photocycle of a blue-light sensory BLUF FAD-protein, Tll0078, of Thermosynechococcus elongatus BP-1.

  2005influential reference
• Structure of a novel photoreceptor, the BLUF domain of AppA from Rhodobacter sphaeroides.

  2005influential reference
• Structure of a cyanobacterial BLUF protein, Tll0078, containing a novel FAD-binding blue light sensor domain.

  2005influential reference
• Light-induced structural changes of apoprotein and chromophore in the sensor of blue light using FAD (BLUF) domain of AppA for a signaling state.

  2005cited by this paper
• The Antirepressor AppA Uses the Novel Flavin‐Binding BLUF Domain as a Blue‐Light‐Absorbing Photoreceptor to Control Photosystem Synthesis

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• Handbook of Photosensory Receptors

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  2005cited by this paper
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  2003cited by this paper
• BLUF: a novel FAD-binding domain involved in sensory transduction in microorganisms.

  2002cited by this paper
• AppA is a blue light photoreceptor that antirepresses photosynthesis gene expression in Rhodobacter sphaeroides.

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• Hemoglobin R.fwdarw.T structural dynamics from simultaneous monitoring of tyrosine and tryptophan time-resolved UV resonance Raman signals

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• UV resonance Raman excitation profiles of the aromatic amino acids

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• Resonance enhancement in the ultraviolet Raman spectra of aromatic amino acids

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  2020cites this paper
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  2018cites this paper
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  2017cites this paper
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  2016cites this paper
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  2015cites this paper
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  2014cites this paper
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  2014cites this paper
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