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Enhancing Proton-Coupled Electron Transfer in Blue Light Using FAD Photoreceptor AppABLUF.

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Blue light receptors (BLUF) use FAD for light absorption. Modifying hydrogen bonds in AppABLUF triggers flavin radical formation, revealing key electron transfer mechanisms in BLUF photoreceptor activation.

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Area of Science:

  • Biochemistry
  • Photochemistry
  • Molecular Biology

Background:

  • Blue Light Using FAD (BLUF) photoreceptors are light-activated proteins.
  • They utilize a noncovalently bound flavin adenine dinucleotide (FAD) cofactor.
  • BLUF proteins initiate signaling cascades upon light absorption.

Purpose of the Study:

  • Investigate the mechanism of BLUF photoreceptor activation.
  • Determine the role of hydrogen bonding and electron transfer in BLUF photocycle.
  • Compare the photocycle mechanisms of PixD and AppABLUF.

Main Methods:

  • Site-directed mutagenesis to alter hydrogen bonding networks.
  • Time-resolved infrared (TRIR) spectroscopy to detect radical intermediates.
  • Analysis of flavin radical formation and light state generation.

Main Results:

  • Introducing a second hydrogen bond to the flavin C2═O in AppABLUF induced flavin radical (FAD•- and FADH•) formation.
  • Replacing the conserved tyrosine with trifluoro-tyrosine in the double mutant abolished radical formation.
  • The modified AppABLUF exhibited a photocycle similar to PixD, involving proton-coupled electron transfer (PCET).

Conclusions:

  • Hydrogen bonding to the flavin C2═O is critical for triggering PCET in BLUF photoreceptors.
  • The study elucidates the mechanism of BLUF photoactivation, highlighting the role of electron transfer.
  • Differences in hydrogen bonding networks explain variations in BLUF protein photocycle mechanisms.