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Fluorination of a conserved tyrosine in POR offers new clues for proton transfer.

Chen-Song DongLin Liu
Published in: The FEBS journal (2024)
Reduction of the 17,18-double bond in the D-ring during chlorophyll biosynthesis is catalyzed by the rare, naturally occurring photoenzyme protochlorophyllide oxidoreductase (POR). A conserved tyrosine residue has been suggested to donate a proton to C18 of the substrate in the past decades. Taylor and colleagues scrutinized the model with a powerful tool that utilized a modified genetic code to introduce fluorinated tyrosine analogues into POR. The presented results show that the suggested catalytically critical tyrosine is unlikely to participate in the reaction chemistry but is required for substrate binding, and instead, a cysteine residue preceding the lid helix is proposed to have the role of proton donor.
Keyphrases
  • electron transfer
  • transcription factor
  • amino acid
  • dna binding
  • genome wide
  • molecular docking
  • gene expression
  • copy number
  • structural basis
  • single molecule
  • structure activity relationship