Assignments of 19F NMR resonances and exploration of dynamics in a long-chain flavodoxin

Taylor A. Varner, Nishya Mohamed-Raseek, Anne Frances Miller

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


Flavodoxin is a small protein that employs a non-covalently bound flavin to mediate single-electron transfer at low potentials. The long-chain flavodoxins possess a long surface loop that is proposed to interact with partner proteins. We have incorporated 19F-labeled tyrosine in long-chain flavodoxin from Rhodopseudomonas palustris to gain a probe of possible loop dynamics, exploiting the presence of a Tyr in the long loop in addition to Tyr residues near the flavin. We report 19F resonance assignments for all four Tyrs, and demonstration of a pair of resonances in slow exchange, both corresponding to a Tyr adjacent to the flavin. We also provide evidence for dynamics affecting the Tyr in the long loop. Thus, we show that 19F NMR of 19F-Tyr labeled flavodoxin holds promise for monitoring possible changes in conformation upon binding to partner proteins.

Original languageEnglish
Article number108839
JournalArchives of Biochemistry and Biophysics
StatePublished - May 30 2021

Bibliographical note

Publisher Copyright:
© 2021 Elsevier Inc.


  • F NMR
  • Fluoro-tyrosine
  • Long-chain flavodoxin
  • Partner protein interactions
  • Protein dynamics

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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