Determining large hyperfine interactions of a model flavoprotein in the semiquinone state using pulse EPR (electron paramagnetic resonance) techniques.

ABSTRACT: Flavoproteins are a versatile class of proteins involved in numerous biological processes, including redox reactions, electron transfer, and signal transduction, often relying on their ability to stabilize different oxidation states of their flavin cofactor. A critical feature of flavin cofactors is their capacity to achieve, within particular protein environments, a semiquinone state that plays a pivotal role in mediating single-electron transfer events and that is key to understanding flavoprotein reactivity. Hyperfine interactions between the unpaired electron and magnetic nuclei in the isoalloxazine ring provide valuable insights into the semiquinone state and its mechanistic roles. This study investigates the hyperfine interactions of isotopically labeled flavodoxin (Fld) with 13C and

SUBMITTER: Martinez JI 

PROVIDER: S-EPMC12326372 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature