A lonely electron blocks incoming pairs

J Biol Chem. 2021 Jan-Jun:296:100294. doi: 10.1016/j.jbc.2021.100294. Epub 2021 Feb 12.

Abstract

Electron bifurcation exploits high energetic states to drive unfavorable single electron reactions and determining the overall mechanism governing these electron transfers represents an arduous task. Using extensive stopped-flow spectroscopy and kinetic simulations, Sucharitakul et al. now explore the bifurcation mechanism of the electron transfer flavoprotein EtfAB from the anaerobic gut bacterium Acidaminococcus fermentans. Strikingly, they illustrated that catalysis is orchestrated by a negatively charged radical, α-FAD, that inhibits further reductions and features an atypical inverted kinetic isotope effect. These results provide additional insight behind electron transfers that are prevalent within multienzyme governed reactions.

Keywords: electron bifurcation; enzyme mechanism; flavin; flavoprotein.

MeSH terms

  • Acidaminococcus / metabolism
  • Bacterial Proteins / metabolism
  • Catalysis
  • Electron Transport*
  • Electrons
  • Energy Metabolism
  • Flavin-Adenine Dinucleotide / metabolism
  • Kinetics
  • Oxidation-Reduction

Substances

  • Bacterial Proteins
  • Flavin-Adenine Dinucleotide

Supplementary concepts

  • Acidaminococcus fermentans