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.

A lonely electron blocks incoming pairs

Nicoll C. R.
Writing – Review & Editing
;
Mattevi A.
Conceptualization
2021-01-01

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.
2021
Biochemistry & Biophysics
Comitato scientifico
Inglese
Internazionale
STAMPA
296
100294
100295
2
electron bifurcation; enzyme mechanism; flavin; flavoprotein; Acidaminococcus; Bacterial Proteins; Catalysis; Electrons; Energy Metabolism; Flavin-Adenine Dinucleotide; Kinetics; Oxidation-Reduction; Electron Transport
https://www.jbc.org/article/S0021-9258(21)00062-4/fulltext
no
3
info:eu-repo/semantics/article
262
Massari, M.; Nicoll, C. R.; Mattevi, A.
1 Contributo su Rivista::1.1 Articolo in rivista
none
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11571/1448288
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