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Modulations of the reduction potentials of flavin‐based electron bifurcation complexes and semiquinone stabilities are key to control directional electron flow
Author(s) -
Sucharitakul Jeerus,
Buttra Supacha,
Wongnate Thanyaporn,
Chowdhury Nilanjan Pal,
Prongjit Methinee,
Buckel Wolfgang,
Chaiyen Pimchai
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15343
Subject(s) - semiquinone , flavoprotein , flavin group , electron transfer , chemistry , flavin adenine dinucleotide , ferredoxin , electron acceptor , photochemistry , stereochemistry , cofactor , quinone , biochemistry , enzyme
The flavin‐based electron bifurcation (FBEB) system from Acidaminococcus fermentans is composed of the electron transfer flavoprotein (EtfAB) and butyryl‐CoA dehydrogenase (Bcd). α‐FAD binds to domain II of the A‐subunit of EtfAB, β‐FAD to the B‐subunit of EtfAB and δ‐FAD to Bcd. NADH reduces β‐FAD to β‐FADH − , which bifurcates one electron to the high potential α‐FAD •− semiquinone followed by the other to the low potential ferredoxin (Fd). As deduced from crystal structures, upon interaction of EtfAB with Bcd, the formed α‐FADH − approaches δ‐FAD by rotation of domain II, yielding δ‐FAD •− . Repetition of this process leads to a second reduced ferredoxin (Fd − ) and δ‐FADH − , which reduces crotonyl‐CoA to butyryl‐CoA. In this study, we measured the redox properties of the components EtfAB, EtfaB (Etf without α‐FAD), Bcd, and Fd, as well as of the complexes EtfaB:Bcd, EtfAB:Bcd, EtfaB:Fd, and EftAB:Fd. In agreement with the structural studies, we have shown for the first time that the interaction of EtfAB with Bcd drastically decreases the midpoint reduction potential of α‐FAD to be within the same range of that of β‐FAD and to destabilize the semiquinone of α‐FAD. This finding clearly explains that these interactions facilitate the passing of electrons from β‐FADH − via α‐FAD •− to the final electron acceptor δ‐FAD •− on Bcd. The interactions modulate the semiquinone stability of δ‐FAD in an opposite way by having a greater semiquinone stability than in free Bcd.