Spectral deconvolution of redox species in the crotonyl-CoA-dependent NADH:ferredoxin oxidoreductase from Megasphaera elsdenii. A flavin-dependent bifurcating enzyme.

Wayne Vigil, Dimitri Niks, Sophie Franz-Badur, Nilanjan Chowdhury, Wolfgang Buckel, Russ Hille

Archives of biochemistry and biophysics 2021 Apr 15

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We have undertaken a spectral deconvolution of the three FADs of EtfAB/bcd to the spectral changes seen in the course of reduction, including the spectrally distinct anionic and neutral semiquinone states of electron-transferring and bcd flavins. We also demonstrate that, unlike similar systems, no charge-transfer complex is observed on titration of the reduced M. elsdenii EtfAB with NAD+. Finally, and significantly, we find that removal of the et FAD from EtfAB results in an uncrossing of the half-potentials of the bifurcating FAD that remains in the protein, as reflected in the accumulation of substantial FAD•- in the course of reductive titrations of the depleted EtfAB with sodium dithionite. Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.

Citation

Wayne Vigil, Dimitri Niks, Sophie Franz-Badur, Nilanjan Chowdhury, Wolfgang Buckel, Russ Hille. Spectral deconvolution of redox species in the crotonyl-CoA-dependent NADH:ferredoxin oxidoreductase from Megasphaera elsdenii. A flavin-dependent bifurcating enzyme. Archives of biochemistry and biophysics. 2021 Apr 15;701:108793