ArticleThe Journal of biological chemistry2022
The reductive half-reaction of two bifurcating electron-transferring flavoproteins: Evidence for changes in flavin reduction potentials mediated by specific conformational changes.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Flavin redox tuning and ferredoxin-dependent kinetics in the electron-bifurcating EtfABCX complex from Thermotoga maritima.The Journal of biological chemistry · 2026Article
- A single hydrogen bond that tunes flavin redox reactivity and activates it for modification.Chemical science · 2024Article
- Correlating Conformational Equilibria with Catalysis in the Electron Bifurcating EtfABCX ofBiochemistry · 2024Article
- Rapid-reaction kinetics of the bifurcating NADThe Journal of biological chemistry · 2023Article
- Noncovalent interactions that tune the reactivities of the flavins in bifurcating electron transferring flavoprotein.The Journal of biological chemistry · 2023Article
- An Abundant and Diverse New Family of Electron Bifurcating Enzymes With a Non-canonical Catalytic Mechanism.Frontiers in microbiology · 2022Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The EtfAB components of two bifurcating flavoprotein systems, the crotonyl-CoA-dependent NADH:ferredoxin oxidoreductase from the bacterium Megasphaera elsdenii and the menaquinone-dependent NADH:ferredoxin oxidoreductase from the archaeon Pyrobaculum aerophilum, have been investigated. With both proteins, we find that removal of the electron-transferring flavin adenine dinucleotide (FAD) moiety from both proteins results in an uncrossing of the reduction potentials of the remaining bifurcating FAD; this significantly stabilizes the otherwise very unstable semiquinone state, which accumulates over the course of reductive titrations with sodium dithionite. Furthermore, reduction of both EtfABs depleted of their electron-transferring FAD by NADH was monophasic with a hyperbolic dependence of reaction rate on the concentration of NADH. On the other hand, NADH reduction of the replete proteins containing the electron-transferring FAD was multiphasic, consisting of a fast phase comparable to that seen with the depleted proteins followed by an intermediate phase that involves significant accumulation of FAD⋅
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