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Published on: July 20, 2022
Electron transfer between the QmoABC membrane complex and adenosine 5'-phosphosulfate reductase
Américo G Duarte1, André A Santos1, Inês A C Pereira1
1Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, Estação Agronómica Nacional, 2780-157, Oeiras, Portugal.
Researchers show direct electron transfer between the QmoABC complex and adenosine 5'-phosphosulfate reductase (AprAB) in sulfate reduction. This confirms QmoABC
Area of Science:
- Biochemistry
- Microbiology
- Electrochemistry
Background:
- The dissimilatory adenosine 5 -phosphosulfate reductase (AprAB) is crucial for sulfate reduction.
- The QmoABC membrane complex is the proposed electron donor for AprAB.
- Direct electron transfer between QmoABC and AprAB has not been previously demonstrated.
Purpose of the Study:
- To demonstrate direct electron transfer between the QmoABC complex and AprAB.
- To elucidate the role of QmoABC in delivering electrons to AprAB for sulfate reduction.
Main Methods:
- Cyclic voltammetry using a QmoABC-modified electrode with AprAB.
- Catalytic experiments with immobilized QmoABC, AprAB, and adenosine 5 -phosphosulfate (APS).
- Substrate dependence studies with varying electrode preparations.
Main Results:
- Direct electron transfer between Desulfovibrio desulfuricans QmoABC and AprAB was observed.
- AprAB's FAD redox behavior was identified through electrochemical signatures.
- Catalytic current, dependent on QmoABC, indicated efficient electron delivery for APS reduction.
Conclusions:
- The QmoABC complex directly transfers electrons to AprAB.
- QmoABC is essential for sustaining catalysis in the sulfate reduction pathway.
- This study confirms the role of QmoABC in electron transfer to AprAB.
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