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Published on: March 18, 2012
Structural and functional insights into sulfide:quinone oxidoreductase
José A Brito1, Filipa L Sousa, Meike Stelter
1Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República EAN, 2780-157 Oeiras, Portugal.
Researchers characterized the first X-ray structure of sulfide:quinone oxidoreductase (SQR) from Acidianus ambivalens. The structure reveals a unique sulfur chain, offering insights into sulfide oxidation and bioenergetics in this archaeon.
Area of Science:
- Biochemistry
- Structural Biology
- Archaea Biology
Background:
- Sulfide:quinone oxidoreductase (SQR) enzymes are crucial in microbial bioenergetics.
- The hyperthermoacidophilic archaeon Acidianus ambivalens utilizes sulfur-dependent pathways for energy production.
Purpose of the Study:
- To determine the first X-ray structure of an SQR enzyme.
- To functionally and structurally characterize SQR from Acidianus ambivalens.
- To elucidate the role of SQR in the bioenergetics of A. ambivalens.
Main Methods:
- Isolation of sulfide:quinone oxidoreductase (SQR) from archaeal membranes.
- X-ray crystallography to determine enzyme structure at 2.6 A resolution.
- Functional characterization of enzyme redox active sites.
Main Results:
- The first X-ray structure of an SQR was determined for Acidianus ambivalens.
- The enzyme possesses two redox active sites: covalently bound FAD and cysteine residues.
- A novel chain of three sulfur atoms bridging cysteine residues was observed.
Conclusions:
- The observed sulfur chain may play a role in the catalytic mechanism of sulfide oxidation.
- SQR is linked to oxygen reduction in the sulfur-dependent bioenergetics of A. ambivalens.
- This study provides structural insights into SQR function in extremophilic archaea.
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