the membrane qmoabc complex interacts directly with the dissimilatory adenosine 5´-phosphosulfate reductase in sulfate reducing bacteria

Clicks: 394
ID: 201529
2012
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Star

Ranked #12 of 875 articles by views in journal of magnetic resonance (san diego, calif : 1997)

Most read Least read

Bar heights use a square-root scale. Only the 120 most-read articles are drawn; the journal has 875 in total.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Abstract
The adenosine 5’-phosphosulfate reductase (AprAB) is the enzyme responsible for the reduction of adenosine 5’-phosphosulfate (APS) to sulfite in the biological process of dissimilatory sulfate reduction, which is carried out by a ubiquitous group of sulfate reducing prokaryotes. The electron donor for AprAB has not been clearly identified, but was proposed to be the QmoABC membrane complex, since an aprBA-qmoABC gene cluster is found in many sulfate-reducing and sulfur-oxidising bacteria. The QmoABC complex is essential for sulfate reduction, but electron transfer between QmoABC and AprAB has not been reported. In this work we provide the first direct evidence that QmoABC and AprAB interact in Desulfovibrio spp., using co-immunoprecipitation, cross-linking Far-Western blot, tag-affinity purification and surface plasmon resonance studies. This showed that the QmoABC-AprAB complex has a strong steady-state affinity (KD = 90 ± 3 nM), but has a transient character due to a fast dissociation rate. Far-Western blot identified QmoA as the Qmo subunit most involved in the interaction. Nevertheless, electron transfer from menaquinol analogues to APS through anaerobically purified QmoABC and AprAB could not be detected. We propose that this reaction requires the involvement of a third partner to allow electron flow driven by a reverse electron bifurcation process i.e. electron confurcation. This process is deemed essential to allow coupling of APS reduction to chemiosmotic energy conservation.
Reference Key
ramos2012frontiersthe Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Ana Raquel Ramos;Kimberly L. Keller;Kimberly L. Keller;Judy D Wall;Judy D Wall;Inês A. Cardoso Pereira
Journal journal of magnetic resonance (san diego, calif : 1997)
Year 2012
DOI
10.3389/fmicb.2012.00137
URL
Keywords

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

No comments yet. Be the first to comment on this article.