Sophia Paul
@sophia-pa.bsky.social
📤 33
📥 25
📝 3
reposted by
Sophia Paul
Gyana Prakash Mahapatra
8 days ago
Excited to share our new preprint! How does the cyanobacterial hydrogenase HoxEFUYH drive photosynthetic H₂ production? Using
#cryoEM
, biochemistry, FTIR and EPR spectroscopy, we reveal its molecular mechanism, including the basis of electron bifurcation/confurcation.
www.biorxiv.org/content/10.6...
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Electron confurcation drives photosynthetic H2 production in cyanobacteria
Cyanobacteria are major contributors to global photosynthesis and are intensively studied for sustainable green H2 production. Central to this process is the bidirectional [NiFe]-hydrogenase HoxEFUYH,...
https://www.biorxiv.org/content/10.64898/2026.06.25.734504v1
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reposted by
Sophia Paul
Sven T. Stripp
2 months ago
Now online with
@natcomms.nature.com
🤩
doi.org/10.1038/s414...
add a skeleton here at some point
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reposted by
Sophia Paul
Anuj
3 months ago
How do “LEGO-like” electron-bifurcating modules combine to drive degradation in BTEX-contaminated ecosystems? Check out our latest preprint, where we use cryo-EM and cryo-ET to reveal how the 1 MDa BCRII complex powers extremely endergonic aromatic ring reduction.
www.biorxiv.org/content/10.6...
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https://www.biorxiv.org/content/10.64898/2026.04.10.717634v1
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reposted by
Sophia Paul
Tomas Pascoa
3 months ago
1/ Excited to share our preprint! 🥳 Degradation of aromatic compounds, including BTEX pollutants, requires highly endergonic aromatic ring reduction. Using
#cryoEM
and in situ
#cryoET
, we show how BCRII couples electron bifurcation modules in one giant redox machine
www.biorxiv.org/content/10.6...
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Congratulations to
@rnfr2d2.bsky.social
for winning the GBM
#PhDAward
! Very well deserved- You put in so much hard work to get here. So happy and proud to see you succeed
add a skeleton here at some point
3 months ago
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reposted by
Sophia Paul
Johannes Rebelein
9 months ago
Our latest work on the nitrogenase-like methylthio-alkane reductase, which specifically reduces reduces carbon-sulfide bonds is now out
@natcatal.nature.com
:
doi.org/10.1038/s419...
. We find for the first time large
#nitrogenase
metalloclusters (P- and L-cluster) outside nitrogenases.
add a skeleton here at some point
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reposted by
Sophia Paul
9 months ago
Have you ever looked at the night sky and wondered if there’s a chlorophyll f in the reaction centre of Photosystem I from far-red light adapted cyanobacteria? 🦠 Well, we did (don’t judge) and the work that followed is now out as a First Release in
@science.org
www.science.org/doi/10.1126/...
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Locating the missing chlorophylls f in far-red photosystem I
The discovery of chlorophyll f-containing photosystems, with their long-wavelength photochemistry, represented a distinct, low-energy paradigm for oxygenic photosynthesis. Structural studies on chloro...
https://www.science.org/doi/10.1126/science.ado6830
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reposted by
Sophia Paul
Schuller Jan
about 1 year ago
Proud to present the lab's latest work. The full structure of the sodium translocating methyltransferase (Mtr) bound to a small oxygen-responsive small protein MtrI. Work by Tristan and together with
@schmitzstreitslab.bsky.social
.
www.biorxiv.org/content/10.1101/2025.06.02.657420v1
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reposted by
Sophia Paul
Schuller Jan
about 1 year ago
One of the largest open questions in anaerobic metabolism solved. The best work of my lab yet, performed by the incredible hard working, talented and motivated coworkers:
@fidelormz.bsky.social
,
@sophia-pa.bsky.social
and
@rnfr2d2.bsky.social
. I am a proud PI today!
www.nature.com/articles/s41...
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Structure of the ATP-driven methyl-coenzyme M reductase activation complex - Nature
The structure and function of the MCR activation complex from Methanococcus maripaludis were revealed, demonstrating its ATP-dependent ability to activate MCR and form methane while uncovering a uniqu...
https://www.nature.com/articles/s41586-025-08890-7
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I am incredibly excited to share my first-ever research paper that has just been published in Nature! I thank my fellow co-first authors
@fidelormz.bsky.social
and
@rnfr2d2.bsky.social
and
@schullerjm.bsky.social
for leading this project.
www.nature.com/articles/s41...
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Structure of the ATP-driven methyl-coenzyme M reductase activation complex - Nature
The structure and function of the MCR activation complex from Methanococcus maripaludis were revealed, demonstrating its ATP-dependent ability to activate MCR and form methane while uncovering a uniqu...
https://www.nature.com/articles/s41586-025-08890-7
about 1 year ago
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reposted by
Sophia Paul
Anuj
about 1 year ago
For decades, how methanogenic archaea activate the MCR complex to produce methane remained a mystery. Today in Nature, we report the high-resolution cryo-EM structure of the MCR activation complex!
www.nature.com/articles/s41...
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Structure of the ATP-driven methyl-coenzyme M reductase activation complex - Nature
The structure and function of the MCR activation complex from Methanococcus maripaludis were revealed, demonstrating its ATP-dependent ability to activate MCR and form methane while uncovering a uniqu...
https://www.nature.com/articles/s41586-025-08890-7
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