Huge discovery from Marburg: Prof. Schuller (@synmikro.bsky.social),doctoral stud. @sophia-pa.bsky.social+colleagues have resolved1️⃣of the🧬🔬largest enzymes. Published in Nature, the study shows how methanogenic archaea generate energy under extreme conditions, offering🆕insights into the🌎carbon cycle.
Excited to share my paper! 🥳 Today in #Nature we reveal an 8 MDa Hdr electron bifurcating super-assembly in class I methanogens that couples the first and last steps of hydrogenotrophic methanogenesis. A lineage-specific adaptation to anaerobic niches. www.nature.com/articles/s41...
1/ Happy to share our preprint! The Mtr complex catalyses the second-to-last step of the methanogenesis and is an essential bioenergetic machine in most methanogenic archaea. Anaerobic cryo-EM of Mtr reveals a nitrogenase-like metallocluster bound at its active site! www.biorxiv.org/content/10.6...
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...
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,...
biorxiv.org
Now online with @natcomms.nature.com 🤩 doi.org/10.1038/s414...
Sven T. Stripp@stripplab.bsky.social · 6mo agoCarbonic anhydrase catalyses the interconversion of CO2 and HCO3- and helps increasing the net-CO2 concentration inside cells. Why? CO2-reducing enzymes like RuBisCO are notoriously slow and ineffective. However, import of HCO3- is typically coupled to ATP consumption...
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...
biorxiv.org
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...
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
GBM (Gesellschaft für Biochemie und Molekularbiologie)@gbmev.bsky.social · 6mo agoThe GBM #PhDAward was presented to Anuj Kumar for his PhD thesis on the „Structural basis of CO2 fixation and energy conservation in acetogens“ Congratulations, Anuj! #MK2026 @unimarburg.bsky.social
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.
Methylthio-alkane reductases use nitrogenase metalloclusters for carbon–sulfur bond cleavage - Nature Catalysis
Methylthio-alkane reductases are recently discovered enzymes that can produce methanethiol and small hydrocarbons from methylated sulfur compounds. Now the cryo-EM structure of a methylthio-alkane red...
doi.org
Max Planck Institute for Terrestrial Microbiology@mpimicrobiomarburg.bsky.social · 11mo agoMicrobial enzymes hold the key to greener plastics! Rhodospirillum rubrum can produce ethylene without releasing CO₂. A team @rebeleinlab.bsky.social purified the enzyme and solved its structure, an important step towards #SustainableChemistry.
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/...
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...
science.org
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
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...
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...
nature.com
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...
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...
nature.com
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...
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...
nature.com