Ribbe Hu Labs

Ribbe Hu Labs

@ribbehulab.bsky.social

Metalloprotein assembly and catalysis; bioinorganic chemistry; structural biology; spectroscopy; microbiology

124 followers186 following34 posts

Ribbe Hu Labs
@ribbehulab.bsky.social

Some exciting papers have recently been added to the collection, with many more to come soon! doi.org/10.1002/cbic... doi.org/10.1002/cbic... doi.org/10.1002/cbic...

doi.orgNickel‐Substituted Rubredoxin Undergoes Demetallation Upon Reaction With Nitric Oxide and NitroxylRubredoxin is a thermally stable thiolate iron-bound protein that can be prepared as a nickel-substituted one. This nickel protein showed sensitivity to reaction with NO and HNO donors, causing its d...
Ribbe Hu Labs
@ribbehulab.bsky.social

We are grateful for the opportunity to contribute and to showcase both our work and the exciting advances emerging from the biological inorganic chemistry and structural biology communities.

Ribbe Hu Labs
@ribbehulab.bsky.social

Congrats, Joe! We’re very proud of you!

Johannes Rebelein@rebeleinlab.bsky.social

A childhood dream has come true – I was appointed Full Professor for Sustainable Biotechnology at the University of Düsseldorf @hhu.de : tinyurl.com/f43s74hp and as Director of the Institute for Molecular Enzyme Technology (IMET, www.iet.uni-duesseldorf.de/en/) at FZ Jülich @fz-juelich.de .

tinyurl.comMathematisch-Naturwissenschaftliche FakultätHeute ernannte Rektorin Prof. Dr. Anja Steinbeck den Biotechnologen Dr. Johannes Rebelein zum W3-Professor für Nachhaltige Biotechnologie. Rebelein wird damit auch Direktor des Instituts für Molekular...
Ribbe Hu Labs
@ribbehulab.bsky.social

Many thanks to Nature Catalysis and to Prof. Zhang and his colleagues for featuring our manuscript in a News & Views article - this is truly appreciated! @ribbehulab.bsky.social @ucibiosci.bsky.social @natcatal.nature.com

Nature Catalysis@natcatal.nature.com

New online! Gating the nitrogenase cofactor

dlvr.itGating the nitrogenase cofactorNature Catalysis, Published online: 26 March 2026; doi:10.1038/s41929-026-01498-8Biological nitrogen fixation is vital for sustainable agriculture, yet nitrogenase engineering is hindered by limited insight into their essential metallocluster cofactor assembly and transfer. Here, by capturing the nitrogenase biosynthetic component NifEN in multiple structural states, a tunnel-and-switch mechanism that coordinates receipt, maturation and delivery of the FeMo-cofactor precursor is revealed.

Ribbe Hu Labs reposted

UC Irvine Charlie Dunlop School of Biological Sciences
@ucibiosci.bsky.social

Congratulations to Assistant Professor Benjamin Morehouse on receiving a $150,000 Michelson Prize from the Michelson Medical Research Foundation 👏 The award supports his innovative immunology research at the Dunlop School. Read more: bit.ly/4bmmJRK

bit.lyBenjamin Morehouse’s Ancient Immunity Breakthrough Targets Antimicrobial ResistanceDr. Benjamin Morehouse uncovers ancient immune protein SIRa1, a breakthrough that could combat antimicrobial resistance by targeting host immunity instead of pathogens.

Ribbe Hu Labs reposted

Johannes Rebelein
@rebeleinlab.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.

doi.orgMethylthio-alkane reductases use nitrogenase metalloclusters for carbon–sulfur bond cleavage - Nature CatalysisMethylthio-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...
Max Planck Institute for Terrestrial Microbiology@mpimicrobiomarburg.bsky.social

Microbial 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.

s.gwdg.deMicrobial Strategy for Renewable PlasticA bacterial enzyme could make it possible to produce the plastic building block ethylene without the emission of CO₂. Researchers at the Max Planck Institute for Terrestrial Microbiology, led by Dr Johannes Rebelein, have now investigated the enzyme's structure and function in vitro.These findings lay the groundwork for more sustainable biotechnological ethylene production and improve our understanding of early biochemical processes.
Ribbe Hu Labs
@ribbehulab.bsky.social

Our second paper that came online within a week 😊! Thanks everyone for their hard work! @ribbehulab.bsky.social @ucibiosci.bsky.social Heterologous synthesis of a simplified nitrogenase analog in Escherichia coli | Science Advances www.science.org/doi/10.1126/...

science.orgHeterologous synthesis of a simplified nitrogenase analog in Escherichia coliHeterologous synthesis of a nitrogenase analog (NifH/NifEN) in E. coli enables N2 reduction and incorporation of N into biomass.

Ribbe Hu Labs reposted

Edwin Antony
@professorantony.bsky.social

Our story detailing how asymmetry in nitrogenase-like proteins regulate electron transfer reactions is finally out! rdcu.be/ejaeK Congratulations to postdoc @rajnandani.bsky.social and fantastic collaborators. Thanks to funding from the Department of Energy and the NIH.

rdcu.beCryo-EM captures the coordination of asymmetric electron transfer through a di-copper site in DPORNature Communications - CryoEM snapshots of the nitrogenase-like DPOR protein complex captured during turnover reveal that asymmetric conformational changes, substrate recognition, and an interplay...
Ribbe Hu Labs
@ribbehulab.bsky.social

Excited to share our latest work highlighting the crucial role of belt-sulfur mobilization in nitrogenase catalysis. A big thank you to everyone who contributed to this effort! @cp-chemcatalysis.bsky.social @ucibiosci.bsky.social www.cell.com/chem-catalys...

cell.comBelt-sulfur mobilization as a crucial mechanistic feature shared between the vanadium and molybdenum nitrogenasesNitrogenase catalyzes the reduction of N2 to NH3 at its active site cofactor. Catalysis by the homologous V- and Mo-nitrogenases involves the same dynamic belt-S mobilization that occurs asymmetricall...

Ribbe Hu Labs reposted

David Barondeau
@barondeau.bsky.social

pubs.acs.org/doi/10.1021/...

pubs.acs.orgFrataxin Traps Low Abundance Quaternary Structure to Stimulate Human Fe–S Cluster BiosynthesisIron–sulfur clusters are essential protein cofactors synthesized in human mitochondria by an NFS1-ISD11-ACP-ISCU2-FXN assembly complex. Surprisingly, researchers have discovered three distinct quaternary structures for cysteine desulfurase subcomplexes, which display similar interactions between NFS1-ISD11-ACP protomeric units but dramatically different dimeric interfaces between the protomers. Although the role of these different architectures is unclear, possible functions include regulating activity and promoting the biosynthesis of distinct sulfur-containing biomolecules. Here, crystallography, native ion-mobility mass spectrometry, and chromatography methods reveal the Fe–S assembly subcomplex exists as an equilibrium mixture of these different quaternary structures. Isotope labeling and native mass spectrometry experiments show that the NFS1-ISD11-ACP complexes disassemble into protomers, which can then undergo exchange reactions and dimerize to reform native complexes. Single crystals isolated in distinct architectures have the same activity profile and activation by the Friedreich’s ataxia (FRDA) protein frataxin (FXN) when rinsed and dissolved in assay buffer. These results suggest FXN functions as a “molecular lock” and shifts the equilibrium toward one of the architectures to stimulate the cysteine desulfurase activity and promote iron–sulfur cluster biosynthesis. An NFS1-designed variant similarly shifts the equilibrium and partially replaces FXN in activating the complex. We propose that eukaryotic cysteine desulfurases are unusual members of the morpheein class of enzymes that control their activity through their oligomeric state. Overall, the findings support architectural switching as a regulatory mechanism linked to FXN activation of the human Fe–S cluster biosynthetic complex and provide new opportunities for therapeutic interventions of the fatal neurodegenerative disease FRDA.

Ribbe Hu Labs reposted

Shane Gonen
@gonenshane.bsky.social

Our #CryoEM study on the binding of a Tarantula toxin to a full-length human voltage-gated sodium channel has been published. Very proud of the awesome people in my lab 🥳🥂 www.nature.com/articles/s41...

nature.comStructural basis of inhibition of human NaV1.8 by the tarantula venom peptide Protoxin-I - Nature CommunicationsAnimal toxins can modulate action potentials and are important leads for therapeutics. Here, the authors use cryo-EM to show the interaction of the tarantula venom peptide Protoxin-I with a human volt...

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