#NatureCatalysis
New in @NatureCatalysis: We tracked dilute oxygen vacancies at Cr/ZnO interfaces in real time, using operando time-resolved EDXAS coupled with transient kinetics and microcalorimetry.

rdcu.be/TfvmyafQ29na
September 25, 2026 at 12:28 PM
🧪Research Highlight: From pollutant to valuable chemical product – Two new #UniSysCat studies show how bacteria convert the greenhouse gas CO₂. The studies have recently been published in #NatureCatalysis.

@dobbek-lab.bsky.social & @humboldtuni.bsky.social & @tuberlin.bsky.social & @nature.com
August 7, 2025 at 10:57 AM
New in @NatureCatalysis: We tracked dilute oxygen vacancies at Cr/ZnO interfaces in real time, using operando time-resolved EDXAS coupled with transient kinetics and microcalorimetry.

rdcu.be/TfvmyafQ29na
September 25, 2026 at 12:32 PM
New #NatureCatalysis paper offers novel tools for understanding how catalytic reactions operate in practice

The work is done by scientists from the @monicaperez.bsky.social group at @iciq.org & @bengurionuni.bsky.social

#BISTCommunity

👉 bist.eu/when-substra...
November 27, 2025 at 5:10 PM
🧪 New paper from the Dell’Amico group in #NatureCatalysis !

Meet PHOENIX 🐦‍🔥— a purely organic photocatalyst that can access a remarkably broad redox windows through sequential light absorption.

shorturl.at/TUt44

Congratulations to all the authors 🎉🎉
Bimodal multiphoton catalysis via structural regeneration - Nature Catalysis
Photocatalysts can generate radical species from substrates following light excitation. Here the authors report a two-photon bimodal catalysis approach in which the light-activated photocatalyst generates reactive intermediates at opposite redox scales, expanding the accessible redox window.
shorturl.at
August 19, 2026 at 9:17 AM
Are you interested in how #epistasis shapes the AMR evolution?

We showed that epistasis can be caused by independently modulating substrate binding and the chemical step ultimately changing the rate-limiting step in the catalytic cycle. @NatureCatalysis

Full read: rdcu.be/dzqjk
Epistasis arises from shifting the rate-limiting step during enzyme evolution of a β-lactamase
Nature Catalysis - The reasons for epistasis, wherein mutations interact non-additively, are often not fully understood. Now it is found that shifting the rate-limiting step from substrate binding...
rdcu.be
February 23, 2024 at 11:09 AM
Check out the latest news from the Jay Keasling lab, published in @NatureCatalysis: QB3-Berkeley researchers engineer biological assembly-line enzymes to create new, sustainable products.

Read the story from grad student Leah Keiser:

bit.ly/bio-assembly-l…
February 27, 2025 at 9:23 PM
Congratulations to our former MS student @SlammingMona and current PhD fellow Francesca De Giorgi for their @NatureCatalysis publication! https://www.nature.com/articles/s41929-019-0382-8
Deciphering the enzymatic mechanism of sugar ring contraction in UDP-apiose biosynthesis - Nature Catalysis
The sugar d-apiose is important in plant cell wall polysaccharides. Here the authors elucidate the complex, multistep biosynthetic pathway for its production using enzyme crystal structures and computational analysis.
www.nature.com
January 18, 2025 at 10:49 AM
#Papers @NatureCatalysis: In situ quantitative single-molecule study of dynamic catalytic processes in nanoconfinement https://www.nature.com/articles/s41929-017-0021-1
In situ quantitative single-molecule study of dynamic cat...
Nanoconfinement effects are crucial in any process that i...
www.nature.com
December 4, 2024 at 6:31 AM