International Conference on Hydrogenase and Other Redox Metalloenzymes 2026 | School of Chemistry | University of Leicester Web page for the International Conference on Hydrogenase and Other Redox Metalloenzymes. The conference will be held in Leicester in Summer 2026.

Registration is now open! The 14th edition of the International Conference on Hydrogenase and Other Redox Metalloenzymes (ICH2026)e at the University of Leicester 26 to 30 July 2026.
@jamesbirrell.bsky.social @rmlab.bsky.social @ir-paash.bsky.social

le.ac.uk/chemistry/re...

A cartoon image of the Leicester skyline, showing buildings such as the clock tower and National Space Centre. Across the top of this are the words ICH 2026, and Register Now!!!

The International Conference on Hydrogenase and Other Redox Metalloenzymes takes place @uniofleicester.bsky.social in the UK, 26-30 July 2026. A reminder that there is still time to submit an abstract and register for this exciting conference!
le.ac.uk/chemistry/re...

Congratulations Patri, Simone and all the team! Great paper!

Thank you to my amazing collaborators and the PhD student doing the work, Sam!
Please have a read, it is a really interesting paper!

An elegant engineering strategy to perform step-wise truncations of the iron-sulfur cluster domains in semi-synthetic [FeFe] hydrogenases to investigate in detail the influence on the catalytic properties of the enzyme and the inhibitors binding!

Engineering the Electron Relay in [FeFe]-Hydrogenase Enhances Electrocatalytic H2 Evolution H2 is an ideal energy vector, but catalysts for its clean production from water are inefficient or expensive. [FeFe]-hydrogenases are the most active H2-converting catalysts in nature, using a unique ...

I couldn't be happier to see this nice piece of work out! It is like my baby project, which I dedicated a lot of time and effort!

lnkd.in/eKpyxrM5http...

Engineering the Electron Relay in [FeFe]-Hydrogenase Enhances Electrocatalytic H2 Evolution H2 is an ideal energy vector, but catalysts for its clean production from water are inefficient or expensive. [FeFe]-hydrogenases are the most active H2-converting catalysts in nature, using a unique ...

Congratulations @rmlab.bsky.social ! pubs.acs.org/doi/10.1021/...

Engineering the Electron Relay in [FeFe]-Hydrogenase Enhances Electrocatalytic H2 Evolution H2 is an ideal energy vector, but catalysts for its clean production from water are inefficient or expensive. [FeFe]-hydrogenases are the most active H2-converting catalysts in nature, using a unique ...

Vincent, Morra, and Rodríguez-Maciá demonstrate that truncating the electron transfer domain of [FeFe]-hydrogenase does *not* diminish their catalytic efficiency (via ACS Catalysis).
doi.org/10.1021/acsc...

The cytochrome P450 decarboxylase from Staphylococcus aureus can produce a diene from a C18 monounsaturated fatty acid: A spectroscopic, structural and kinetic characterisation Certain members of the bacterial cytochrome P450 152 family (CYP152) are peroxygenases that catalyse the decarboxylation of fatty acids into terminal …

Our first foray into the P450 world. Thanks to @bellp450enzyme.bsky.social for sharpening our GC-MS skill set @jamesbirrell.bsky.social for the microwaves😃 and Lewis for persevering 🧪

1️⃣ 𝗠𝗜𝗕𝗧𝗣-𝗕𝗕𝗦𝗥𝗖 - 𝟮𝟳𝘁𝗵 𝗡𝗼𝘃𝗲𝗺𝗯𝗲𝗿 𝟮𝟬𝟮𝟱 𝗱𝗲𝗮𝗱𝗹𝗶𝗻𝗲:
warwick.ac.uk/fac/cross_fa...

2️⃣ 𝗖𝗘𝗡𝗧𝗔-𝗡𝗘𝗥𝗖 - 𝟳𝘁𝗵 𝗝𝗮𝗻𝘂𝗮𝗿𝘆 𝟮𝟬𝟮𝟲 𝗱𝗲𝗮𝗱𝗹𝗶𝗻𝗲:
centa.ac.uk/studentship/...

Any questions or more information? Please email me, happy to help!

#metalloenzymes #biohybridcatalysts #sustainablechemistry #greenchemistry

Are you excited about #metalloenzymes and #biohybridcatalysts? Are you interested in investigating new approaches for #sustainable and #greenchemistry?

If so, I have 𝘁𝘄𝗼 𝗣𝗵𝗱 𝗽𝗼𝘀𝗶𝘁𝗶𝗼𝗻𝘀 to join my group in 📅 Sept 2026 under the schemes.

👇+Info👇

We have a 𝗣𝗼𝘀𝘁𝗱𝗼𝗰𝘁𝗼𝗿𝗮𝗹 𝗥𝗲𝘀𝗲𝗮𝗿𝗰𝗵 𝗔𝘀𝘀𝗼𝗰𝗶𝗮𝘁𝗲 (𝗣𝗗𝗥𝗔) position for a project in collaboration with my colleagues Phil Ash & James Pickering, via the AMBER Postdoctoral Programme funded by MSCActions.

Come and join us at @uniofleicester!

👇+info👇

Research opportunities | Institute for Structural and Chemical Biology | University of Leicester Postdoc opportunities at the Leicester Institute for Structural and Chemical Biology

Information about the project here: le.ac.uk/research/ins...

Information about the position and how to apply:
jobs.le.ac.uk/vacancies/11...

Deadline 7 Dec 2025!

For any enquires please send an email!

Delightful combination of spectroscopies (electronic, microwave) and protein crystallography in @jarworrall.bsky.social's new paper on cytochrome P450 decarboxylase from Staphylococcus aureus 🤩
doi.org/10.1016/j.ji...

We are delighted to confirm that the and Other Redox Metalloenzymes will take place from 26-30 July 2026 at the University of Leicester, UK.

Details of the conference, including regularly updated confirmed speakers, are available on our website (link in bio).

Ok, thanks. Solution potential of the activity assay ought to be pretty negative though, right? 100 mM sodium dithionite at pH 6.8. I’d guess ca. -600 mV vs SHE compared with an eq potential of H2 of ca. -400. So you could have 200 mV of overpotential…

I’m also interested in a coordination chemist’s view of the 7 coordinate Fe intermediate. Is there likely to be a low barrier to its formation?

Hi Sven. Interesting paper. You said “no significant extra driving force”…You mean no significant overpotential? What is the overpotential and how did you measure it? Also, is it right that the turnover frequency is less than 1 per second? Any ideas how to make this better?

Two-dimensional infrared spectroscopy as a tool to reveal the vibrational and molecular structure of [FeFe] hydrogenases [FeFe] hydrogenases are Nature's most efficient catalysts for the cleavage and evolution of molecular hydrogen. Despite decades of research, key aspects of the catalytic cycle and the underlying geome...

Congrats @rmlab.bsky.social and co-authors on "Two-dimensional infrared spectroscopy as a tool to reveal the vibrational and molecular structure of [FeFe] hydrogenases" in Chemical Science pubs.rsc.org/en/content/a...

Promotional poster for an event from the Royal Society of Chemistry titled "RSC Desktop Seminar: Chemistry of Inorganic Clusters" on Tuesday May 27 at 2pm EDT and 7pm BST

Join us next Tuesday May 27 for a Desktop Seminar on the Chemistry of Inorganic Clusters! Featuring talks and live Q&A from Stephen Ragsdale (University of Michigan) and Patrick Holland (Yale University), this is one you don't want to miss!

Register and find more details rsc.zoom.us/webinar/regi...

We probed both directions, and it really seems to be the F-domain that modulates the on/off dynamics. We didn't investigate DdH tho...

We have positions for pCNF SDM of CpI in a recent grant application... Very encouraging to see Kylie's data!

Presumably, only reduced ferredoxin binds to *oxidised* hydrogenase (during proton reduction)? Meanwhile oxidised ferredoxin should bind to reduced hydrogenase (during hydrogen oxidation)? I guess I need to read the paper…nice work! Any plans to engineer pCNF into CpI?

We believe that these protein-protein-interactions propell fast & repeated one-electron-transfer reactions, driving multi-electron redox catalysis with a one-electron mediator. In hydrogenase, and other oxidoreductases as well.
Find all the details in the paper:
pubs.rsc.org/en/content/a...

Uli's brilliant microscale thermophoresis experiments show that *only* reduced ferredoxin binds to hydrogenase, which facilitates assigning the secondary structural changes to redox changes and a shift from an "attractive" to a "repulsive" configuration.

Infrared difference spectra reveal that the reduction of ferredoxin is accompanied with larger secondary structural changes - clearly associated with the "F-domain" of [FeFe]-hydrogenase, as reference experiments with "minimal hydrogenase" CrHydA1 lack this spectral feature.
A surprise‼️

Interestingly, in the ferredoxin from C. pasteurianum, reduction alone does *not* affect the nitrile frequency. Only in complex with [FeFe]-hydrogenase CpI, redox changes affect the artificial amino acid...

Ross @milton-group.bsky.social came up with a very similar idea: how about introducing cyanophenylalanine to a (bacterial) ferredoxin that binds two [4Fe-4S] clusters?
One might learn where the electron resides as most ferredoxins are considered one-electron redox mediators... 🧵

"redox-dependent nitrile band shifts" 🤩

Lovely stuff Zehui et al.!