James Birrell
@jamesbirrell.bsky.social
49 followers 33 following 24 posts
Lecturer at University of Essex. Interested in metalloenzyme structure and spectroscopy.
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Reposted by James Birrell
ich2026.bsky.social
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).
jamesbirrell.bsky.social
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…
jamesbirrell.bsky.social
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?
jamesbirrell.bsky.social
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?
Reposted by James Birrell
chemhurst.bsky.social
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...
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
Reposted by James Birrell
stripplab.bsky.social
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...
Reposted by James Birrell
stripplab.bsky.social
We have positions for pCNF SDM of CpI in a recent grant application... Very encouraging to see Kylie's data!
jamesbirrell.bsky.social
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?
Reposted by James Birrell
stripplab.bsky.social
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...
Reposted by James Birrell
stripplab.bsky.social
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.
Reposted by James Birrell
stripplab.bsky.social
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‼️
Reposted by James Birrell
stripplab.bsky.social
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...
Reposted by James Birrell
stripplab.bsky.social
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... 🧵
stripplab.bsky.social
First off, let me highlight recent work from Vincent et al.: the authors modified plant ferredoxin with cyanophenylalanine and succeeded in measuring FeS-redox-dependent nitrile band shifts in the IR spectra.
Reposted by James Birrell
bioinorgchemuw.bsky.social
"redox-dependent nitrile band shifts" 🤩
Reposted by James Birrell
sandykilla.bsky.social
Lovely stuff Zehui et al.!
Reposted by James Birrell
stripplab.bsky.social
Applying this genetic approach to [FeFe]-hydrogenase, the nitrile band allows probing the FeS cluster redox states AND the H-cluster. This will be a powerful tool in other FeS proteins as well!
doi.org/10.1002/cbic...
Reposted by James Birrell
stripplab.bsky.social
First off, let me highlight recent work from Vincent et al.: the authors modified plant ferredoxin with cyanophenylalanine and succeeded in measuring FeS-redox-dependent nitrile band shifts in the IR spectra.
Reposted by James Birrell
stripplab.bsky.social
Who's ready to talk about ferredoxin?
jamesbirrell.bsky.social
3 does EB. And EB is my thing now 🤷‍♂️
Reposted by James Birrell
rmlab.bsky.social
It is a real pleasure to collaborate with you guys! 😊
jamesbirrell.bsky.social
Thanks to Marius Horch and the rest of his awesome team, especially Cornelius Bernitzky and Yvonne Rippers. I also want to thank @rmlab.bsky.social for help with preparation of beautiful [FeFe] hydrogenase samples.
jamesbirrell.bsky.social
I’d argue that in most cases it is inferred. Mutagenesis studies are quite clear for some states, and for the COs isotope exchange helps. But the terminal COs show strong coupling. I think 2DIR is pretty useful at being able to tackle much of this without needing to manipulate the system.