James Birrell
@jamesbirrell.bsky.social
๐ค 49
๐ฅ 33
๐ 25
Lecturer at University of Essex. Interested in metalloenzyme structure and spectroscopy.
reposted by
James Birrell
Rodriguez-Macia Lab
2 months ago
Thank you to my amazing collaborators and the PhD student doing the work, Sam! Please have a read, it is a really interesting paper!
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James Birrell
Rodriguez-Macia Lab
2 months ago
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!
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James Birrell
Rodriguez-Macia Lab
2 months ago
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...
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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 ...
https://pubs.acs.org/doi/10.1021/acscatal.5c03665
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reposted by
James Birrell
Leicester Institute for Structural and Chemical Biology
2 months ago
Congratulations
@rmlab.bsky.social
!
pubs.acs.org/doi/10.1021/...
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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 ...
https://pubs.acs.org/doi/10.1021/acscatal.5c03665
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James Birrell
Sven T. Stripp
2 months ago
Vincent, Morra, and Rodrรญguez-Maciรก demonstrate that truncating the electron transfer domain of [FeFe]-hydrogenase does *not* diminish their catalytic efficiency (via ACS Catalysis).
doi.org/10.1021/acsc...
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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 ...
https://doi.org/10.1021/acscatal.5c03665
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James Birrell
Jonathan Worrall
3 months ago
Our first foray into the P450 world. Thanks to
@bellp450enzyme.bsky.social
for sharpening our GC-MS skill set
@jamesbirrell.bsky.social
for the microwaves๐ and Lewis for persevering ๐งช
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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 โฆ
https://www.sciencedirect.com/science/article/pii/S0162013425002983
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James Birrell
Rodriguez-Macia Lab
3 months ago
1๏ธโฃ ๐ ๐๐๐ง๐ฃ-๐๐๐ฆ๐ฅ๐ - ๐ฎ๐ณ๐๐ต ๐ก๐ผ๐๐ฒ๐บ๐ฏ๐ฒ๐ฟ ๐ฎ๐ฌ๐ฎ๐ฑ ๐ฑ๐ฒ๐ฎ๐ฑ๐น๐ถ๐ป๐ฒ:
warwick.ac.uk/fac/cross_fa...
2๏ธโฃ ๐๐๐ก๐ง๐-๐ก๐๐ฅ๐ - ๐ณ๐๐ต ๐๐ฎ๐ป๐๐ฎ๐ฟ๐ ๐ฎ๐ฌ๐ฎ๐ฒ ๐ฑ๐ฒ๐ฎ๐ฑ๐น๐ถ๐ป๐ฒ:
centa.ac.uk/studentship/...
Any questions or more information? Please email me, happy to help!
#metalloenzymes
#biohybridcatalysts
#sustainablechemistry
#greenchemistry
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reposted by
James Birrell
Rodriguez-Macia Lab
3 months ago
Are you excited about
#metalloenzymes
and
#biohybridcatalysts
? Are you interested in investigating new approaches for
#sustainable
and
#greenchemistry
? If so, I have ๐๐๐ผ ๐ฃ๐ต๐ฑ ๐ฝ๐ผ๐๐ถ๐๐ถ๐ผ๐ป๐ to join my group in ๐ Sept 2026 under the schemes. ๐+Info๐
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reposted by
James Birrell
Rodriguez-Macia Lab
3 months ago
We have a ๐ฃ๐ผ๐๐๐ฑ๐ผ๐ฐ๐๐ผ๐ฟ๐ฎ๐น ๐ฅ๐ฒ๐๐ฒ๐ฎ๐ฟ๐ฐ๐ต ๐๐๐๐ผ๐ฐ๐ถ๐ฎ๐๐ฒ (๐ฃ๐๐ฅ๐) 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! ๐+info๐
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reposted by
James Birrell
Rodriguez-Macia Lab
3 months ago
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!
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Research opportunities | Institute for Structural and Chemical Biology | University of Leicester
Postdoc opportunities at the Leicester Institute for Structural and Chemical Biology
https://le.ac.uk/research/institutes/structural-chemical-biology/opportunities
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reposted by
James Birrell
Sven T. Stripp
3 months ago
Delightful combination of spectroscopies (electronic, microwave) and protein crystallography in
@jarworrall.bsky.social
's new paper on cytochrome P450 decarboxylase from Staphylococcus aureus ๐คฉ
doi.org/10.1016/j.ji...
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James Birrell
ICH2026
6 months ago
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).
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reposted by
James Birrell
Leicester Institute for Structural and Chemical Biology
8 months ago
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...
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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...
https://pubs.rsc.org/en/content/articlelanding/2025/sc/d5sc01811k
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reposted by
James Birrell
Michael Hurst
8 months ago
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...
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reposted by
James Birrell
Sven T. Stripp
8 months ago
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...
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reposted by
James Birrell
Sven T. Stripp
8 months ago
We have positions for pCNF SDM of CpI in a recent grant application... Very encouraging to see Kylie's data!
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reposted by
James Birrell
Sven T. Stripp
8 months ago
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...
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reposted by
James Birrell
Sven T. Stripp
8 months ago
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.
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James Birrell
Sven T. Stripp
8 months ago
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 surpriseโผ๏ธ
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James Birrell
Sven T. Stripp
8 months ago
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...
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reposted by
James Birrell
Sven T. Stripp
8 months ago
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... ๐งต
add a skeleton here at some point
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reposted by
James Birrell
8 months ago
"redox-dependent nitrile band shifts" ๐คฉ
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James Birrell
Sandy Kilpatrick
8 months ago
Lovely stuff Zehui et al.!
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reposted by
James Birrell
Sven T. Stripp
8 months ago
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...
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reposted by
James Birrell
Sven T. Stripp
8 months ago
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.
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reposted by
James Birrell
Sven T. Stripp
8 months ago
Who's ready to talk about ferredoxin?
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reposted by
James Birrell
Rodriguez-Macia Lab
8 months ago
It is a real pleasure to collaborate with you guys! ๐
add a skeleton here at some point
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reposted by
James Birrell
Rodriguez-Macia Lab
8 months ago
Very happy to see this out! Take a look at this interesting paper on the application of 2D IR to [FeFe] hydrogenases ๐
add a skeleton here at some point
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Out now in
@chemicalscience.rsc.org
: We apply 2DIR spectroscopy to study [FeFe] hydrogenase for the first time. Check it out!
pubs.rsc.org/en/content/a...
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Two-dimensional Infrared Spectroscopy as a Tool to Reveal the Vibrational and Molecular Structure of [FeFe] Hydrogenases
[FeFe] hydrogenases are Natureโs 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...
https://pubs.rsc.org/en/content/articlelanding/2025/sc/d5sc01811k
8 months ago
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reposted by
James Birrell
Mike Hough
9 months ago
As part of this work we explicitly measured the XFEL temporal pulse profiles with a Wakefield device rather than inferring pulse length from electron bunch parameters
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reposted by
James Birrell
Mike Hough
9 months ago
Our new paper exploring the effect of XFEL pulse length and pulse intensity on electron density maps of two radiation sensitive proteins. A great collaboration between Diamond, SwissFEL and University of Essex's Worrall group.
journals.iucr.org/m/issues/202...
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Damage before destruction? X-ray-induced changes in single-pulse serial femtosecond crystallography
Varied pulse-duration and pulse-intensity serial femtosecond crystallography data do not show significant signs of radiation damage under typical experimental conditions.
https://journals.iucr.org/m/issues/2025/03/00/car5003/index.html
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reposted by
James Birrell
Sven T. Stripp
9 months ago
The meanest title โบ๏ธ
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reposted by
James Birrell
Sven T. Stripp
9 months ago
Here's what my former employer
@tuberlin.bsky.social
wrote about our work (๐ฉ๐ช)
www.tu.berlin/news/pressem...
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Durchbruch in der Methan-Forschung: Aktivierungsmechanismus des Methan-produzierenden Enzyms entschlรผsselt
โNatureโ-Publikation offenbart die evolutionรคre Verbindung zwischen zwei fundamentalen biologischen Prozessen
https://www.tu.berlin/news/pressemitteilung/durchbruch-in-der-methan-forschung-aktivierungsmechanismus-des-methan-produzierenden-enzyms-entschluesselt
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reposted by
James Birrell
Sven T. Stripp
9 months ago
Short press piece
@unipotsdam.bsky.social
about our new article
@nature.com
on methyl coenzyme M reductase (MCR)
www.uni-potsdam.de/en/headlines...
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Early life โ Enzyme for biological methane production decoded
https://www.uni-potsdam.de/en/headlines-and-featured-stories/detail/2025-04-17-early-life-enzyme-for-biological-methane-production-decoded
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reposted by
James Birrell
ChemComm
9 months ago
From our Emerging Investigators collection ๐ 'Terminal hydride formation in [FeFe] hydrogenase: understanding the role of the dithiolate bridgehead' by Patricia Rodrรญguez-Maciรก (
@rmlab.bsky.social
), James Birrell and colleagues.
#OpenAccess
๐
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Terminal hydride formation in [FeFe] hydrogenase: understanding the role of the dithiolate bridgehead
[FeFe]-hydrogenases are highly-active hydrogen-conversion biocatalysts using Earth-abundant metals in their active-site. Understanding their mechanism may enable design of catalysts for renewableโฆ
https://buff.ly/k5NFG1Z
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James Birrell
Rodriguez-Macia Lab
9 months ago
Have you read it yet? โบ๏ธ
add a skeleton here at some point
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reposted by
James Birrell
Gerti Schut
10 months ago
#2 out of 3 bfu family bifurcating structure with our CryoEM collaborators. Cryo-EM Structures Define the Electron Bifurcating Flavobicluster and Ferredoxin Binding Site in an Archaeal Nfn-Bfu Transhydrogenase - Journal of Biological Chemistry
www.jbc.org/article/S002...
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Cryo-EM Structures Define the Electron Bifurcating Flavobicluster and Ferredoxin Binding Site in an Archaeal Nfn-Bfu Transhydrogenase
Flavin-based electron bifurcation couples exergonic and endergonic redox reactions in one enzyme complex to circumvent thermodynamic barriers and minimize free energy loss. Two unrelated enzymes desig...
https://www.jbc.org/article/S0021-9258%2825%2900259-5/fulltext
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reposted by
James Birrell
Rodriguez-Macia Lab
10 months ago
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reposted by
James Birrell
Rodriguez-Macia Lab
10 months ago
bit.ly/4kOHp7P
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James Birrell
Sven T. Stripp
10 months ago
Very interesting! Toward a deeper understanding of the dithiolate ligand of [FeFe]-hydrogenase.
add a skeleton here at some point
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James Birrell
Sven T. Stripp
10 months ago
Big title for a DFT-only research paper...
onlinelibrary.wiley.com/doi/full/10....
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James Birrell
Rodriguez-Macia Lab
10 months ago
Big day today! Excited to share our new publication in
@chemcomm.rsc.org
about the formation of the very important hydride state in [FeFe] hydrogenases! Enjoy the reading! โบ๏ธ
pubs.rsc.org/en/content/a...
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https://pubs.rsc.org/en/content/articlepdf/2025/CC/D5CC00860C?page=search
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James Birrell
Chemical Science
10 months ago
In this Perspective, Patricia and colleagues detail the missing pieces that are still needed to understand the full catalytic cycle of these hydrogen conversion enzymes. Find out about how detailed insights have revealed a sophisticated, optimised, molecular catalyst, the active site H-cluster!
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reposted by
James Birrell
Chemical Science
10 months ago
Patricia Rodrรญguez-Maciรก holds an interest in [FeFe] hydrogenases and has published a number of works exploring the catalysis of these systems. Her latest Perspective on these enzymes is available to read here:
doi.org/10.1039/D4SC...
#ChemSky
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The missing pieces in the catalytic cycle of [FeFe] hydrogenases
Hydrogen could provide a suitable means for storing energy from intermittent renewable sources for later use on demand. However, many challenges remain regarding the activity, specificity, stability and sustainability of current hydrogen production and consumption methods. The lack of efficient catalysts bas
https://doi.org/10.1039/D4SC04041D
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reposted by
James Birrell
Sven T. Stripp
11 months ago
Not so relevant for infrared spectroscopy, unfortunatelly, but for any other kind of SEC these guys got some hot designs, love it!
redox.me/collections/...
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R/T/A Spectro-EC 1.75 mL - Reflection / Transmission / Absorption Spectro-Electrochemical Cell
This is a horizontally mounted, multi-purpose spectroelectrochemical cell designed to be used with standard UV-Vis or IR spectrometers. It enables obtaining electrochemical and spectroscopic informati...
https://redox.me/collections/spectro-electrochemical-cells/products/r-t-a-spectro-ec-1-75-ml-reflection-transmission-absorption-spectro-electrochemical-cell
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reposted by
James Birrell
Sven T. Stripp
11 months ago
Forgot to tag
@jamesbirrell.bsky.social
โผ๏ธ
add a skeleton here at some point
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reposted by
James Birrell
Sven T. Stripp
12 months ago
Interesting preprint from Plumere and Winkler et al. on [FeFe]-hydrogenase maturation (PDF)
chemrxiv.org/engage/api-g...
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James Birrell
Chris Greening
12 months ago
In Nature Chemical Biology today, we reveal how microbes clean our atmospheres by consuming carbon monoxide (CO) gas. A methodological tour de force from Ashleigh Kropp, Rhys Grinter, and David Gillett with broad implications for the atmosphere and bioenergetics.
www.nature.com/articles/s41...
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Quinone extraction drives atmospheric carbon monoxide oxidation in bacteria - Nature Chemical Biology
Here, Kropp et al. use cryo-electron microscopy and structural modeling to show that the enzyme [MoCu]-CO dehydrogenase interacts with its partner, the membrane-bound quinone-binding protein CoxG, to ...
https://www.nature.com/articles/s41589-025-01836-0
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