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Biography

• Publication profile on ResearcherID
• Research profile on ORCID
• Publication profile on Scopus

After receiving his PhD from the University of Cambridge (2003), I undertook postdoctoral research at the University of Southampton (2003−2004) and at the University of East Anglia (2005−2012). I was appointed to a faculty position at the University of East Anglia as Lecturer in Energy Materials in September 2012 and was promoted to Senior Lecturer in 2021. Research efforts in my group are focussed on developing metal-mediated activation of small molecules, with a particular interest in exploiting detailed mechanistic understanding enabling the development of novel systems. I am the co-author of 75 publications with around 2400 citations (h-index 30). My research group currently comprises one PhD student and one post-doctoral research assistant (funder: Leverhulme Trust). Over the past decade, I have focussed heavily on modelling the [FeFe]-hydrogenase active site, producing a significant number of high-profile publications. Other active research projects include synthesis of novel molybdenum/tungsten complexes, activation of dinitrogen, development of new dithiolene ligands to create functionalised molybdenum complexes capable of fixing carbon dioxide and synthesising novel CO-release molecules for anti-inflammatory treatments.

Selected publications

Ferracyclic carbonyl complexes as anti-inflammatory agents

M. A. Wright, T. Wooldridge, M. A. O'Connell and J. A. Wright,

Chem. Commun., 2020, 56, 4300, DOI: 10.1039/D0CC01449D

Muonium Chemistry at Diiron Subsite Analogues of [FeFe]-Hydrogenase

J. A. Wright, J. N. T. Peck, S. P. Cottrell, A. Jablonskytė, V. S. Oganesyan, C. J. Pickett and U. A. Jayasooriya, Angew. Chem. Int. Ed., 2016, 55, 14580, DOI: 10.1002/anie.201607109

Electronic control of the protonation rates of Fe-Fe bonds

A. Jablonskytė, L. R. Webster, T. R. Simmons, J. A. Wright and C. J. Pickett, J. Am. Chem. Soc., 2014, 136, 13 038, DOI: 10.1021/ja506693m

[FeFe] Hydrogenase: Protonation of 2Fe3S Systems and Formation of Super-reduced Hydride States

A. Jablonskytė, J. A. Wright, S. A. Fairhurst, L. R. Webster and C. J. Pickett, Angew. Chem. Int. Ed., 2014, 53, 10 143, DOI: 10.1002/anie.201406210

CO Releasing Molecules

The synthesis of deliverable organometallic compounds which release the therapeutic small molecule carbon monoxide (CO) when subjected to a suitable ‘trigger’ is currently of significant interest. Carbon monoxide, like nitric oxide (NO), is a vasodilatating substance and has been implicated in the regulation of large number of physiological and pathological processes, including inhibition of platelet aggregation and hormone release. Recognition of these roles has begun to drive research into CO-releasing therapeutics, including initial exploration of metallosystems, but the area is in its infancy.

Based on earlier work in modelling enzyme active sites, we have identified a new family of iron-containing molecules with benign co-ligands and which offer a starting point for research on the dynamics of triggered release. These possess ferracyclic structures analogous to those found at the active site of certain enzymes: an iron atom is held within an organometallic five-membered ring formed and importantly these systems bind up to three CO molecules. The project focuses on synthesising water- and lipo-soluble systems by modification of the ferracyclic ring to ensure deliverability. 

Functionalised models for formate dehydrogenase chemistry

There is an urgent need to develop new approaches to storing and releasing energy, particularly those usable in fuel cells. Formate is a ‘hydrogen carrier’, capable of delivering an equivalent of H2 as a liquid fuel to such devices, and so new routes to this molecule are extremely attractive. The formate dehydrogenase enzymes (FDH) can interconvert CO₂ and formate with selectively, with low overpotential and without requiring precious metals (Proc. Natl. Acad. Sci. USA, 2008, 105, 10654).The enzyme themselves are too large and oxygen-sensitive to be used in technological applications, and so new catalytically-active chemical models of the active site are urgently needed.

Chemical modelling related to the FDH active site has to date been concentrated on reproducing the metal coordination sphere (see for example Chem. Rev., 2004, 104, 1175). Crucially, there has been no work to introduce hydrogen-bond donors around this core, features which are established as vital in enzyme turn-over (J. Biol. Inorg. Chem., 2006, 11, 849). In a project funded by the Leverhulme Trust, we are developing new ligand architectures to introduce secondary coordination sphere donors to enable new catalytic manifolds.

Modelling metalloenzyme functionality

The unique ability of metalloproteins to catalyse economically-important chemistry has attracted a great deal of research attention over the past several years. The possibility of reproducing the functional chemistry of the protein systems offers the chance to harness these abilities in practical catalytic system.

The group has two ongoing research interests focussed on the [FeFe]-hydrogenase and nitrogenase enzymes. In the nitrogenase area, our focus is on mononuclear molybdenum complexes which have the potential to active dinitrogen. The core architectures involved are pincer-based motifs which will support the reactive metal centre. Our work on iron systems is concentrated on the introduction of novel ligand systems around a di-iron core to replicate both the structure and function of the natural systems. We are also interested in understanding the reactivity of these systems using a wide range of advanced mechanistic tools.