Christopher Pickett

Christopher Pickett


  • 2.07 Chemistry

Personal profile


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School Position:

Professor of Chemistry, Director of the Energy Materials Laboratory

PhD Studentship available:

Hydrogen Chemistry Related to the Hydrogenases

Chris Pickett joined UEA as Professor of Chemistry in October 2005. He completed his PhD in the Southampton Electrochemistry Group under the guidance of Professor Derek Pletcher in 1975 and was then appointed to the staff of the Unit of Nitrogen Fixation at the University of Sussex. which was then directed by the late Professor Joseph Chatt FRS. He was awarded the Silver Medal for Chemistry and Electrochemistry of the Transition Metals by the Royal Society of Chemistry in 1993 for his work on Nitrogen Fixation which included the discovery of a route for the electrosynthesis of ammonia (Nature 1985, 317, 652).

In July 2009 Chris received the Royal Society of Chemistry Ludwig Mond Award for fundamental contributions to bioinorganic chemistry and electrochemistry (click HERE to view).

His group is currently researching into the chemistry of the metallo-sulfur hydrogenase enzymes, (see Chem. Rev., 2009, 109, Issue: 6, Pages: 2245-2274). These enzymes catalyse the reversible uptake/evolution of dihydrogen, chemistry which is of potential technological importance to clean energy transduction. The research has received widespread coverage in the scientific press [Science 2003, ACS Chemistry 2004, Chem. Eng. News 2005 (Feb), New Scientist 2005, Chem. Eng. News 2005(Dec), Fuel Cell Today 2005] with a paper in Nature on the assembly of the H-cluster framework chosen as one of the top twenty publications in chemistry for the year 2005 by Chem. Eng. News.

Recently the group has extended its interests to include artificial photosynthesis, looking at solar driven carbon dioxide fixation linked to alkane oxidation. This is a chemistry ‘grand challenge’, undertaken in collaboration with researchers from five UK laboratories, the SolarCAP Consortium ( The group also participates in the Supergen V biofuel cells programme, with particular emphasis on structuring electrode interfaces for artificial, enzymic or microbial energy transduction.

Studies on incorporating natural and synthetic clusters in amino acid/peptide functionalised electropolymers for electrocatalysis led to the recognition of the wider value of these electropolymer materials. In 2002, Chameleon Biosurfaces Ltd was founded to exploit their use as coatings for medical implant devices; the company has its research laboratory based in the School and has received funding from ICENI , Rainbow VCF,and other seed-corn funds.

  • Professor Invité, Université de Bretagne Occidentale 1992 - 3
  • RSC Award for Chemistry and Electrochemistry of the Transition Metals 1993
  • Associate Head of Department of Biological Chemistry, John Innes Centre 2001 -2005
  • Founder, Chameleon Biosurfaces Ltd., 2002
  • RSC Ludwig Mond Award, 2009

Selected Publications

Electronic Control of the Protonation Rates of Fe–Fe Bonds
Aušra Jablonskytė, Lee R. Webster, Trevor R. Simmons, Joseph A. Wright, and Christopher J. Pickett
J. Am. Chem. Soc., 2014, 136 (37), pp 13038–13044
DOI: 10.1021/ja506693m

[FeFe] Hydrogenase: Protonation of {2Fe3S} Systems and Formation of Super-reduced Hydride States
Aušra Jablonskytė, Dr. Joseph A. Wright, Dr. Shirley A. Fairhurst, Dr. Lee R. Webster and Prof. Christopher J. Pickett.
Angewandte Chem Int. Ed. 2014,53, (38), pp 10143–10146.
DOI: 10.1002/anie.201406210

The third hydrogenase: a ferracyclic carbamoyl with close structural analogy to the active site of Hmd.
P. J. Turrell, J. A. Wright, J. N. T. Peck, V. S. Oganesyan and C. J. Pickett
Angew. Chem. Int. Ed., 2010, 49, (41), pp 7508-7511
DOI: 10.1002/anie.201004189

Paramagnetic Bridging Hydrides of Relevance to Catalytic Hydrogen Evolution at Metallosulfur Centers
Aušra Jablonskytė, Joseph A. Wright, Shirley A. Fairhurst, Jamie N. T. Peck, Saad K. Ibrahim, Vasily S. Oganesyan, and Christopher J. Pickett
J. Am. Chem. Soc., 2011, 133 (46), pp 18606–18609
DOI: 10.1021/ja2087536

Structural and Functional Analogues of the Active Sites of the [Fe]-, [NiFe]-, and [FeFe]-Hydrogenases.  
Tard C, Pickett CJ. 
Chemical Reviews, 2009, 109, (6), pp 2245-2274

Key Research Interests

International collaborations

Chris Pickett's research on iron-only hydrogenase and on nitrogen fixation has involved key international collaborations. Dr Stephen Best at the University of Melbourne has brought to our studies much expertise in the application of powerful spectroelectrochemical techniques which has allowed us to obtain infrared and EXAFFS data on redox intermediates generated from hydrogenase models and from the iron molybdenum cofactor of nitrogenase; we have been supported by the Australian Research Council to undertake this collaborative work. Dr Luca De Gioia and his group in Milan have performed advanced DFT calculations on our structural models and on chemically or electrochemically generated intermediates and this has been invaluable to our understanding of the chemistry of hydrogenase diiron subsite and H-cluster analogues. Professor Lai - Shen Wang and his group at the North West Pacific National Laboratory have provided much insight into the electronic structure of our molecules by ion-trapping / photoelectron spectroscopy experiments and Dr Robert Szilagyi at Montana State University is probing electronic interactions across by sulfur K-edge XAS measurements.

  • Iron-only hydrogenase: artificial systems
  • The chemistry of biological nitrogen fixation
  • Bioelectropolymers

Iron-only hydrogenase: artificial systems

The crystallographic characterisation of Fe-only hydrogenase has revealed a striking resemblance of the diiron subsite of the catalytic centre, the H-cluster, to known [Fe2(m-SR)2(CO)6] (R = organic group) complexes. This type of assembly, first discovered by Reihlen and co-workers more than 70 years ago opened the way for the synthesis of {2Fe2S}- and {2Fe3S}-complexes with key structural and/or spectroscopic features of this biologically unprecedented - low-valent, carbon monoxide and cyanide coordinated - diiron unit, Figure. Whereas detailed studies of synthetic subsites have played a key role in informing the biological catalysis, particularly in the recognition of an unprecedented role for Fe(I) in biology, a major challenge has been to build a free-standing analogue of the entire H-cluster, Figure.

This is because it offers the prospect of  understanding the electronic and mechanistic interplay of the conjoined diiron and cubane units that form the enzymic catalytic machinery and may also presage the development of new electrocatalytic materials based on the biological structure. We have recently described the synthesis of  the entire iron – sulfur framework the H-cluster and have shown that such structures can electrocatalyse proton reduction, though at large overpotentials. These assemblies and the  chemistry we have developed for building are providing us with the springboard to construct new electrocatalytic materials.


Figure Composite structure of the H-cluster constructed from the crystal structures of Fe-only hydrogenase isolated from D. desulfuricans (Code 1HFE) and C. pasteurianum (Code 1FEH) and FTIR data from D. vulgaris. The apical group on the sub-site ligand may possibly be an NH or O but this remains crystallographically and analytically unresolved.

Key Publications

On the Electronic Strucure of the hydrogenase H-cluster
Schwab D.E.,Tard C., Brecht E., Peters J.W., Pickett C.J., Szilagyi R.K.
Chem Comm., 2006 , 3696-3698

Synthesis of the H-Cluster Framework of Iron-Only Hydrogenase.
C.Tard, X. Liu, S. K. Ibrahim, M. Bruschi, L. De Gioia, S. C. Davies, X.Yang, L-S. Wang, G.Sawers and C. J. Pickett
Nature, 2005,  434,  610-613.

A Novel {FeI-FeII-FeII-FeI} iron thiolate carbonyl assembly which electrocatalyses hydrogen evolution. 
C Tard, X Liu, D L Hughes and C J Pickett .
Chem Comm., 2005 , 133-135.

Dissecting the intimate mechanism of cyanation of [Fe2S3] complexes related to the active site of all-iron hydrogenases by DFT analysis of energetics, transition states, intermediates and products in the carbonyl substitution pathway.
G Zampella,M Bruschi, P Fantucci,M Razavet, C J  Pickett, L De Gioia.
Chem EU J  2005, 11, 509-533.

Electron-Transfer at a Dithiolate-Bridged Di-Iron Assembly; Electrocatalytic Hydrogen Evolution.
S. J. Borg, T. Behrsing and S. P. Best M Razavet, X Liu and C J. Pickett
J Amer Chem Soc.,  2004, 126, 509-533.

Chemistry and the Hydrogenases.
DJ Evans and CJ Pickett.
Chem Soc Rev., 2003 ,32, 268-275

Probing the Electronic Structure of the Di-Iron Subsite of [Fe]-Hydrogenase: A Photoelectron Spectroscopic Study of Fe(I)-Fe(I) Model Complexes.
X Yang, M Razavet, X-B Wang, C. J. Pickett, and L-S Wang.
J Phys Chem., 2003, 14072-14081   

All-iron hydrogenase: synthesis, structure and properties of {2Fe3S]-assemblies related to the di-iron sub-site of the H-cluster.
Razavet M, Davies SC, Hughes DL, Barclay JE, Evans DJ, Fairhurst SA, Liu X, Pickett CJ.
Dalton Trans.,  2003,  586-595

Transient FTIR spectroelectrochemical and stopped-flow detection of a mixed valence {Fe(I)-Fe(II)} bridging carbonyl intermediate with structural elements and spectroscopic characteristics of the di-iron sub-site of all-iron hydrogenase.
Razavet M, Borg SJ, George SJ, Best SP, Fairhurst SA, Pickett CJ.
Chem Comm., 2002 , 700-701. 

{2Fe3S} clusters related to the di-iron sub-site of the H-centre of all-iron hydrogenases.
Razavet M., Davies S. C., Hughes D. L., Pickett C. J.
Chem Comm., 2001 , 847-8.


The chemistry of biological nitrogen fixation

Biological nitrogen fixation is a key life process whereby free - living or symbiotic bacteria convert the rather inert dinitrogen molecule into ammonia by combining it with electrons and protons. The bacterial enzyme which carries out this remarkable chemistry under ambient conditions is nitrogenase. The active site of the common enzyme is a iron-sulfur molybdenum cofactor of stoichiometry Fe6S9Mo (FeMoco). The structure of the cluster is known but how it works remains unclear. Over many years the work of the Nitrogen Fixation Laboratory has established the basic functional group chemistry of molecular nitrogen at metal centres and this has provided the primary basis for discussion for how the enzyme functions at the atomic level. FeMoco can be extracted from the enzyme which has now allowed us to study its chemical and electrochemical properties in isolation. We are beginning to understand the redox levels at which isolated FeMoco binds inhibitors and substrates and have shown that the cluster shows chemistry akin to the whole enzyme system. 

Infra-red spectroelectrochemistry showing the binding of carbon monoxideto the extracted iron molybdenum cofactor of nitrogenase, FeMoco. 

Key Publications

CJ Pickett, KA Vincent, S K  Ibrahim,C A Gormal, B E Smith,S A Fairhurst, S P Best.
Synergic binding of carbon monoxide and cyanide to the MoFe cofactor of nitrogenase : relic chemistry of an ancient enzyme?
Chem EU J., 2004 10  4770-4776

Oganesyan V S, Barclay J E, Hardy S M, Evans D J, Pickett C J And Jayasooriya U A
Nuclear inelastic scattering spectroscopy of iron-sulfur cubane compounds
Chem Commun., 2004, 214-215

Probing the intrinsic electronic structure of the cubane [4Fe-4S] cluster: Nature's favorite cluster for electron transfer and storage
Wang XB, Niu SQ, Yang X, Ibrahim SK, Pickett CJ, Ichiye T, Wang LS
J. Am, Chem, Soc, 2003 , 125, 14072-14081

Electron-transfer chemistry of the iron-molybdenum cofactor of nitrogenase: Delocalized and localized reduced states of FeMoco which allow binding of carbon monoxide to iron and molybdenum
Pickett CJ, Vincent KA, Ibrahim SK, Gormal CA, Smith BE, Best SP
Chem EU J, 2003, , 9, 76-87

Coulomb- and antiferromagnetic-induced fission in doubly charged cubelike Fe-S clusters
Yang X, Wang XB, Niu SQ, Pickett CJ, Ichiye T, Wang LS
Phys.Rev.Let, 2002, 89, 163401,

Electrochemical cleavage of N=N bonds at a Mo-2(mu-SMe)(3) site relevant to the biological reduction of dinitrogen at a bimetallic sulfur centre
Le Grand N, Muir KW, Petillon FY, Pickett CJ, Schollhammer P, Talarmin J
Chemistry - A European Journal, 2002, 8 , 3115-3127

The isolated iron-molybdenum cofactor of nitrogenase catalyses hydrogen evolution at high potential
Chem Comm., 1999, 773

The isolated iron-molybdenum cofactor of nitrogenase binds carbon monoxide on electrochemically accessing reduced states
Chem Comm., 1999, 1019


We are developing methods for synthesising pyrrole monomers with diverse functionality which can be electropolymerised to give robust conducting films. Functionality includes:

  • amino acid , peptide and sugar functions
  • redox active metallo - centres
  • reactive ester groups
  • photo- or chemically deprotectable amine functions

The reactive ester and protected amine polymers allow facile post-polymerisational chemistry to be performed on the bulk polymers. Patents on this work cover:

  • chemical patterning of conducting polymer surfaces
  • growth of multilayers with different functionalities
  • biocompatible and other surfaces for coating implant devices
  • methods for electrochemically controlled drug delivery

A spin-out company, Chameleon Biosurfaces Ltd, was formed in 2002 to develop the commercial potential of the polymers, and has been funded by Plant Biosciences Ltd, the ICENI and Rainbow VCF funds.

Key Publications

Poly(ferredoxin) based electrode materials
Faraday Discuss., 2000, 116, 235

Synthesis of N-derivatised pyrroles: precursors to highly functionalised electropolymers
J Chem Soc Perkin Trans I, 1999, 1657

Merrifield chemistry on electropolymers: protection/(photo)deprotection of amine functions
Chem. Comm., 1998, 1175

Solid-phase Chemistry of  Electropolymers
M S Passos , M A Queiros  , T Le Gall , S K Ibrahim and C J Pickett
J  Electroanalytical Chem., 1997, 435 , 189 -203

Peptide Derivatised Poly(pyrrole) Modified Electrodes with Built -In Ion - Exchange Functions
S K Ibrahim, C J Pickett and C Sudbrake
J  Electroanalytical Chem., 1995 , 387, 139-142

Bioinorganic Reaction Centres on Electrodes. Modified Electrodes Possessing Amino-Acid, Peptide and Ferredoxin Type Groups on a Poly(pyrrole) Backbone:
Pentafluorophenolate Esters for Covalent Derivatisation before  and after Electropolymerisation
C J Pickett  and K S Ryder
JCS Dalton Trans, 1994 ,2181

Synthesis and Anodic Polymerisation of an L - Cystine Derivatised Pyrrole ; Co-polymerisation with a Tetraalkylammonium Pyrrole allows
Reduction of the Cystinyl Film to a Cysteinyl State that binds Electroactive {Fe4S4}2+ Centres.
C J Pickett , K S Ryder and J - C Moutet
Chem Comm., 1992 ,694

Iron-sulphur Clusters in Ionic Polymers on Electrodes: Preparation, Electron-transfer Properties, Ligand Exchange, EPR and FTIR Spectroscopy of Clusters Bound at Poly (tetraalkylammonium pyrrole) Modified Electrodes
C J Pickett , K S Ryder and J - C Moutet
JCS Dalton Trans., 1993 ,3695


Research Funding

Supergen5 Biological Fuel Cells Phase II 2010 -2014
Pickett + 6 laboratories April 2010 - March 2013

Carbon dioxide and alkanes as electron sink and source in a solar nanocell : towards tandem photosynthesis of carbon monoxide and methanol
Pickett, CJ ; Nann T
1 June 2008 - 31 May 2011

Royal Society / Wolfson Foundation
The Hydrogen Energy Laboratory
Pickett, CJ ; C Shang
1 March 2008 - completion 30 April 2009

Iron-only hydrogenases: a functional H-cluster
Pickett, CJ
1 July 2007 - 30 June 2010

ICASE : Anti-thrombolytic electropolymers.
Pickett, CJ
1-Nov-06 - 30-April 10

Follow on fund : In vitro biocompatibility and release characteristics of polypyrrole -bupivacaine coatings for neurostimulators
Pickett, CJ
01-May-06 - 30-Apr-07

The Supergen5 Biological Fuel Cells Consortium
Pickett, C, Slade, R (Surrey), Armstrong, F (Oxford), Premier, G (Glamorgan), Sloan, W (Glasgow) and Guo, ZX (Queen Mary, London)
01-Jan-06 - 31-Dec-09

The Diawa Anglo-Japanese Foundation
Construction of metallo-sulfur catalysts based on Natures’ blueprints for transforming small molecules
Redshaw, C and Pickett, C J.
02-Aug-06 – 02-Aug-07

Foreign and Commonwealth Office, Global Opportunities Fund
Hydrogen economy and fuel cells next generation hydrogenase models
Redshaw, C and Pickett, C J.
01-Oct-05 - 30-Apr-06

The Royal Society
Incoming Short Visits : Prof Xiaoming Liu, Nanching, China.
Pickett C J
03-July-06 - 24-Sep-06

Chameleon Biosurfaces

Chameleon Biosurfaces

Artificial Hydrogenases
Pickett CJ
01-Dec-2001 - 30-Nov-2004

Molybdenum Chemistry
Pickett C J
01-Jan-04 - 31-Dec-04

Radical Chemistry
Pickett C J
01-Jan-03 - 31-August-03

Research Group or Lab Membership

Chris Pickett's group researches into chemistry related to the hydrogenases, including artificial enzyme research; solar fuels; photocatalysis at semiconductor electrodes; systems for the fixation of carbon dioxide and for the generation / utilisation of hydrogen; electrochemistry of anodophilic microbes for energy harvesting.

Current Members of the Research Group

  • Professor Chris Pickett (Director, Energy Materials Laboratory)
  • Dr. Saad Ibrahim (Senior Research Fellow, EPSRC Supergen V)
  • Dr. Joseph Wright (Senior Research Associate)
  • Mr Khalaf Alenezi (Postgraduate Student)
  • Miss Ausra Jablonskyte (Postgraduate Student)
  • Mr Lee Webster (Postgraduate Student)
  • Miss Amanda Hill (Postgraduate Student)
  • Mr Mark Fowler (BSc Project Student)
  • Mr James Box (MChem Project Student)

Visiting Scientist 2012:

  • Dr. Peiyi Li (Senior Lecturer, Xi'an Jiaotong - Liverpool University, Jiangsu Province, PRC)

Visiting Scientists 2009-10:

  • Dr Ali Al-Ghamdi (Taibah University, Saudi Arabia)
  • Mr Alexandre Erdmann (6 month internship student from UFR des Sciences, Universite Paris-Sud 11)
  • Miss Audrey Roger ( 6 month internship student from UFR des Sciences, Universite Paris-Sud 11)

Visiting Scientist 2008-9:

  • Dr Woi Pei Meng (University of Malaya, Kuala Lumpur)

Visiting Scientists 2007-8:

  • Prof. Xiaoming Liu (Royal Society Short Term Visiting Fellow) 
  • Dr Stephen P Best ( Sabbaticant, University of Melbourne)

Dr Saad Ibrahim setting up to do some electrochemistry.... Saad did his PhD in the Nitrogen Fixation Laboratory at the University of Sussex on the synthesis and electrochemistry of metal sulfur clusters and other metallo-sulfur systems and then joined Professor Chris Pickett's laboratory in NFL as a permanent scientist. He has underpinned the groups research on biological metal sulfur systems such as the iron-molybdenum cofactor of nitrogenase, novel electropolymers, electrochemistry and synthesis providing a cornerstone in the training and guidance of postgraduate and postdoctoral scientists. This continued  with the move of the  Nitrogen Fixation Laboratory to Norfolk  in 1995. He is with Chris a founder scientist of Chameleon Biosurfaces and co-inventor of the technology on which the company is based in UEA. Currently he is researching on new electrocatalytic materials based on the active site of iron-only hydrogenase, on photoelectrochemistry at semiconductor electrodes and on molecular catalysis of carbon dioxide reduction and hydrogen generation.

Tim Boote started his PhD on the synthesis of novel electropolymers for biomedical application in November 2007, funded on an award from the East of England Development Association as an Industrial Case Student having previously completed a degree in Medical Biochemistry at the University Birmingham. He successfully completed his PhD in 2010, his thesis is entitled : 'Anti-thrombogenic electropolymers for coronary stents, surface motifs and garlic extracts.'

Ausra Jablonskyte, pictured in the Energy Materials Laboratory, (Spring 2012). Following her EPSRC funded summer internship, (July - September 2009). Ausra completed her MChem Project on mechanistic aspects of chemistry related to [FeFe]-hydrogenase, and is now undertaking a PhD exploring new synthetic chemistry. She has recently had a paper published in JACS (Journal of the American Chemical Society) relating to paramagnetic hydrides in biology.  


Dr Peiyi Li joined the Energy Materials Laboratory in 2008. In September 2011, Peiyi took up a new position as Senior Lecturer at Xi'an Jiaotong-Liverpool University in Jiangsu Province, China. We are very happy to welcome her back in 2012 as our visiting scientist for the next few months.She is researching into electrochemical alkane oxidation for generation of oxygenated products and exploring the use of metalloporphyrin electrochemistry for electrocatalysis and photocatalysis.

Amanda Hill completed her MChem at UEA in 2011 after a successful final year project in the Energy Materials Laboratory. After graduating she found immediate employment in the School of Pharmacy as a research assistant. Amanda rejoined the EML in at the beginning of 2012 as a PhD student where she is currently studying models for the mono-[Fe] Hydrogenase.In the presence of its carbocation substrate, the enzyme catalyzes the reversible cleavage of dihydrogen into proton and hydride, placing the latter concomitantly onto the substrate molecule. The enzyme is of interest in the context of catalysis of hydrogenations of organic materials which will avoid the use of rhodium, iridium or other precious metals.  Amanda enjoys nature, photography and walking her dog.

Lee Webster is in his second year of PhD and is researching on the electrochemistry and photoelectrochemistry of small molecule activation, including electrocatalysis and photoelectrocatalysis of proton reduction. Recently Lee presented his work at the Royal Society Summer Science Exhibition in July 2011 and to MPs at the 'SET for Britain' event at the Houses of Parliament.

Khalaf Alenezi  received his BSc degree in Chemistry from the University of King Saud (Saudi Arabia) in 1999. He worked as a teacher in the Ministry of Education in Saudi Arabia (2000 -2007), receiving his MSc degree from King Saud University in 2007. Khalaf moved to Hail University in 2008, where he gained a scholarship to study for his PhD at the Energy Materials Laboratory, UEA. Since October 2010 Khalaf has been looking at electrocatalysis and photoelectrocatalysis of small molecule reduction and alkane oxidation by metalloporphyrin systems.  

Areas of Expertise

Electrochemistry; biological hydrogen; stent and other medical device coatings.

Expertise related to UN Sustainable Development Goals

In 2015, UN member states agreed to 17 global Sustainable Development Goals (SDGs) to end poverty, protect the planet and ensure prosperity for all. This person’s work contributes towards the following SDG(s):

  • SDG 7 - Affordable and Clean Energy