Oxford University Crest

The Armstrong Research Group
Inorganic Chemistry Laboratory

Third floor ICL, rooms: T7–T12, T17
Phone: T12 (Fraser’s office): +44 (0)1865 272647
e-mail: fraser.armstrong@chem.ox.ac.uk

Fraser Armstrong
Fraser Armstrong

Fraser Armstrong is Professor of Chemistry and a Fellow of St John’s College. His interests are in biological chemistry, bioenergetics and in the mechanisms and exploitation of enzymes related to energy production. He has received a number of awards including the European Award for Biological Inorganic Chemistry, the Carbon Trust Innovation Award, the Max Planck Award for Frontiers in Biological Chemistry and the Royal Society of Chemistry Award for Interdisciplinary Chemistry. He travels widely giving invited lectures on topics including catalysis, bioenergetics and renewable energy. He is co-editor of Energy … beyond oil which focuses on alternative energy-generating technologies.

Outside of the office, Fraser can be found with his group at the Lamb & Flag Thursday nights in term time.

Fraser has been elected Fellow of the Royal Society.

Post-Doctoral Researchers
rhiannon Rhiannon Evans

I completed my PhD in Chemistry at Cardiff University in 2010 investigating various aspects of dihydrofolate reductase catalysis. My interests involve relating enzyme structure and function, with a particular focus on how we can explore and exploit differences in environmental optima. Since joining forces with Fraser my work has mainly focused on the differences of oxygen tolerant and oxygen sensitive hydrogenases and how we can take advantage of conserved differences in their amino acid compositions. The ultimate aim is to use site directed mutagenesis to learn about the mechanistics of dealing with oxygen attack, whist still having a functional enzyme to study using physical chemistry techniques such as protein film electrochemistry and EPR. I have a keen interest in relating the research we conduct in the group to the public and have been involved in national science festivals such as the Royal Society Summer Science Exhibition and Oxfordshire Science Festival. I have recently become a Junior Research Fellow of Wolfson College here in Oxford. Outside of the lab I enjoy catching up on series that I spend the rest of the time trying to avoid spoilers from.

zhijiang Zhijiang Wang

I completed my PhD in Materials Physics and Chemistry at Harbin Institute of Technology in 2010. My interests involve nanostructures with controlled structure and interface interactions, which could greatly enhance the potential and broaden the application of nanomaterials related to energy production and environmental protection. In Fraser’s group, my project, inspired by the mechanism of H2 activation by hydrogenases, is to develop novel semiconductor based colloidal catalysts to achieve highly efficient and low-cost H2 evolution.

ClareMegarity Clare Megarity

I completed my PhD at Queen’s University Belfast in 2014. My research focused on the structure and function of oxidoreductase enzymes, in particular, using site-directed mutagenesis to elucidate the mechanism of negative cooperativity induced by specific inhibitors. My thesis presented evidence to support the presence of a pathway linking the two active sites in these dimeric enzymes through which negative cooperativity propagates.

I joined the Armstrong group in July 2015. My research here involves the physical characterization of redox enzymes produced in recombinant strains of the photosynthetic organism Chlamydomonas reinhardtii. Since starting, my work has focused on the kinetics of activation of an apo-hydrogenase enzyme upon binding an inorganic [2Fe] active site mimic. I have been using protein film electrochemistry to measure the rates of both H2 oxidation and H+ reduction, catalysed by the activated hydrogenase. The project is collaborative with the groups of Thomas Happe (Ruhr University of Bochum, Germany) and Gilles Peltier (CEA Cadarache, France). The ultimate aim is to produce fuels and interesting chemicals from sunlight. Outside of the lab I enjoy art, reading, pondering the idea of getting back into running and actively not joining Facebook.

Kourosh Kourosh H. Ebrahimi

I am interested in understanding the fundamentals underlying the enzymatic reactions performed by metalloenzymes such as hydrogenases, radical-SAM enzymes, and ferritin. Outside lab I enjoy paining with oil on canvas and having a quiet time at home.

Lab Technician
elena Elena Nomerotskaia
I am the group’s lab technician, and my work mainly involves large-scale purification of enzymes for use in electrochemical and EPR experiments. I am also responsible for ensuring the lab is kept clean, tidy and well stocked!
Doctoral Students
wang Yiduo Wang

I am a 4th year DPhil student. I am investigating how Metalloenzymes work in aqueous microenvironment confined by ionic liquids and how enzymatic fuel cells work using ionic liquids as electrolyte.

I like swimming and reading in my spare time.

Tania Shams Afroza Islam (Tania)

I am in the fourth year of my DPhil studies and attached with St. John’s College. I completed my B.Sc. and M.S. in Applied Chemistry and Chemical Engineering from University of Dhaka, Bangladesh, with top positions in both before joining as a faculty member of that department. As Assistant Professor, my job was to conduct classes, both theoretical and practical. In Fraser’s lab, I am investigating various highly efficient redox enzymes (hydrogenase, CODH and reductive dehalogenase) with Protein Film Electrochemistry and Site-Directed Mutagenesis techniques.

When not in the lab, my time is taken up with caring for my two children, aged 6 and 4, and matters related to them. My spare time is spent with my husband, usually chatting or watching TV. Besides trying to tie up the loose ends in my investigations with the enzymes, I plan on getting to watch (good) movies as soon as they are released in the theatres and eating out more often. Fingers crossed!

bhavin Bhavin Siritanaratkul

I’m a fourth year DPhil student from Thailand. Before coming here, I studied in Japan for 7 years and received a Bachelor’s and Master’s degree in Chemical Engineering from the University of Tokyo. Previously I did some research on photocatalytic water splitting by using semiconductor powders, and I hope to combine that knowledge with the use of enzymes to construct systems for CO2 reduction under visible light. I am also investigating light-driven enzymatic systems for other reactions, such as reductive dehalogenation.

In my free time, I like to read science fiction and fantasy. I also write science fiction short stories, with the dream of getting published in Nature’s Futures section.

Emily Emily Brooke

I am a second year DPhil student with St. John’s college. Before joining Fraser’s group, I received my MChem from the University of York. My current work is focused on the role of conserved amino acid residues that neighbour the active site of the [NiFe]-hydrogenases. To do so, I am using site-directed mutagenesis of the oxygen-tolerant hydrogenase enzyme Hyd-1, from E. coli, and using techniques such as Protein Film Electrochemistry, X-ray Crystallography and EPR spectroscopy.

My greatest passions in life, outside the lab of course, are drinking tea, eating Yorkshire Puddings and indulging in hours of reading, knitting & crochet and my bunny rabbits. To work off all those Yorkshire puddings, I occasionally go for a run or a long walk!

f35 Stephen Beaton

I am a first-year MSc student at Exeter College. I received my undergraduate from a small technical college in the United States. My current work is focused on understanding the mechanism of hydrogen reduction in Hyd-2 of E. coli. This work includes analyzing the effect of site-directed mutagenesis on Hyd-2 from E. coli with a variety of techniques.

In my free time, I enjoy going to events at the Oxford Union and the Oxford University Strategic Studies group, as well as traveling, running, and pretending that I am an F-35 practicing short-takeoffs from aircraft carriers.

Part II Students
Alexander Alexander Bridgeman

I’m a part II student from St Hilda’s College. For my project I’m investigating what happens to H+ ions after dihydrogen has been oxidized at the NiFe active site of an oxygen-tolerant hydrogenase enzyme known as ’Hyd1’. I’m going to be doing this by site directed mutagenesis of the wild-type enzyme to vary potentially important residues which form part of (what could be considered as) the second coordination shell of the active site and then electrochemically probing these mutants.

In my free time I can be found at the gym, pulling pints in the college bar, rowing, cooking, or doing something outdoorsy on a mountain somewhere.

amelia Amelia Girling

I’m a Part II student from Trinity. This year, I am looking at the reaction mechanism for hydrogen activation in hydrogenases using EPR and a freeze quench machine.

Outside of the lab I enjoy dancing and playing music but spend the majority of my time trying, unsuccessfully, to train my pet rabbit.

ThomasRoberts Thomas Roberts

I’m Tom, a part II student at St Hugh’s College. Within the Armstrong group, I’m studying the electrochemistry of the enzyme PetF on a graphite electrode.

ElliotRogers Elliott Rogers

Hello! I’m a Part II student from Keble College. My project involves testing the possibility of protecting HydA1 from O2 by fusing it with a blue Cu oxidase protein, an O2 scavenger. It would give us an interesting way to address O2 protection, as this method of protection is similar to how O2-tolerant [NiFe]-hydrogenases work.

In my spare time I enjoy playing sports, getting involved with student societies and listening to jazz.