Professor Armstrong tutors Inorganic Chemistry and lectures in the Inorganic Chemistry Laboratory.
Professor Armstrong leads a research group concerned with mechanistic and exploratory Bioinorganic Chemistry. The principal aims are to understand the chemical reactions carried out by the active sites of metalloproteins (a well-known example would be the Fe-porphyrin group as occurs in haemoglobin) and to elucidate how long-range electron transfer in complex protein systems is coupled to catalysis and ion/proton transfer.
Subjects range from the properties of unstable Fe-S clusters and
Fe(IV)=O (to most chemists an unusual oxidation state) to medically
important respiratory chain electron transport enzymes such as succinate
dehydrogenase. To study these systems, his group uses a range of
kinetic techniques, and is currently developing a powerful new method in
which the chemistry of metalloprotein active sites is probed
electrochemically while they are absorbed on a carbon electrode