Fraser Armstrong - Biography#
SUMMARY OF CAREER:
Fraser Armstrong is a Professor of Chemistry at Oxford University and a Fellow of St John’s College, Oxford. He obtained his PhD at University of Leeds with Geoff Sykes in 1978 then carried out postdoctoral research with Peter Kroneck (Konstanz), Ralph Wilkins (New Mexico), Helmut Beinert (Madison) and Allen Hill (Oxford). In 1983 he was awarded a Royal Society University Research Fellowship which he held in Oxford until 1989. In 1989 he joined the Chemistry Faculty at the University of California, Irvine, and was granted tenure in 1992. He moved to his present position in Oxford in 1993. In 2008, he was elected a Fellow of the Royal Society, which is the Scientific National Academy of the United Kingdom and Commonwealth. In addition to his research, he coauthors a popular undergraduate textbook on Inorganic Chemistry.
RESEARCH AREAS:
Biological chemistry; and in particular, understanding the nature and mechanism of complex biological electron-transfer reactions.
The development and application of a concept and suite of methods called ‘Protein Film Electrochemistry’ to study active sites in electron-transfer proteins and enzymes; labile and vacillatory Fe-S clusters; chemical coupling and gating of biological electron transfer reactions; mechanisms and regulation of catalytic electron transport in multi-centred metalloenzymes.
Studies and exploitation of electrocatalysis by hydrogenases and CO2-reducing enzymes and the discovery that many enzymes behave as reversible electrocatalysts.
Enzyme active sites as real and inspirational electrocatalysts in fuel cells and artificial photosynthesis.
Mechanistic basis of microbial energy capture from trace H2. Tackling challenges for achieving efficient H2 production by microorganisms (making hydrogenases operate in air).
Enzyme catalysis on photoexcitable nanoparticles.
Invention of the ‘Electrochemical Leaf’ for driving, monitoring and controlling multi-enzyme tandem catalysis within electrode nanopores – a new way of studying and exploiting enzyme cascades.