Enzyme catalysts are central to life and to delivery of the bioeconomy. They are essential components in the new science of 'synthetic biology', offering new routes to biofuels, bulk and commodity chemicals and novel therapeutics. Despite this, our ability to create new enzymes through rational engineering is limited, which is a consequence of our poor understanding of mechanism and quantitative appreciation of the 'catalytic effect'. We are interested in gaining deeper understanding of catalysis and using this information to drive new applications in synthetic biology and metabolic engineering. We focus on fundamental studies of enzyme mechanism, developing 'sharper' tools to analyse mechanisms across a wide range of timescales (femtoseconds to seconds). This involves both classical and quantum mechanical appreciation of the underlying chemistry. We then translate this knowledge into applications, e.g. in industrial biotechnology (chemicals manufacture), or development of potent inhibitors of enzyme function (drug discovery). Our work is highly interdisciplinary and we have broad interests captured by the descriptors: quantum biology; isotope effects; enzyme chemistry; laser spectroscopy; fast reactions methods; structural biology; kinetics and inhibition; enzyme evolution and pathway engineering; biocatalysis and biomanufacture.
Nigel Scrutton is Director of the Manchester Institute of Biotechnology (MIB) responsible for the strategic leadership and operational management of the institute, which comprises over 50 leading research groups from across all Faculties and is home to ca £100M of current grant funding and 8 spin out companies.
Nigel has an established position in the field of enzyme catalysis, biophysics and biomolecular engineering. He holds an EPSRC Established Career Fellowship, is recipient of the Biochemical Society Colworth Medal, the RSC Charmian Medal, the RSC Rita and John Cornforth Award and a Royal Society Wolfson Research Merit Award. He has served on several national steering groups, advisory boards and governing bodies. He heads a group of ca 40 researchers. He has published ca 380 scientific papers, holds several patents, and has edited 3 volumes on enzyme chemistry, quantum biology, biocatalysis, synthetic biology and engineering. He has held contiguous externally funded research fellowships for 29 years (1988-2017) with only a 12-month break due to University relocation. Nigel is PI/Director of the BBSRC/EPSRC Synthetic Biology Research Centre 'SYNBIOCHEM' based in MIB. He is also PI/Director of a Marie Curie IDP 'MAGIC' responsible for the training of 12 early stage researchers at Manchester and a Director of the MIB spin out company C3 Biotechnologies Ltd.
Nigel received a first class degree in Biochemistry, was awarded a Sambrooke Exhibition and the Robson Prize from the University of London, King's College. He gained his ScD and PhD (as a Benefactors' Scholar) at St John's College, the University of Cambridge. At Cambridge he was awarded the Henry Humphrey's Research Prize, held a Royal Commission for the Exhibition of 1851 Research Fellowship, a St John's College Research Fellowship and a Royal Society University Research Fellowship. He also held a Fellowship and was Director of Studies at Churchill College, University of Cambridge. In 1995 he moved to the University of Leicester as Royal Society University Research Fellow, where he later became Lister Institute Research Professor of Biochemistry and Professor of Biochemistry. He was appointed Professor at the University of Manchester in 2005, where he held a BBSRC Professorial Research Fellowship and was Associate Dean for Research prior to his appointment as MIB Director.
Nigel’s group is noted for its contributions to catalysis science, especially in the fields of quantum biology (tunnelling), dynamics and biocatalysis, and more recently synthetic biology. His work is interdisciplinary at the interfaces of chemistry, biology and physics, supported by a genuinely world-leading infrastructure for biophysical chemistry that he has established in MIB.