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Contact details+64 (06) 356 9099 ext. 84626
I received BScHons (1974) and PhD degrees (1977) from the University of Canterbury under the mentorship of Ward Robinson and the late Gordon Rodley. After a post-doctoral fellowship with Jim Ibers at Northwestern University in bioinorganic chemistry, I took up a research associate position in solid-state chemistry at the University of Zürich. In 1982 I returned to the USA to Georgetown University in Washington DC earning tenure in 1987, as well as securing NIH and NSF grants. After a sabbatical in NZ with Ted Baker at Massey University 1989-1990, I finally returned to New Zealand in 1994, moving into structural biology.
Since 2001 I have been Professor in Structural Chemistry and Biology. Awards and honours include: election as Fellow of the Royal Society of New Zealand (2003), the SGS Prize by the New Zealand Institute of Chemistry, the Massey University Research Medal (Individual) (2010), the Marsden Medal of the New Zealand Association of Scientists (2011). In 2005, I travelled widely in Pakistan, as a guest of the Pakistan Higher Education Commission. Along the way, I have published over 160 papers and book chapters, helped with NZ's investment and access to the Australian Synchrotron (on-going), secured funding for NZ's highest field NMR spectrometer, the Bruker 700 MHz with Cryoprobe, advised on the MacDiarmid Institute-funded acquisition of Massey University's unique capability for chemical crystallography, and contributed fully to teaching.
I am an Associate Investigator in the MacDiarmid Institute for Advanced Materials and Nanotechnology and the Maurice Wilkins Centre for Molecular BioDiscovery, and a Principal Investigator in the Riddet Institute and holds an Adjunct Professorship and Associate Investigator position in the Biomolecular Interactions Centre.
I serve on Academic Board and as a Director of the New Zealand Synchrotron Group Ltd and chair of its Access Committee.
My research interests span solid-state chemistry to enzyme structure and function to origin of life studies. Much of this research is underpinned by use of X-ray diffraction techniques as the ultimate "microscope" into the structure of matter. I am increasingly interested in the role that entropy, the "dynamics of thermodynamics", plays in protein structure and function. NMR techniques give insight into this fourth dimension of time.
We are using our 0.90 Ã structures of manganese superoxide dismutase, a key enzyme of biological defences against reaction oxygen species that arise from living with and using molecular oxygen, to uncover how this enzyme couples proton transfer to electron transfer as superoxide anion-radicals are alternately reduced to hydrogen peroxide and oxidised to molecular oxygen. By means of site-directed mutants, we are also uncovering the origin of metal specificity that has pairs of near-identical enzymes, where one is active with manganese and the other with iron but not with the "wrong" metal ion.
With Barry Scott, we are pursuing structural genomics on fungal gene clusters of secondary metabolism to understand substrate trafficking. With Ren Dobson, Juliet Gerrard and Emily Parker (both at the University of Canterbury), we are looking at structure-function relationships in enzymes that come from metabolic pathways found in pathogens but not found in humans not only to understand the biophysics of enzyme regulation but also to design inhibitors as potential drugs.
In collaboration with Gill Norris, Pat Edwards and the Riddet Institute, we are investigating the dynamics of a key protein from milk whey that is involved in fouling milk-processing equipment, beta-lactoglobulin, by both X-ray and NMR techniques.
I am also interested in the evolution of protein structure and the role that the quaternary structure of proteins plays in controlling protein dynamics to optimise substrate specificity and activity, a role quite different to the cooperative functions generally associated with multi-subunit protein structures.
Our origin of life studies, with Pat Edwards and David Penny, focus on the chemical and physical behaviour of RNA and its components at extremes of pressure and temperature. This latter research is concomitant with the development of high-pressure/high-temperature NMR capability at Massey University.
Finally, I have a long-standing interest in solving the challenges posed by twinned and other pathological crystal structures, of both protein and small molecules.
Health and Well-being, Future Food Systems
Field of research codes
Biochemistry and Cell Biology (060100):
Bioinorganic Chemistry (030201):
Biological Sciences (060000):
Chemical Science (030000): Chemical Thermodynamics and Energetics (030602):
Inorganic Chemistry (030200): Macromolecular and Materials Chemistry (030300): Nanochemistry and Supramolecular Chemistry (030302): Physical Chemistry (incl. Structural (030600):
Structural Biology (incl. Macromolecular Modelling) (060112):
Structural Chemistry and Spectroscopy (030606): Theoretical and Computational Chemistry (030700)
Protein structure and function, including milk proteins (especially β-lactoglobulin and lactoferrin), proteins of fungal secondary metabolism, biological defences against reactive oxygen species (especially iron and manganese superoxide dismutases, enzymes from metabolic pathways of microorganisms and plants not shared by vertebrates (especially shikimate, bacterial cell wall and lysine biosynthetic pathways, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase, 3-deoxy-D-manno-octulosonate 8-phosphate synthase and dihydrodipicolinate synthase),
Pectin methylesterases as molecular motors, including application of molecular dynamics to enzyme mechanism.
Evolution of protein structure and function, enzyme allostery, protein dynamics,
Protein structure determination by X-ray (especilly ultra-high resolution protein structure) and NMR methods.
X-ray crystallography, especially crystal twinning and pathological structures in both protein and chemical crystallography (including polyoxometallates).
Applications of thermodynamics into protein and RNA folding, ligand binding and RNA stability; optimal conditions for origin of life, including development of capability for high-temperature/high-pressure nuclear magnetic resonance (NMR) spectroscopy and isothermal titration calorimetry (ITC).
Through involvement in capability building for synchrotron science in New Zealand, associated with investment in the Australian Synchrotron, broad knowledge of synchrotron techniques and expert knowledge of synchrotron diffraction techniques.
Project Title: Optimal chemical and physical conditions for the origin of RNA life forms
Date Range: 2010 - 2013
Funding Body: Marsden Fund - Full
My teaching currently spans first year biological chemistry to third year thermal physics.
I am course controller for and teach into the following courses:
123.220 Advanced Chemistry for Technology (hosted by Singapore Polytechnic)
123.311 Advanced Physical and Analytical Chemistry
I currently teach or have have recently taught into the following undergraduate courses:
123.172 Chemistry for Biological Systems 2
123.201 Chemical Energetics
123.271 Molecules to Materials
123.326 Advanced Chemical Biology
124.327 Modern Statistical Physics and Thermodynamics
236.301 Advanced Nanoscience
and from time to time into:
123.203 Inorganic Chemistry and Modelling
At the postgraduate level I teach modules on X-ray Crystallography and Statistical Thermodynamics