Willows, Robert - Macquarie University - Department of Chemistry and Biomolecular Sciences

研究领域

Innovative Grain Foods CRC Brian Atwell, Tom Roberts and I work together with BRI Pty Ltd on a bioprocessing project for the Grain Foods CRC. This also involves industry partner George Weston Foods. We are investigating how biological processes might increase the yield and quality of flour. The work involves monitoring biochemical and structural changes that occur in grains prior to and during milling. Traditionally a technological field of inquiry driven by engineers, it has the potential for innovative biochemical discoveries with significant industry application. FORC iTTC A/Prof Brian Atwell, and I work on the proteomics of cereals with industry partner Grain Growers Pty Ltd. We are investigating how proteomic analysis of grain samples may be used to determine provenance, variety and quality characteristics of grains. Specifically how location and environmental factors effect the proteomic profile of cereals and how this may effect quality, as well as being a predictor of the location and time that the grain was grown and harvested. Molecular Machines Working with Dr. Anthony Duff at ANSTO and Dr. Steve Harrop at the Australian Synchrotron, my lab also is involved in investigations into molecular machines could potentially reveal how nanotechnology can be harnessed for the building of nanostructures that may be directed to perform mechanical work. I am investigating how the AAA+ class of molecular machines catalyse changes in structure at the molecular level in order to understand how those processes might be manipulated. AAA+ proteins are the one of the largest and most ubiquitous class of proteins and can potentially be modified for other biotechnical applications. Chlorophyll Biosynthesis and Chlorophyll f The main field of inquiry throughout my career has been in porphyrin biosynthesis and metabolism, specifically the biochemistry of heme and chlorophyll biosynthesis in bacteria, plants and algae. Our group was the first to define the structure of a magnesium chelatase subunit. The current focus of research efforts relate to the mechanism of metal ion insertion into protoporphyrin IX to make heme or magnesium protoporphyrin IX, and the regulation of these two competing reactions. I am also interested in the regulation and synthesis of aminolevulinic acid, which is the universal precursor of all tetrapyrroles. Together with A/Prof Min Chen at the University of Sydney we are also working on characterising Halomicronema hongdechloris, the chlorophyll f synthesizing cyanobacteria that we discovered in stomatolites off Shark Bay, WA.

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Gibson L.C.D., Willows R.D., Kannangara C.G., Wettstein D. von, and Hunter C.N., (1995) Magnesium-protoporphyrin chelatase of Rhodobacter sphaeroides: reconstitution of activity by combining the products of the bchH, I and D genes expressed in E.coli. Proc. Natl. Acad. Sci. U.S.A., 92, 1941-19 Willows R.D., Gibson L.C.D., Kannangara C.G., Hunter C.N. and Wettstein D. von. (1996) Three separate proteins constitute the magnesium chelatase of Rhodobacter sphaeroides. Eur. J. Biochem. 235, 438-443 Willows, R.D. and Beale, S.I. (1998) Magnesium Chelatase: Heterologous Expression of the Rhodobacter capsulatus BchI, -D, And -H Genes that Encode Mg Chelatase Subunits and Characterization of the Reconstituted Enzyme. J. Biol. Chem. 273, 34206-34213 Willows R.D., Mayer S.M., Foulk M.S., DeLong A., Hanson K., Chory J., and Beale S.I. (2000) Phytobilin biosynthesis: the Synechocystis sp. PCC 6803 heme oxygenase-encoding ho1 gene complements a phytochrome-deficient Arabidopsis thaliana hy‑1 mutant. Plant. Mol. Biol. 43,113-120 Fodje M. N., Hansson A., Hansson M., Olsen J., Gough S., Willows R. D., and Al-Karadaghi S. (2001) Interplay between an AAA module and an integrin I domain may regulate the function of magnesium chelatase. J. Mol. Biol. 311, 111-122 Hansson A., Willows R.D., Roberts T. H., Hansson M. (2002) Three semidominant mutants with single aminoacid substitutions in the smallest magnesium chelatase subunit form defective AAA+ hexamers. Proceeding of the National Academy of Sciences, USA 99, 13944-13949 Willows R.D. (2003) Biosynthesis of Chlorophylls from Protoporphyrin IX. Natural Product Reports, 20, 327-341 Willows R.D., Hansson A., Birch D., Al-Karadaghi, S., Hansson, M. (2004) EM single particle analysis of the ATP-dependent BchI complex of magnesium chelatase: an AAA+ hexamer. J. Struct. Biol. 146, 227-233