Professor Vic Arcus

Vic Arcus


Qualifications: BSc, MSc Waikato, PhD Cambridge

Research Supervised


  • Hamill, Carlin (in progress). Understanding allosteric enzyme regulation using macromolecular rate theory.
  • Grout, Emily (in progress). Understanding enzymatic mechanism and allostery using macromolecular rate theory.
  • Cookson, Ruth (in progress). Plant Biochemistry research, investigating the mechanism underlying the apparent loss of regulated growth in Lolium perenne roots following reintroduction of a transcriptional regulator deleted from the grasses approximately 65 million years ago.
  • Batterton, Chris (in progress). Fundamental aspects of enzyme structure and function.
  • Chonira, Vikas (2019). Engineering of an OB-fold protein scaffold for molecular recognition of cancer-specific intracellular kinases.
  • Mulholland, Claire (2019). Local and international origins of tuberculosis in New Zealand.
  • Prentice, Erica (2018). The temperature dependence of enzymatic rates.
  • Vickers, Chelsea (2017). Determining the function and regulation of the prokaryotic VapBC toxin-antitoxin protein complexes.
  • Zhang, Heng (2019). Characterising the three dimensional structure and function of a Bovine Salivary Protein (BSP30b).
  • Oulavallickal, Tifany (2016). Reconstruction of aroa/mura ancestral enzymes and screening of potential inhibitors.
  • Hennebry, Alexander (2014). Identifying the signalling pathway of a novel Myostatin Splice Variant (MSV).
  • Ruthe, Alaine (2014). Time to diagnosis and persistence: The two major determinants of effective tuberculosis control.
  • Andrews (nee Littlejohn), Emma (2013). The biology and biochemistry of PhoH2 proteins.
  • Summers, Emma (2013). The biochemistry and structural biology of Lsr2 from Mycobacterium tuberculosis.
  • Cumming, Mathew (2012). Structural and enzymatic characterisation of nucleoside triphosphate diphosphohydrolases from Trifolium repens and Dolichos biflorus.
  • McKenzie, Joanna (2011). The biochemistry of VapBC toxin-antitoxins.
  • Steemson, John (2011). Directed evolution and structural analysis of an OB-fold domain towards a specific binding reagent.
  • Till, Marisa (2011). Fibre degrading enzymes from Butyrivibrio proteoclasticus.

MSc (Research)

  • Steele, Mackenzie (in progress). 
  • Hamill, Carlin (2020). Understanding allosteric enzyme regulation using macromolecular rate theory.
  • Maguren, Ashleigh (2020). Physicochemical characterisation of allene oxide synthase variants.
  • Walker, Emma (2020). Parthenium argentatum allene oxide synthase as an antioxidant for bovine technologies.
  • Dillon, Brooke (2017). Caldalkibacillus thermarum PhoH2: Solving the solubility puzzle.
  • Kraakman, Kirsty (2017). Predicting carbon dioxide contributions from respiration and photosynthesis using Rhodobacter sphaeroides and macromolecular rate theory.


  • Schipper, Daniel (2020). Finding the good vibes of life, man: identifying catalytic vibrations in enzyme catalysis.
  • McMillan, Joel (2013). Biochemical characterisation of reconstructed ancestral CM-DAH7PS enzymes
  • Prentice, Erica (2013). Characterisation of enzyme evolution through ancestral enzyme reconstruction.
  • Sharrock, Abigail (2013). Characterisation of VapBC toxin-antitoxins from Mycobacterium tuberculosis.
  • Duyestyn, Jo (2012). Mechanism of RNase cleavage by VapC from Pyrobaculum aerophilum.
  • Easter, Ashley (2010). Decoupling enzyme catalysis from thermal denaturation.

BSc (Hons)

  • Shim, Ko Un Konny (2015). The implementation of a new method of ancestral sequence reconstruction incorporating species phylogeny.

Research Interests

Research and postgraduate study are encouraged in the Department of Biological Sciences. All research students acquire basic research skills and a knowledge of techniques, as well as training in specialist disciplines.

Our research focuses on molecular biology, structural biology and protein engineering. We are interested in the three-dimensional structures of several protein families and we use this information to study their biochemical functions. We use X-ray crystallography, protein NMR and other biophysical techniques. We are also interested in protein engineering to manipulate the structure and function of proteins. Here, we use site-directed mutagenesis and combinatorial mutagenesis in combination with structure determination to engineer new proteins.

Structural and Functional Biology of Microbial Toxin-Antitoxin Networks

Toxin-antitoxin pairs in bacteria act in concert to maintain low-copy number plasmids in daughter cells. It is also thought that these protein pairs are involved in microbial growth arrest under conditions of nutrient starvation and stress. We are pursuing the structures of a number of toxin-antitoxin complexes in an effort to find out more about the mechanism of cell-cycle arrest in Mycobacterium tuberculosis and M. bovis.

Protein Engineering to Produce Artificial Antibodies

We use a common protein scaffold to engineer a library of variants by randomizing up to seventeen amino acid positions on one face of the protein. We can then pick variants with desirable traits out of this library using phage display. This process is analogous to the selection of recombinant antibodies with the advantage that our scaffold is small and thermostable. Potential biotechnology applications are the current focus of our efforts.

Structural Biology of Proteins Involved in Plant Flowering

We are interested in several proteins which serve as checkpoints in triggering photoperiodic flowering in plants and their relationship with circadian controlled processes. We are using a range of biophysical techniques including X-ray crystallography, NMR, circular dichroism and electron microscopy to look at the structure and function of these proteins. Currently we are focusing on the proteins GI, FT and CO.

Endophyte Non-Ribosomal Peptide Sythetases

Very recently, our collaborators at AgResearch and Massey University have identified large operons in the symbiotic fungus Neotyphodium lollii, which code for non-ribosomal peptide sythetases. These genes code for proteins which are responsible for the biosynthesis of the important secondary metabolites. We are determining the structures of a number of domains from these operons to look at the molecular details of the biosynthesis of peramine.

Recent Publications

  • Alster, C. J., Robinson, J. M., Arcus, V. L., & Schipper, L. A. (2022). Assessing thermal acclimation of soil microbial respiration using macromolecular rate theory. Biogeochemistry. doi:10.1007/s10533-021-00885-6

  • Kwok, A., Camacho, I. S., Winter, S., Knight, M., Meade, R. M., Van der Kamp, M. W., . . . Pudney, C. R. (2021). A Thermodynamic Model for Interpreting Tryptophan Excitation-Energy-Dependent Fluorescence Spectra Provides Insight Into Protein Conformational Sampling and Stability. Frontiers in Molecular Biosciences, 8. doi:10.3389/fmolb.2021.778244

  • Duffy, K. A., Schwalm, C. R., Arcus, V. L., Koch, G. W., Liang, L. L., & Schipper, L. A. (2021). How close are we to the temperature tipping point of the terrestrial biosphere?. Science Advances, 7(3), eaay1052. doi:10.1126/sciadv.aay1052

  • Winter, S. D., Jones, H. B. L., Răsădean, D. M., Crean, R. M., Danson, M. J., Pantoş, G. D., . . . Pudney, C. R. (2021). Chemical Mapping Exposes the Importance of Active Site Interactions in Governing the Temperature Dependence of Enzyme Turnover. ACS Catalysis, 14854-14863. doi:10.1021/acscatal.1c04679

Find more research publications by Vic Arcus

Contact Details

Email: [email protected]
Room: C.2.11
Phone: +64 7 838 4679