Research Network for Metals in Medicine



Dr Gerhard Schenk

Position: Lecturer, Chemistry

Affiliation: Molecular & Microbial Sciences School, University of Queensland

Postal Address:
Department of Chemistry
School of Molecular and Microbial Science
The University of Queensland
Brisbane, Queensland 4072

Phone: +61 (07) 3365 4144
Webpage: Dr Schenk's web-page

Research Profile

My research lies at the interface between biochemistry, inorganic and physical chemistry. Methodologies applied range from protein expression, purification and characterisation, steady- and pre-steady state enzyme kinetics and bioinformatics to molecular spectroscopy (cw and pulsed EPR, MCD and VTVH MCD, absorption and Raman) and density functional computations. More specifically, I am interested in the study of the reaction mechanisms of enzymes requiring transition metal ions for their catalytic function.

In particular, my current research focuses on a group of binuclear metallohydrolases, which play crucial roles in a variety of metabolic functions, including bone and collagen resorption, prevention of oxidative damage, correction of errors in DNA replication and cell proliferation. My aim is to gain detailed insight into the geometric and electronic structures of these enzymes to develop and design transition state analogues and specific inhibitors of chemotherapeutic significance.

I am also interested in the role of manganese in biological systems. Due to the versatility of its coordination chemistry and its wide range of oxidation states manganese offers a great opportunity to investigate the role of metal ions in enzymatic catalysis. Studies on protein systems are complemented by studies on relevant model complexes. In addition to these predominantly mechanistic investigations I also engage in comparative studies to define sequence and structural fingerprints that contribute to metal ion selectivity in protein active sites.

Selected Publications

  1. Schenk, G., Pau, M.Y.M. and Solomon, E.I. (2003) Electronic Structure of an S=3/2 {FeNO}7 model complex and its correlation to the geometric and electronic structure and the reactivity of {FeO2}8 complexes. J. Am. Chem. Soc. (submitted).
  2. Schenk, G., Neidig, M.L., Zhou, J., Holman, T.R. and Solomon, E.I. (2003) Spectroscopic Characterization of Soybean Lipoxygenase-1 Mutants: The Role of Second Coordination Sphere Residues in the Regulation of Enzyme Activity. Biochemistry (submitted).
  3. Solomon, E.I., Neidig, M.L. and Schenk, G. (2003) Magnetic Circular Dichroism of Paramagnetic Species. Comp. Coord. Chem. (in press).
  4. Twitchett, M.B., Schenk, G., Aquino, M.A.S., Yiu, D.T.-Y., Lau, T.-C. and Sykes, A.G. (2002) Reactivity of MII Metal-Substituted Derivatives of Pig Purple Acid Phosphatase (Uteroferrin) with Phosphate. Inorg. Chem. 41, 5787-5794.
  5. Schenk, G., Boutchard, C.L., Carrington, L.E., Noble, C.J., Moubarki, B., Murray, K.S., de Jersey, J., Hanson, G.R. and Hamilton, S. (2001) A Purple Acid Phosphatase from Sweet Potato Contains an Antiferromagnetically Coupled Binuclear Fe-Mn Center. J. Biol. Chem. 276, 19084-19088.


I'm a part of the Centre of Metals in Biology at UQ. Recently, Mark Riley, Graeme Hanson, Lawrie Gahan and myself received funding to purchase a Rapid-Freeze-Quench, which will complement our Stopped-Flow facility