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Prof Wolfgang Maret

WolfgangMaret140x180Professor of Metallomics

Department of Nutrition and Dietetics
Diabetes & Nutritional Sciences Division
King's College London
Room 3.79
Franklin-Wilkins Building
150 Stamford Street

Tel: +44 (0) 20 7848 4264
Fax: +44 (0) 20 7848 4171


  • Senior Lecturer, King’s College London, 2009 to present
  • Associate Professor, The University of Texas Medical Branch, Galveston, TX, USA 2002-2009
  • Assistant Professor, Harvard Medical School, Boston, MA, USA 1986-2002
  • Research Associate, Saarland University, Saarbrucken, Germany 1982-1986
  • Postdoctoral Research Fellow, The University of Chicago, Chicago, IL, USA 1980-1982

Research interests

  • Molecular and cellular mechanisms of metal homeostasis
  • Role of micronutrients in normal physiology and pathophysiology
  • Sulfur and selenium redox biochemistry
  • Structure and function of metalloenzymes
  • Key words: Transition Metals, Zinc, Iron, Selenium, Redox Stress, Redox Signaling, Metallothionein, Alcohol Dehydrogenases, Glutathione, Polyols, Carotenoids and Retinoids, Cellular Injury and Repair, Diabetes

Research Programme: Metal ions in pure and applied biochemistry
The biochemical principles of life are based on both organic and inorganic chemistry. My laboratory focuses on the inorganic biochemical aspects, namely how the nutritionally essential transition metal ions maintain human life and how they support growth and development. Manganese, iron, copper, and zinc ions are constituents of thousands of proteins and function in enzymatic catalysis and protein structure. Transition metal ions regulate protein functions and proteins regulate their availability. For these activities, proteins employ dynamic coordination environments that link metal ion binding and protein conformational changes.

Cellular metal ion homeostasis requires multiple proteins for transport, sensing, chaperoning, and other functions in a network of tightly controlled interactions and with full integration into metabolism and signaling. The metal-regulatory proteins employ specific molecular mechanisms. One mechanism is the sulfur-ligand centered reactivity in zinc/thiolate coordination environments. Sulfur donors confer redox activity on the otherwise biologically redox-inert zinc ion. This coupling between zinc and redox metabolism provides a way of controlling zinc binding and protein functions.

Fundamental insights into the control of transition metal ion homeostasis will lead to an understanding of the pharmacological activity and toxic actions of metal ions, and aid in developing strategies for optimizing human health and for preventing, diagnosing, and treating human diseases. 

Key Grants

BBSRC  BB/K001442/1

Regulatory Roles of the Micronutrient Zinc in Phosphorylations (Wolfgang Maret, PI, Christer Hogstrand, Co-PI)

Our long term interests are the roles of zinc in biology, with the objective of understanding the homeostatic control of zinc in cellular time and space.  Zinc is essential for almost all physiological processes. It functions in about 3000 human proteins as a catalytic and structural cofactor.  In addition, it has regulatory functions.  The rationale for this research grant is that understanding these regulatory functions would demonstrate a new role of a major micronutrient in health and disease.  Our planned experiments focus on the molecular targets of the regulatory functions of zinc.  They are based on our discovery that picomolar concentrations of zinc(II) ions inhibit some protein tyrosine phosphatases.  Such remarkably strong inhibition suggests that zinc(II) ions are intracellular messengers that control these important enzymes.  


  • Wilson, M., Hogstrand, C., and Maret, W.  Picomolar concentrations of free zinc(II) ions regulate receptor protein tyrosine phosphatase beta activity.  J. Biol. Chem.  287:9322-9326; 2012.
  • Maret, W.  New perspectives of zinc coordination environments in proteins.  J. Inorg. Biochem.  111:110-116; 2012.
  • Maret, W.  Zinc biochemistry: From a single zinc enzyme to a key element of life.  Adv. Nutr. 4:82-91; 2013
  • Maret, W.  Inhibitory zinc sites in enzymes.  BioMetals 26:197-204; 2013

Full Publication List

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