Dr. Norman Metanis earned his B.A. degree in Chemistry in 2000 (Cum Laude) from the Technion - Israel Institute of Technology, Haifa, Israel. He then moved to The Scripps Research Institute (TSRI), La Jolla, CA as a visiting student and spent one year in the laboratories of Prof. Ehud Keinan and Prof. Philip Dawson where he was trained in chemical protein synthesis. Upon returning to the Technion, he completed his M.A. degree in 2004 (Cum Laude). Then he moved back to TSRI where he worked with Prof. Ehud Keinan and Prof. Philip Dawson on a joint program between the Technion and TSRI. During his Ph.D. (2004-2008), Dr. Metanis was engaged in different projects including synthetic methodologies for peptide and protein chemistry and the chemical synthesis of the enzyme 4-oxalocrotonate tautomerase and analogs containing the non-coded amino acid citrulline instead of arginine in the active site. This work provided the first direct evidence that the role of a specific arginine residue in the enzyme active site was to provide electrostatic stabilization to the transition state of the catalyzed reaction. Then he focused on another important enzyme belonging to the thiol-disulfide oxidoreductase, glutaredoxin 3. He reported the first total chemical synthesis of this member of the thioredoxin family and analogs containing selenocysteine (Sec) substitutions at the active site cysteine (Cys) residues in the conserved CXXC motif. This work was the first one to provide the reduction potential of seleno-sulfide and diselenide bonds in proteins. Additionally, the diselenide mutant was found to be 10,000 fold faster than the wild-type, disulfide enzyme. These findings led to suggest a possible role for diselenide bonds in biological systems, which was confirmed one year after his publication. Dr. Metanis additionally developed novel ligation methods based on the unique reactivity of selenium in comparison to sulfur, which led to traceless ligation of cysteine peptides using selective deselenization.

Upon the completion of his Ph.D. in 2008, Dr. Metanis joined the group of Prof. Donald Hilvert at ETH Zurich and worked on oxidative protein folding using selenocysteine as a tool to manipulate oxidative folding in predictive and more productive routes. Here, he chemically synthesized a small protein bovine pancreatic trypsin inhibitor and analogs with Cys to Sec substitutions at multiple positions in the protein sequence. In one case, a non-native diselenide bond containing analog was found to fold to the native state faster, much more efficient and in different route than the wild-type protein.

In 2013, Dr. Metanis joined the Institute of Chemistry at the Hebrew University of Jerusalem as a Senior Lecturer (Assistant Professor). In 2018, Dr. Metanis was promoted to Associate Professor.