Noam Adir

Noam Adir

Structural Biology of Photosynthetic complexes, enzymes, stress related proteins, etc. Renewable energy from direct photosynthetic activity to hydrogen conversion.

The Technion Centre for Macromolecular Structure

Fig. 1. Crystal of Phycocyanin and it’s X-ray diffraction pattern to 1.25Å. Additional details on this system can be found in references #2, 5, 7, 8 and 9.

Research, located in the Schulich Faculty of Chemistry was established in 1995. Within this centre my students and I perform research aimed at obtaining an understanding of the structure/function relationship of biologically important molecules on the atomic level. Our major structural tool is X-ray crystallography, however we use many additional physical tools in our research. A deep understanding of complicated Biological systems can be obtained by the determination of the three dimensional structures of the molecules that participate in these system. In my lab, macromolecules are isolated and crystallized, and by using powerful X-ray beams, their three-dimensional structures are determined. Knowledge of the positions of all of the atoms, including solvent, prosthetic groups, chromophors, ligands, etc., can reveal the functional characteristics of the molecules (proteins and nucleic acids) and more intricate complexes.


The lab is heavily involved in studying different aspects of photosynthesis, on the molecular level. These include light harvesting complexes (especially centred on a huge complex called the Phycobilisome), electron transfer and accessory proteins involved in complex stability (See figure 1). These interests have led to attempts to directly use natural photosynthetic

Fig. 2. Schematic illustration of the use of Photosystem II in a biogenerator – for the production of molecular hydrogen gas by biological solar energy conversion. See reference #1 for details.

membranes and complexes for the direct production of energy.


We have patented a novel “bio-generator” that can create a useful electric current using water as the electron source. The device will be completely non-polluting and thus may serve as an excellent source of clean “green” energy from the sun (see figure 2).
The lab is also heavily involved in unravelling the mechanisms of difficult biochemical systems, including metal ion transport and enzymes.

The group has determined structures from ion transport systems, regulatory proteins and enzymes. The lab is collaborating with the Fishman group from Biotechnology on the determination of the first structures of a bacterial tyrosinase in its active form (Fig. 3: The active site of the enzyme Tyrosinase with bound ligands. Details can be found in references #3 and 9.). These are the first structures of an active enzyme.

Fig. 3. The active site of the enzyme Tyrosinase with bound ligands. Details can be found in references #3 and 9.

B. Sc. in Chemistry1984,Hebrew University in Jerusalem, Israel.
Ph. D. in Biochemistry 1990, Hebrew University in Jerusalem, Israel.
Postdoctoral research 1990-1995, Dept. of Physics, Univ. of California, San Diego,USA.
Joined the Schulich Faculty of Chemistry, Technion – Israel Institute of Technologyin 1995.

  1. Engineering of an alternative electron transfer path in Photosystem II. S. Larom, F. Salama, G. Schuster and N. Adir, Proceedings of the National Academy of Science, USA 107, 9650-9655 (2010).
  2. Identification of the molecular attributes required for aminoglycoside activity against Leishmania. M. Shalev, J. Kondo, D. Kopelyanskiy, C.L. Jaffe, N. Adir* and T. Baasov* (*corresponding authors). Proceedings of the National Academy of Science, USA 110(33):13333-13338 (2013).
  3. Structural studies show energy transfer within stabilized Phycobilisomes independent of the mode of rod-core assembly. L. David, M. Prado, A. A. Arteni, D.A. Elmlund, R. E. Blankenship and N. Adir. Biochimica et Biophysica Acta – Bioenergetics. 1837(3):385-389 (2014).
  4. Determination of tyrosinase substrate binding modes reveals mechanistic differences between type-3 copper proteins. M. Goldfeder, M. Kanteev, S. Isaschar-Ovdat, N. Adir* and A. Fishman*. Nature Communications, 5, 4505 (2014). (*corresponding authors).
  5. Crystal structure of the bovine COPI Delta subunit MHD domain at 2.15Å resolution. A. Lahav, H. Rozenberg, A. Parnis, D. Cassel* and N. Adir* Acta Crystallographica D71, 1328-1334(2015) (*corresponding authors).
  6. The Orange Carotenoid Protein burrows into the Phycobilisome to provide photoprotection. D. Harris, O. Tal, D. Jallet, A. Wilson, D. Kirilovsky and N. Adir. Proceedings of the National Academy of Sciences, USA 113(12), E1655-1662(2016).
  7. The amino acid sequence repertoire of the bacterial proteome and the occurrence of untranslatable sequences.S. Penias Navon, G. Kornberg, J. Chen, T. Schwartzman, A. Tsai, J.D. Puglisi* and N. Adir*. E.V. Puglisi, J.D. Puglisi* and N. Adir*. 113(26), 7166-7170. Proceedings of the National Academy of Sciences, USA(2016). (*corresponding authors).
  8. Hybrid Bio-Photo-Electro-Chemical Cells for Solar Water Splitting. R. I. Pinhassi, H. Dotan, A. Linkov, D. Kallmann, G. Saper, G. Schuster, N. Adir,and A. Rothschild. Nature Communications In Press (2016).

Name Email Room Phone
Avital Lahav 411 3716
Itay Goldshmid 411  3716
Shira Bar-Zvi 411 3716
Dvir Harris  411  3716
Dan Kallmann  411  3716
Gadi Saper 411 3716
Tarek Tarabeh 411 3716
Tunde Toth 411 3716