Dr. Takahiro Hayashi

Dr. Takahiro Hayashi
ZHAW Life Sciences und Facility Management
Einsiedlerstrasse 31
8820 Wädenswil

+41 (0) 58 934 52 75
takahiro.hayashi@zhaw.ch

Persönliches Profil

Tätigkeit an der ZHAW als

Wissenschaftlicher Mitarbeiter

www.zhaw.ch/icbt/biokatalyse

Arbeits- und Forschungsschwerpunkte, Spezialkenntnisse

Protein Chemistry, Enzymology, Protein Engineering, Bioconjugation, Biospectroscopy, Crystallography, Biotransformation, Directed Evolution, HTP screening

Aus- und Fortbildung

6/2006-6/2011
Ph.D. in Biochemistry and Molecular Biology
School of Medicine, Oregon Health and Science University (Oregon, USA)
Advisor: Dr. Pierre Moënne-Loccoz

4/2004-3/2006
B.Sc. in Biotechnology
Department of Biotechnology and Life Science
Tokyo University of Agriculture and Technology (Tokyo, Japan)
Advisor: Dr. Hiroyuki Ohno

4/1999-3/2004
A.Sc. in Chemistry
Department of Chemistry and Biochemistry
Numazu National College of Technology (Shizuoka, Japan)
Advisor: Dr. Tatsuo Oshikawa

Beruflicher Werdegang

7/2014-3/2017
ETH Zürich (Zürich, Switzerland)
Department of Chemistry and Applied Biosciences
Direct advisor: Dr. Donald Hilvert

7/2011-7/2014
Kyoto University (Kyoto, Japan)
Department of Synthetic Chemistry and Biological Chemistry
Direct advisor: Dr. Itaru Hamachi

Publikationen vor Tätigkeit an der ZHAW

1. *Green A., *Hayashi T., Mittl P., and Hilvert D. “A chemically programmed proximal ligand enhances the catalytic properties of a heme enzyme” J. Am. Chem. Soc., 138, 11344-11352 (2016). Highlighted in JACS Spotlights and ACS Chemical Biology

2. Frey R., Hayashi T., and Hilvert D. “Enzyme-medicated polymerization inside engineered protein cages” Chem. Commun., 52, 10423-10426 (2016).

3. Hayashi T., Yasueda Y., Tamura T., Takaoka Y., and Hamachi I. “Analysis of cell-surface receptor dynamics through covalent labeling by catalyst-tethered antibody” J. Am. Chem. Soc., 137, 5372-5380 (2015)

4. Jiang Y., Hayashi T., Matsumura H., Do L.H., Majumdar A., Lippard S.J., Moënne-Loccoz P. “Light-induced N2O production from a non-heme iron-nitrosyl dimer” J. Am. Chem. Soc., 136, 12524-12527 (2014).

5. Matsumura H., Hayashi T., Chakraborty S., Lu Y., Moënne-Loccoz P. “The production of nitrous oxide (N2O) by the heme/nonheme diiron center of engineered myoglobins (FeBMbs) proceeds through a trans iron-nitrosyl dimer” J. Am. Chem. Soc., 136, 2420-2431 (2014).

6. Hayashi T., Sun Y., Tamura T., Kuwata K., Song Z., Takaoka Y., and Hamachi I. “Semisynthetic lectin-DMAP conjugates for labeling and profiling glycoproteins on live cell surfaces” J. Am. Chem. Soc., 135, 12252-12258 (2013).

7. Hayashi T.. and Hamachi I. “Traceless affinity labeling of endogenous proteins for functional analysis in living cells” Acc. Chem. Res., 45, 1460-1469 (2012).

8. Hayashi T., Caranto J.D., Matsumura H., Kurtz Jr. D.M., and Moënne-Loccoz P. “Vibrational analysis of mononitrosyl complexes in hemerythrin and flavodiiron proteins: relevance to detoxifying NO reductase” J. Am. Chem. Soc., 134, 6878-6884 (2012).

9. Hayashi T., Miner K.D., Yeung N., Lin Y-W., Lu Y., and Moënne-Loccoz P. “Spectroscopic characterization of mononitrosyl complexes in heme-nonheme diiron centers within the myoglobin scaffold (FeBMb): relevance to denitrifying NO reductase” Biochemistry, 50, 5939-5947 (2011).

10. Tran N.G., Kalyvas H., Skodje K.M., Hayashi T., Moënne-Loccoz P., Callan P.E., Shearer J., Kirschenbaum L.J., and Kim E. “Phenol nitration induced by an {Fe(NO)2}10 dinitrosyl iron complex” J. Am. Chem. Soc., 133, 1184-1187 (2011).

11. Kommineni S., Yukl E., Hayashi T., Delepine J., Geng H., Moënne-Loccoz P., and Nakano M.M. “Nitric oxide sensitive and insensitive interaction of Bacillus subtillis NsrR with a ResDE-controlled promoter” Mol. Microbiol., 78, 1280-1293 (2010).

12. Hayashi T., Caranto J.D., Wampler D.A., Kurtz Jr. D.M., and Moënne-Loccoz P. “Insights into the nitric oxide reductase mechanism of flavo-diiron proteins from a flavin-free enzyme” Biochemistry, 49, 7040-7049 (2010).

13. Do L.H., Hayashi T., Moënne-Loccoz P., and Lippard S.J. “Carboxylate as the protonation site in (peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins” J. Am. Chem. Soc., 132, 1273-1275 (2010).

14. Namuswe F., Hayashi T., Yunbo J., Kasper G.D., Narducci Sarjeant A.A., Moënne-Loccoz P., and Goldberg D.P. “Influence of the nitrogen donors on non-heme iron models of superoxide reductase: high-spin FeIII-OOR complexes” J. Am. Chem. Soc., 132, 157-167 (2010).

15. Friedle S., Kodanko J.J., Morys A.J., Hayashi T., Moënne-Loccoz P., and Lippard S.J. “Modeling the syn disposition of nitrogen donors in non-heme diiron enzymes. synthesis, characterization, and hydrogen peroxide reactivity of diiron(III) complexes with the syn N-donor ligand H2BPG2DEV” J. Am. Chem. Soc., 131, 14508-14520 (2009).

16. Jiang Y., Sivaramakrishnan S., Hayashi T., Cohen S., Moënne-Loccoz P., Shaik S., and Ortiz de Montellano P.R. “Calculated and experimental spin state of seleno cytochrome P450” Angew. Chem. Int. Ed., 48, 7193-7195 (2009).

17. Hayashi T., Lin M.T., Ganesan K., Chen Y., Fee J.A., Gennis R.B., and Moënne-Loccoz P. “Accommodation of two diatomic molecules in cytochrome bo3: insights into NO reductase activity in terminal oxidases” Biochemistry, 48, 883-890 (2009).

18. Alontaga A.Y., Rodriguez J.C., Schönbrunn E., Becker A., Funke T., Yukl E.T., Hayashi T., Stobaugh J., Moënne-Loccoz P., and Rivera M. “Structural characterization of the hemophore HasAp from Pseudomonas aeruginosa: NMR spectroscopy reveals protein-protein interactions between Holo-HasAp and hemoglobin” Biochemistry, 48, 96-109 (2009).

19. Namuswe F., Kasper G.D., Sarjeant A.A., Hayashi T., Krest C.M., Green M.T., Moënne-Loccoz P., and Goldberg D.P. “Rational tuning of the thiolate donor in model complexes of superoxide reductase: direct evidence for a trans influence in Fe(III)-OOR complexes” J. Am. Chem. Soc., 130, 14189-14200 (2008).

20. Tamada M., Ueda S., Hayashi T., and Ohno H. “Thermally stable polymer gel electrolytes composed of branched polyimide and ionic liquid/zwitterion mixture prepared by in situ polycondensation” Chem. Lett., 37, 86-87 (2008).

21. Hayashi T., Lin I.J., Chen Y., Fee J.A., and Moënne-Loccoz P. “Fourier transform infrared characterization of a CuB-nitrosyl complex in cytochrome ba3 from Thermus thermophilus: relevance to NO reductase activity in heme-copper terminal oxidases” J. Am. Chem. Soc., 129, 14952-14958 (2007).

22. Tamada M., Hayashi T., and Ohno H. “Improved solubilization of pyromellitic dianhydride and 4,4'-oxydianiline in ionic liquid by the addition of zwitterion and their polycondensation” Tetrahedron Letters, 48, 1553-1557 (2007).