Yasunori Okamoto

Department of Chemistry, University of Basel

Contact

University of Basel


Department of Chemistry
Spitalstrasse 51
4056 Basel
Switzerland
Office phone +41 61 207 10 09
yasunori.okamoto(at)unibas.ch

Read more about the Ward-Group here.


About

Yasunori Okamoto studied chemistry for his bachelor, master and PhD at Osaka University, Japan, from 2005 to 2014. He worked on functional analysis and engineering of a diiron protein in the group of Prof. T. Hayashi from 2008 to 2014.

During his PhD, he was a research fellow of Japan Society for the Promotion of Science (DC1), a research student for the special collaboration program at the Institute for Molecular Science, National Institute of Natural Science, Japan (Prof. S. Aono group), and a visiting student at the University of Texas at San Antonio, US (Prof. D. M. Kurtz).

As a first posdoc, he joined the group of Prof. S. Aono at Okazaki Institute for Integrative Bioscience, National Institute of Natural Science, Japan, where he worked on structure-function relationship of proteins related to the iron acquisition in pathogenic bacteria until July 2014. In August 2014, he joined the group of Prof. T. R. Ward and started to work in the filed of artificial metalloenzymes within the framework of the NCCR Molecular Systems Engineering.

Articles

F. Schwizer, Y. Okamoto, T. Heinisch, Y. Gu, M. M. Pellizzoni, V. Lebrun, R. Reuter, V. Köhler, J. C. Lewis, T. R. WardArtificial Metalloenzymes: Reaction Scope and Optimization Strategies“ Chem. Rev. (2017). [Link]
Y. OkamotoT. R. WardCross-Regulation of an Artificial Metalloenzyme“ Angew. Chem. Int. Ed. (2017). [Link]
Y. OkamotoT. R. WardO. WengerFrom Photodriven Charge Accumulation to Fueling Enzyme Cascades in Molecular Factories“ Chimia 6, 395 (2016). [Link]
Y. Okamoto, V. Köhler, C. E. Paul, F. Hollmann, T. R. WardEfficient In Situ Regeneration of NADH Mimics by an Artificial Metalloenzyme“ ACS Catal. 6, 3553 (2016). [Link]
Y. Okamoto, V. Köhler, T. R. WardAn NAD(P)H-Dependent Artificial Transfer Hydrogenase for Multienzymatic Cascades“ J. Am. Chem. Soc. 138, 5781 (2016). [Link]