Inorganic Chemistry Seminar: Professor Shinobu Itoh, Osaka University
About the Seminar
Modeling Studies of Mononuclear Copper Active Sites in Copper Monooxygenases
Copper complexes of the active-oxygen species such as superoxide, peroxide, and oxyl have been invoked as the key reactive intermediates not only in a variety of biological oxidation and oxygenation reactions but also in the copper-catalyzed oxidation reactions in synthetic organic chemistry and catalytic oxidation chemistry. In this seminar, our efforts to develop structural and functional models of mononuclear copper reaction centers of copper monooxygenases will be introduced. The topics are as follows.
1) Modeling ‘histidine brace’ of lytic polysaccharide monooxygenases (LPMO)
2) Controlling reactivity of cupric end-on superoxide complexes
3) Reactivity of tetrahedral copper(II)-methoxide complex
About the Speaker
Shinobu Itoh was born in Fukui prefecture in 1958. He received his Doctor’s degree in engineering under the supervision of Professor Toshio Agawa and Professor Yoshiki Ohshiro from Osaka University in 1986. Then, he joined Professor Ohshiro’s group at Osaka University as Assistant Professor, where he worked on the chemistry of coenzyme PQQ and cofactor TTQ as well as model compounds of galactose oxidase. During that period, he spent a year (1987-1988) as a postdoctoral fellow in Professor Teddy G. Traylor’s group at the University of California, San Diego, where he learned the chemistry of heme proteins. In 1994, he was promoted to Associate Professor and worked with Professor Shunichi Fukuzumi at Osaka University, when he started copper/dioxygen chemistry. He moved to Osaka City University as a full Professor in 1999, where he expanded his biomimetic chemistry to more biological system using real enzymes. He returned to Osaka University as a full Professor in 2008 and constructed a new laboratory for BioFunctional Chemistry (BFC). His current research interest is focused on chemical modeling and application of novel active sites in biological systems and development of biocatalysts based on rational modifications of metalloenzymes active sites.
Link to Prof. Itoh's CV.