Issue 26, 2014
From the journal:

Chemical Communications

H2O2-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin†

Yasunori Okamoto,a   Akira Onoda,*a   Hiroshi Sugimoto,b   Yu Takano,c   Shun Hirota,d   Donald M. Kurtz, Jr.,e   Yoshitsugu Shirob  and  Takashi Hayashi*a  

* Corresponding authors

a Department of Applied Chemistry, Graduate School of Engineering, Osaka University, Suita, Osaka 565-0871, Japan
E-mail: onoda@chem.eng.osaka-u.ac.jp, thayashi@chem.eng.osaka-u.ac.jp

b Biometal Science Laboratory, RIKEN SPring-8 Center, Sayo, Hyogo 679-5148, Japan

c Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan

d Graduate School of Materials Science, Nara Institute of Science and Technology, Ikoma 630-0192, Japan

e Department of Chemistry, University of Texas at San Antonio, San Antonio, Texas 78249, USA

Abstract

The O2-binding carboxylate-bridged diiron site in DcrH-Hr was engineered in an effort to perform the H2O2-dependent oxidation of external substrates. A His residue was introduced near the diiron site in place of a conserved residue, Ile119. The I119H variant promotes the oxidation of guaiacol and 1,4-cyclohexadiene upon addition of H2O2.

Graphical abstract: H2O2-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin

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Article information

DOI
https://doi.org/10.1039/C3CC48108E
Article type
Communication
Submitted
22 Oct 2013
Accepted
09 Dec 2013
First published
08 Jan 2014
This article is Open Access
Creative Commons BY license

Chem. Commun., 2014,50, 3421-3423

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H2O2-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin

Y. Okamoto, A. Onoda, H. Sugimoto, Y. Takano, S. Hirota, D. M. Kurtz, Y. Shiro and T. Hayashi, Chem. Commun., 2014, 50, 3421 DOI: 10.1039/C3CC48108E

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