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


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.

SUBMITTER: Okamoto Y 

PROVIDER: S-EPMC3947700 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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

Okamoto Yasunori Y   Onoda Akira A   Sugimoto Hiroshi H   Takano Yu Y   Hirota Shun S   Kurtz Donald M DM   Shiro Yoshitsugu Y   Hayashi Takashi T  

Chemical communications (Cambridge, England) 20140108 26


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. ...[more]

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