Enhancement of peroxygenase activity of horse heart myoglobin by modification of heme-propionate side chains

Takashi Hayashi; Takaaki Matsuda; Yoshio Hisaeda

doi:10.1246/cl.2003.496

Enhancement of peroxygenase activity of horse heart myoglobin by modification of heme-propionate side chains

Takashi Hayashi, Takaaki Matsuda, Yoshio Hisaeda

Research output: Contribution to journal › Article › peer-review

16 Citations (Scopus)

Abstract

A myoglobin reconstituted with an artificially created heme having two benzene moieties bound at the terminal of two heme-propionates shows a clear enhancement in peroxygenase activity toward thioether and styrene oxidations due to the expanding hydrophobic heme pocket.

Original language	English
Pages (from-to)	496-497
Number of pages	2
Journal	Chemistry Letters
Volume	32
Issue number	6
DOIs	https://doi.org/10.1246/cl.2003.496
Publication status	Published - Jun 5 2003

All Science Journal Classification (ASJC) codes

Chemistry(all)

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10.1246/cl.2003.496

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title = "Enhancement of peroxygenase activity of horse heart myoglobin by modification of heme-propionate side chains",

abstract = "A myoglobin reconstituted with an artificially created heme having two benzene moieties bound at the terminal of two heme-propionates shows a clear enhancement in peroxygenase activity toward thioether and styrene oxidations due to the expanding hydrophobic heme pocket.",

author = "Takashi Hayashi and Takaaki Matsuda and Yoshio Hisaeda",

year = "2003",

month = jun,

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doi = "10.1246/cl.2003.496",

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journal = "Chemistry Letters",

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AU - Hayashi, Takashi

AU - Matsuda, Takaaki

AU - Hisaeda, Yoshio

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N2 - A myoglobin reconstituted with an artificially created heme having two benzene moieties bound at the terminal of two heme-propionates shows a clear enhancement in peroxygenase activity toward thioether and styrene oxidations due to the expanding hydrophobic heme pocket.

AB - A myoglobin reconstituted with an artificially created heme having two benzene moieties bound at the terminal of two heme-propionates shows a clear enhancement in peroxygenase activity toward thioether and styrene oxidations due to the expanding hydrophobic heme pocket.

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DO - 10.1246/cl.2003.496

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JO - Chemistry Letters

JF - Chemistry Letters

SN - 0366-7022

IS - 6

ER -

Enhancement of peroxygenase activity of horse heart myoglobin by modification of heme-propionate side chains

Abstract

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