Density functional study on possible peroxo form of non-heme diiron enzyme model

Kazunari Yoshizawa; Yasunori Yokomichi; Yoshihito Shiota; Takehiro Ohta; Tokio Yamabe

doi:10.1246/cl.1997.587

Density functional study on possible peroxo form of non-heme diiron enzyme model

Kazunari Yoshizawa, Yasunori Yokomichi, Yoshihito Shiota, Takehiro Ohta, Tokio Yamabe

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

25 Citations (Scopus)

Abstract

Dioxygen binding to the active dinuclear iron site of methane monooxygenase (MMO) is theoretically analyzed with a density functional method. The μ-η¹:η¹-O₂ mode was calculated to be the most favorable binding mode of dioxygen to a supposed active site of MMO that contains two five-coordinate irons(II).

Original language	English
Pages (from-to)	587-588
Number of pages	2
Journal	Chemistry Letters
Issue number	7
DOIs	https://doi.org/10.1246/cl.1997.587
Publication status	Published - Jan 1 1997
Externally published	Yes

All Science Journal Classification (ASJC) codes

Chemistry(all)

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10.1246/cl.1997.587

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title = "Density functional study on possible peroxo form of non-heme diiron enzyme model",

abstract = "Dioxygen binding to the active dinuclear iron site of methane monooxygenase (MMO) is theoretically analyzed with a density functional method. The μ-η1:η1-O2 mode was calculated to be the most favorable binding mode of dioxygen to a supposed active site of MMO that contains two five-coordinate irons(II).",

author = "Kazunari Yoshizawa and Yasunori Yokomichi and Yoshihito Shiota and Takehiro Ohta and Tokio Yamabe",

year = "1997",

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doi = "10.1246/cl.1997.587",

language = "English",

pages = "587--588",

journal = "Chemistry Letters",

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T1 - Density functional study on possible peroxo form of non-heme diiron enzyme model

AU - Yoshizawa, Kazunari

AU - Yokomichi, Yasunori

AU - Shiota, Yoshihito

AU - Ohta, Takehiro

AU - Yamabe, Tokio

PY - 1997/1/1

Y1 - 1997/1/1

N2 - Dioxygen binding to the active dinuclear iron site of methane monooxygenase (MMO) is theoretically analyzed with a density functional method. The μ-η1:η1-O2 mode was calculated to be the most favorable binding mode of dioxygen to a supposed active site of MMO that contains two five-coordinate irons(II).

AB - Dioxygen binding to the active dinuclear iron site of methane monooxygenase (MMO) is theoretically analyzed with a density functional method. The μ-η1:η1-O2 mode was calculated to be the most favorable binding mode of dioxygen to a supposed active site of MMO that contains two five-coordinate irons(II).

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U2 - 10.1246/cl.1997.587

DO - 10.1246/cl.1997.587

M3 - Article

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JO - Chemistry Letters

JF - Chemistry Letters

SN - 0366-7022

IS - 7

ER -

Density functional study on possible peroxo form of non-heme diiron enzyme model

Abstract

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