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

24 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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Yoshizawa, K., Yokomichi, Y., Shiota, Y., Ohta, T., & Yamabe, T. (1997). Density functional study on possible peroxo form of non-heme diiron enzyme model. Chemistry Letters, (7), 587-588. https://doi.org/10.1246/cl.1997.587

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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).",

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AU - Ohta, Takehiro

AU - Yamabe, Tokio

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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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