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 languageEnglish
Pages (from-to)587-588
Number of pages2
JournalChemistry Letters
Issue number7
DOIs
Publication statusPublished - Jan 1 1997
Externally publishedYes

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methane monooxygenase
Oxygen
Enzymes
Iron

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

Cite this

Density functional study on possible peroxo form of non-heme diiron enzyme model. / Yoshizawa, Kazunari; Yokomichi, Yasunori; Shiota, Yoshihito; Ohta, Takehiro; Yamabe, Tokio.

In: Chemistry Letters, No. 7, 01.01.1997, p. 587-588.

Research output: Contribution to journal › Article

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, no. 7, pp. 587-588. https://doi.org/10.1246/cl.1997.587
Yoshizawa K, Yokomichi Y, Shiota Y, Ohta T, Yamabe T. Density functional study on possible peroxo form of non-heme diiron enzyme model. Chemistry Letters. 1997 Jan 1;(7):587-588. https://doi.org/10.1246/cl.1997.587
Yoshizawa, Kazunari ; Yokomichi, Yasunori ; Shiota, Yoshihito ; Ohta, Takehiro ; Yamabe, Tokio. / Density functional study on possible peroxo form of non-heme diiron enzyme model. In: Chemistry Letters. 1997 ; No. 7. pp. 587-588.
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