Hydrogen-bonded dioxygen adduct of an iron porphyrin with an alkanethiolate ligand: An elaborate model of cytochrome P450

Mikiya Matsu-Ura, Fumito Tani, Shinya Nakayama, Nobuhumi Nakamura, Yoshinori Naruta

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

A stable dioxygen adduct is formed from a synthetic analogue for cytochrome P450, which has an alkanethiolate ligand and hydroxyl groups inside the molecular cavities (see scheme). The structure exhibits the first clear evidence for a hydrogen bond to bound dioxygen among thiolate- coordinated hemes, including the enzymes.

Original languageEnglish
Pages (from-to)1989-1991
Number of pages3
JournalAngewandte Chemie - International Edition
Volume39
Issue number11
DOIs
Publication statusPublished - Jun 2 2000

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Porphyrins
Cytochrome P-450 Enzyme System
Hydrogen
Hydrogen bonds
Iron
Enzymes
Ligands
Oxygen
Heme
Hydroxyl Radical

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)

Cite this

Hydrogen-bonded dioxygen adduct of an iron porphyrin with an alkanethiolate ligand : An elaborate model of cytochrome P450. / Matsu-Ura, Mikiya; Tani, Fumito; Nakayama, Shinya; Nakamura, Nobuhumi; Naruta, Yoshinori.

In: Angewandte Chemie - International Edition, Vol. 39, No. 11, 02.06.2000, p. 1989-1991.

Research output: Contribution to journalArticle

Matsu-Ura, Mikiya ; Tani, Fumito ; Nakayama, Shinya ; Nakamura, Nobuhumi ; Naruta, Yoshinori. / Hydrogen-bonded dioxygen adduct of an iron porphyrin with an alkanethiolate ligand : An elaborate model of cytochrome P450. In: Angewandte Chemie - International Edition. 2000 ; Vol. 39, No. 11. pp. 1989-1991.
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