The alkene monooxygenase from Xanthobacter Py2 is a binuclear non-haem iron protein closely related to toluene 4-monooxygenase

Ning Yi Zhou, Alistair Jenkins, Chan K.N. Chan Kwo Chion, David J. Leak

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

The genes encoding the six polypeptide components of the alkene monooxygenase from Xanthobacter Py2 have been sequenced. The predicted amino acid sequence of the first ORF shows homology with the iron binding subunits of binuclear non-haem iron containing monooxygenases including benzene monooxygenase, toluene 4-monooxygenase (> 60% sequence similarity) and methane monooxygenase (> 40% sequence similarity) and that the necessary sequence motifs associated with iron coordination are also present. Secondary structure prediction based on the amino acid sequence showed that the predominantly α-helical structure that surrounds the binuclear iron binding site was conserved allowing the sequence to be modelled on the coordinates of the methane monooxygenase α-subunit. Significant differences in the residues forming the hydrophobic cavity which forms the substrate binding site are discussed with reference to the differences in reaction specificity and stereospecificity of binuclear non-haem iron monooxygenases.

Original languageEnglish
Pages (from-to)181-185
Number of pages5
JournalFEBS Letters
Volume430
Issue number3
DOIs
Publication statusPublished - 3 Jul 1998

Keywords

  • Alkene monooxygenase
  • Epoxide
  • Methane monooxygenase
  • Non-heme iron
  • Toluene 4-monooxygenase
  • Xanthobacter

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

The alkene monooxygenase from Xanthobacter Py2 is a binuclear non-haem iron protein closely related to toluene 4-monooxygenase. / Zhou, Ning Yi; Jenkins, Alistair; Chan Kwo Chion, Chan K.N.; Leak, David J.

In: FEBS Letters, Vol. 430, No. 3, 03.07.1998, p. 181-185.

Research output: Contribution to journalArticle

Zhou, Ning Yi ; Jenkins, Alistair ; Chan Kwo Chion, Chan K.N. ; Leak, David J. / The alkene monooxygenase from Xanthobacter Py2 is a binuclear non-haem iron protein closely related to toluene 4-monooxygenase. In: FEBS Letters. 1998 ; Vol. 430, No. 3. pp. 181-185.
@article{89e1de8e58e840749e01c36c9ff906c5,
title = "The alkene monooxygenase from Xanthobacter Py2 is a binuclear non-haem iron protein closely related to toluene 4-monooxygenase",
abstract = "The genes encoding the six polypeptide components of the alkene monooxygenase from Xanthobacter Py2 have been sequenced. The predicted amino acid sequence of the first ORF shows homology with the iron binding subunits of binuclear non-haem iron containing monooxygenases including benzene monooxygenase, toluene 4-monooxygenase (> 60{\%} sequence similarity) and methane monooxygenase (> 40{\%} sequence similarity) and that the necessary sequence motifs associated with iron coordination are also present. Secondary structure prediction based on the amino acid sequence showed that the predominantly α-helical structure that surrounds the binuclear iron binding site was conserved allowing the sequence to be modelled on the coordinates of the methane monooxygenase α-subunit. Significant differences in the residues forming the hydrophobic cavity which forms the substrate binding site are discussed with reference to the differences in reaction specificity and stereospecificity of binuclear non-haem iron monooxygenases.",
keywords = "Alkene monooxygenase, Epoxide, Methane monooxygenase, Non-heme iron, Toluene 4-monooxygenase, Xanthobacter",
author = "Zhou, {Ning Yi} and Alistair Jenkins and {Chan Kwo Chion}, {Chan K.N.} and Leak, {David J.}",
year = "1998",
month = "7",
day = "3",
doi = "10.1016/S0014-5793(98)00653-X",
language = "English",
volume = "430",
pages = "181--185",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Wiley-Blackwell",
number = "3",

}

TY - JOUR

T1 - The alkene monooxygenase from Xanthobacter Py2 is a binuclear non-haem iron protein closely related to toluene 4-monooxygenase

AU - Zhou, Ning Yi

AU - Jenkins, Alistair

AU - Chan Kwo Chion, Chan K.N.

AU - Leak, David J.

PY - 1998/7/3

Y1 - 1998/7/3

N2 - The genes encoding the six polypeptide components of the alkene monooxygenase from Xanthobacter Py2 have been sequenced. The predicted amino acid sequence of the first ORF shows homology with the iron binding subunits of binuclear non-haem iron containing monooxygenases including benzene monooxygenase, toluene 4-monooxygenase (> 60% sequence similarity) and methane monooxygenase (> 40% sequence similarity) and that the necessary sequence motifs associated with iron coordination are also present. Secondary structure prediction based on the amino acid sequence showed that the predominantly α-helical structure that surrounds the binuclear iron binding site was conserved allowing the sequence to be modelled on the coordinates of the methane monooxygenase α-subunit. Significant differences in the residues forming the hydrophobic cavity which forms the substrate binding site are discussed with reference to the differences in reaction specificity and stereospecificity of binuclear non-haem iron monooxygenases.

AB - The genes encoding the six polypeptide components of the alkene monooxygenase from Xanthobacter Py2 have been sequenced. The predicted amino acid sequence of the first ORF shows homology with the iron binding subunits of binuclear non-haem iron containing monooxygenases including benzene monooxygenase, toluene 4-monooxygenase (> 60% sequence similarity) and methane monooxygenase (> 40% sequence similarity) and that the necessary sequence motifs associated with iron coordination are also present. Secondary structure prediction based on the amino acid sequence showed that the predominantly α-helical structure that surrounds the binuclear iron binding site was conserved allowing the sequence to be modelled on the coordinates of the methane monooxygenase α-subunit. Significant differences in the residues forming the hydrophobic cavity which forms the substrate binding site are discussed with reference to the differences in reaction specificity and stereospecificity of binuclear non-haem iron monooxygenases.

KW - Alkene monooxygenase

KW - Epoxide

KW - Methane monooxygenase

KW - Non-heme iron

KW - Toluene 4-monooxygenase

KW - Xanthobacter

UR - http://www.scopus.com/inward/record.url?scp=0032479368&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(98)00653-X

DO - 10.1016/S0014-5793(98)00653-X

M3 - Article

VL - 430

SP - 181

EP - 185

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 3

ER -