Oxidation of linoleyl alcohol by potato tuber lipoxygenase: Kinetics and positional, stereo, and geometrical (cis, trans) specificity of the reaction

I. A. Butovich, S. M. Luk'Yanova, C. Channa Reddy

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

The dioxygenation of linoleyl alcohol (LAL) by potato tuber lipoxygenase leads to formation of two positional isomeric products - 9- and 13- hydroperoxyoctadecadien-1-ols (Butovich, I. A., Luk'yanova, S. M., and Reddy, C. C. (1998) Biochem. Biophys. Res. Commun. 249, 344-349). In the present study, we examined the stereospecificity and double-bond conformation of primary dioxygenation products of LAL catalyzed by potato lipoxygenase. In contrast to the product profiles of linoleic acid oxidation by potato lipoxygenase, oxidation of LAL led to all possible positional (9- and 13-), stereo, and geometrical (cis,trans and all-trans) isomers in equimolar mixtures at 25°C. The reaction appears to proceed through an enzyme- catalyzed formation of a pentadiene carbon-centered radical followed by resonance stabilization of the radical and molecular oxygen insertion in an enzyme-dependent as well as an enzyme-independent pathway. A strict positional, stereo, and geometrical specificity of the dioxygenation products of LAL oxidation appears to be maintained when the reaction occurs at the active site of the enzyme. However, when the pentadiene carbon-centered radical of LAL is dissociated from the active site of the enzyme, it appears to be nonenzymatically transformed into a mixture of all possible positional and geometrical stereoisomers of primary dioxygenation products. The latter pathway was effectively blocked by the free radical scavenger 4-hydroxy- TEMPO, which substantially reduced the production of all-trans hydroperoxyoctadecadienols. In the presence of the scavenger, 9(S)- hydroperoxy-10E, 12Z-octadecadien-1-ol was the predominant LAL oxidation product, representing approximately 80% of the total conjugated dienes, with 13(S)-hydroxy-9Z, 11E-octadecadien-1-ol the expected product of reverse orientation of the substrate at the active site, accounting for approximately 10%. A similar pattern in oxidation of LAL was observed when the reactions were carried out at 0°C. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)65-77
Number of pages13
JournalArchives of Biochemistry and Biophysics
Volume378
Issue number1
DOIs
StatePublished - Jun 1 2000

Fingerprint

Lipoxygenase
Solanum tuberosum
Oxidation
Kinetics
Alkadienes
Enzymes
Catalytic Domain
Carbon
Free Radical Scavengers
Stereoisomerism
Molecular oxygen
Linoleic Acid
linoleyl alcohol
Isomers
Conformations
Reactive Oxygen Species
Stabilization
Substrates

Keywords

  • 4-hydroxy-TEMPO
  • Chirality
  • cis,trans isomerism
  • Free radical scavengers
  • Free radicals
  • Linoleyl alcohol
  • Potato tuber lipoxygenase
  • Stereoisomers

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Oxidation of linoleyl alcohol by potato tuber lipoxygenase : Kinetics and positional, stereo, and geometrical (cis, trans) specificity of the reaction. / Butovich, I. A.; Luk'Yanova, S. M.; Reddy, C. Channa.

In: Archives of Biochemistry and Biophysics, Vol. 378, No. 1, 01.06.2000, p. 65-77.

Research output: Contribution to journalArticle

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abstract = "The dioxygenation of linoleyl alcohol (LAL) by potato tuber lipoxygenase leads to formation of two positional isomeric products - 9- and 13- hydroperoxyoctadecadien-1-ols (Butovich, I. A., Luk'yanova, S. M., and Reddy, C. C. (1998) Biochem. Biophys. Res. Commun. 249, 344-349). In the present study, we examined the stereospecificity and double-bond conformation of primary dioxygenation products of LAL catalyzed by potato lipoxygenase. In contrast to the product profiles of linoleic acid oxidation by potato lipoxygenase, oxidation of LAL led to all possible positional (9- and 13-), stereo, and geometrical (cis,trans and all-trans) isomers in equimolar mixtures at 25°C. The reaction appears to proceed through an enzyme- catalyzed formation of a pentadiene carbon-centered radical followed by resonance stabilization of the radical and molecular oxygen insertion in an enzyme-dependent as well as an enzyme-independent pathway. A strict positional, stereo, and geometrical specificity of the dioxygenation products of LAL oxidation appears to be maintained when the reaction occurs at the active site of the enzyme. However, when the pentadiene carbon-centered radical of LAL is dissociated from the active site of the enzyme, it appears to be nonenzymatically transformed into a mixture of all possible positional and geometrical stereoisomers of primary dioxygenation products. The latter pathway was effectively blocked by the free radical scavenger 4-hydroxy- TEMPO, which substantially reduced the production of all-trans hydroperoxyoctadecadienols. In the presence of the scavenger, 9(S)- hydroperoxy-10E, 12Z-octadecadien-1-ol was the predominant LAL oxidation product, representing approximately 80{\%} of the total conjugated dienes, with 13(S)-hydroxy-9Z, 11E-octadecadien-1-ol the expected product of reverse orientation of the substrate at the active site, accounting for approximately 10{\%}. A similar pattern in oxidation of LAL was observed when the reactions were carried out at 0°C. (C) 2000 Academic Press.",
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PY - 2000/6/1

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N2 - The dioxygenation of linoleyl alcohol (LAL) by potato tuber lipoxygenase leads to formation of two positional isomeric products - 9- and 13- hydroperoxyoctadecadien-1-ols (Butovich, I. A., Luk'yanova, S. M., and Reddy, C. C. (1998) Biochem. Biophys. Res. Commun. 249, 344-349). In the present study, we examined the stereospecificity and double-bond conformation of primary dioxygenation products of LAL catalyzed by potato lipoxygenase. In contrast to the product profiles of linoleic acid oxidation by potato lipoxygenase, oxidation of LAL led to all possible positional (9- and 13-), stereo, and geometrical (cis,trans and all-trans) isomers in equimolar mixtures at 25°C. The reaction appears to proceed through an enzyme- catalyzed formation of a pentadiene carbon-centered radical followed by resonance stabilization of the radical and molecular oxygen insertion in an enzyme-dependent as well as an enzyme-independent pathway. A strict positional, stereo, and geometrical specificity of the dioxygenation products of LAL oxidation appears to be maintained when the reaction occurs at the active site of the enzyme. However, when the pentadiene carbon-centered radical of LAL is dissociated from the active site of the enzyme, it appears to be nonenzymatically transformed into a mixture of all possible positional and geometrical stereoisomers of primary dioxygenation products. The latter pathway was effectively blocked by the free radical scavenger 4-hydroxy- TEMPO, which substantially reduced the production of all-trans hydroperoxyoctadecadienols. In the presence of the scavenger, 9(S)- hydroperoxy-10E, 12Z-octadecadien-1-ol was the predominant LAL oxidation product, representing approximately 80% of the total conjugated dienes, with 13(S)-hydroxy-9Z, 11E-octadecadien-1-ol the expected product of reverse orientation of the substrate at the active site, accounting for approximately 10%. A similar pattern in oxidation of LAL was observed when the reactions were carried out at 0°C. (C) 2000 Academic Press.

AB - The dioxygenation of linoleyl alcohol (LAL) by potato tuber lipoxygenase leads to formation of two positional isomeric products - 9- and 13- hydroperoxyoctadecadien-1-ols (Butovich, I. A., Luk'yanova, S. M., and Reddy, C. C. (1998) Biochem. Biophys. Res. Commun. 249, 344-349). In the present study, we examined the stereospecificity and double-bond conformation of primary dioxygenation products of LAL catalyzed by potato lipoxygenase. In contrast to the product profiles of linoleic acid oxidation by potato lipoxygenase, oxidation of LAL led to all possible positional (9- and 13-), stereo, and geometrical (cis,trans and all-trans) isomers in equimolar mixtures at 25°C. The reaction appears to proceed through an enzyme- catalyzed formation of a pentadiene carbon-centered radical followed by resonance stabilization of the radical and molecular oxygen insertion in an enzyme-dependent as well as an enzyme-independent pathway. A strict positional, stereo, and geometrical specificity of the dioxygenation products of LAL oxidation appears to be maintained when the reaction occurs at the active site of the enzyme. However, when the pentadiene carbon-centered radical of LAL is dissociated from the active site of the enzyme, it appears to be nonenzymatically transformed into a mixture of all possible positional and geometrical stereoisomers of primary dioxygenation products. The latter pathway was effectively blocked by the free radical scavenger 4-hydroxy- TEMPO, which substantially reduced the production of all-trans hydroperoxyoctadecadienols. In the presence of the scavenger, 9(S)- hydroperoxy-10E, 12Z-octadecadien-1-ol was the predominant LAL oxidation product, representing approximately 80% of the total conjugated dienes, with 13(S)-hydroxy-9Z, 11E-octadecadien-1-ol the expected product of reverse orientation of the substrate at the active site, accounting for approximately 10%. A similar pattern in oxidation of LAL was observed when the reactions were carried out at 0°C. (C) 2000 Academic Press.

KW - 4-hydroxy-TEMPO

KW - Chirality

KW - cis,trans isomerism

KW - Free radical scavengers

KW - Free radicals

KW - Linoleyl alcohol

KW - Potato tuber lipoxygenase

KW - Stereoisomers

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