Porcine leukocyte 5- and 12-lipoxygenases are iron enzymes

5- and 12-lipoxygenases isolated from porcine leukocytes were investigated by electron paramagnetic resonance at X-band and atomic absorption spectroscopy. For comparison potato 5-lipoxygenase was studied under identical experimental conditions. All three lipoxygenases contained between 0.7 and 0.9...

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Published inFEBS letters Vol. 287; no. 1; pp. 105 - 107
Main Authors Kroneck, Peter M.H., Cucurou, Christophe, Ullrich, Volker, Ueda, Natsuo, Suzuki, Hiroshi, Yoshimoto, Tanihiro, Matsuda, Satoshi, Yamamoto, Shozo
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 05.08.1991
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Summary:5- and 12-lipoxygenases isolated from porcine leukocytes were investigated by electron paramagnetic resonance at X-band and atomic absorption spectroscopy. For comparison potato 5-lipoxygenase was studied under identical experimental conditions. All three lipoxygenases contained between 0.7 and 0.9 Fe atoms/enzyme molecule. As isolated, both mammalian enzymes exhibited a characteristic EPR signal at low magnetic field with a maximum at g =5.20 indicative of a high-spin ferric iron center. The signal was not affected by the oxidants 12-hydroperoxyeicosatetraenoic acid or arachidonic acid, nor was it affected by the reductant nordihydroguaiaretic acid. In the case of the potato enzyme an intense EPR signal with resonances at g =7.50, 6.39 and 5.84 was only observed after addition of an oxidant, such as 9-hydroperoxyoctadecadienoic acid.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(91)80026-Y