Oxidation of C18 Hydroxy‐Polyunsaturated Fatty Acids to Epoxide or Ketone by Catalase‐Related Hemoproteins Activated with Iodosylbenzene. Issue 7 (19th June 2017)

• Record Type: Journal Article
• Authors: Teder, Tarvi; Boeglin, William E.; Brash, Alan R.
• Is Part Of: Lipids. Volume 52:Issue 7(2017)
• Page Start: 587
• Page End: 597
• Publication Date: 2017-06-19
• Subjects: Fusarium -- Catalase -- Lipoxygenase -- Peroxidase -- HODE -- Iodosylbenzene; Lipids -- Periodicals; Lipids -- Periodicals; Lipiden; Lipides -- Périodiques; 547.77
• DOI: 10.1007/s11745-017-4271-0
• Languages: English
• ISSNs: 0024-4201

Abstract

Abstract: Small catalase‐related hemoproteins with a facility to react with fatty acid hydroperoxides were examined for their potential mono‐oxygenase activity when activated using iodosylbenzene. The proteins tested were a Fusarium graminearum 41 kD catalase hemoprotein (Fg‐cat, gene FGSG_02217), a Pseudomonas fluorescens Pfl01 catalase (37.5 kD, accession number WP_011333788.1), and a Mycobacterium avium ssp. paratuberculosis 33 kD catalase (gene MAP‐2744c). 13‐Hydroxy‐octadecenoic acids (which are normally unreactive) were selected as substrates because these enzymes react specifically with the corresponding 13 S ‐hydroperoxides (Pakhomova et al . 18:2559–2568, 5 ; Teder et al . 1862:706–715, 14 ). In the presence of iodosylbenzene Fg‐cat converted 13 S ‐hydroxy‐fatty acids to two products: the 15, 16‐double bond of 13 S ‐hydroxy α‐linolenic acid was oxidized stereospecifically to the 15 S, 16 R ‐ cis ‐epoxide or the 13‐hydroxyl was oxidized to the 13‐ketone. Products were identified by UV, HPLC, LC–MS, NMR and by comparison with authentic standards prepared for this study. The Pfl01‐cat displayed similar activity. MAP‐2744c oxidized 13 S ‐hydroxy‐linoleic acid to the 13‐ketone, and epoxidized the double bonds to form the 9, 10‐epoxy‐13‐hydroxy, 11, 12‐epoxy‐13‐hydroxy, and 9, 10‐epoxy‐13‐keto derivatives; equivalent transformations occurred with 9 S ‐hydroxy‐linoleic acid as substrate. In parallel incubations in the presence of iodosylbenzene, human catalase displayed no activity towards 13 S ‐hydroxy‐linoleic acid, as expected from the highly restricted access to its active site. The results indicated that with suitable transformation to Compound I, monooxygenase activity can be demonstrated by these catalase‐related hemoproteins with tyrosine as the proximal heme ligand.