Feußner, Ivo

[["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","ChemInform"],["dc.bibliographiccitation.volume","41"],["dc.contributor.author","Goebel, Cornelia"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2021-12-08T12:29:47Z"],["dc.date.available","2021-12-08T12:29:47Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1002/chin.201005278"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/96209"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-476"],["dc.relation.eissn","1522-2667"],["dc.relation.issn","0931-7597"],["dc.rights.uri","http://doi.wiley.com/10.1002/tdm_license_1.1"],["dc.title","ChemInform Abstract: Methods for the Analysis of Oxylipins in Plants"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","819"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Plant Physiology"],["dc.bibliographiccitation.lastpage","839"],["dc.bibliographiccitation.volume","182"],["dc.contributor.author","Zienkiewicz, Agnieszka"],["dc.contributor.author","Zienkiewicz, Krzysztof"],["dc.contributor.author","Poliner, Eric"],["dc.contributor.author","Pulman, Jane A."],["dc.contributor.author","Du, Zhi-Yan"],["dc.contributor.author","Stefano, Giovanni"],["dc.contributor.author","Tsai, Chia-Hong"],["dc.contributor.author","Horn, Patrick"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Farre, Eva M."],["dc.contributor.author","Childs, Kevin L."],["dc.contributor.author","Brandizzi, Federica"],["dc.contributor.author","Benning, Christoph"],["dc.date.accessioned","2020-12-10T18:25:55Z"],["dc.date.available","2020-12-10T18:25:55Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1104/pp.19.00854"],["dc.identifier.eissn","1532-2548"],["dc.identifier.issn","0032-0889"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75876"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The Microalga Nannochloropsis during Transition from Quiescence to Autotrophy in Response to Nitrogen Availability"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9052"],["dc.bibliographiccitation.issue","23"],["dc.bibliographiccitation.journal","Journal of the American Chemical Society"],["dc.bibliographiccitation.lastpage","9062"],["dc.bibliographiccitation.volume","133"],["dc.contributor.author","Fielding, Alistair J."],["dc.contributor.author","Brodhun, Florian"],["dc.contributor.author","Koch, Christian"],["dc.contributor.author","Pievo, Roberta"],["dc.contributor.author","Denysenkov, Vasyl"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Bennati, Marina"],["dc.date.accessioned","2018-11-07T08:55:03Z"],["dc.date.available","2018-11-07T08:55:03Z"],["dc.date.issued","2011"],["dc.description.abstract","PpoA is a fungal dioxygenase that produces hydroxylated fatty acids involved in the regulation of the life cycle and secondary metabolism of Aspergillus nidulans. It was recently proposed that this novel enzyme employs two different heme domains to catalyze two separate reactions: within a heme peroxidase domain, linoleic acid is oxidized to (8R)-hydroperoxyoctadecadienoic acid [(8R)-HPODE]; in the second reaction step (8R)-HPODE is isomerized within a P450 heme thiolate domain to 5,8-dihydroxyoctadecadienoic acid. In the present study, pulsed EPR methods were applied to find spectroscopic evidence for the reaction mechanism, thought to involve paramagnetic intermediates. We observe EPR resonances of two distinct heme centers with g-values typical for Fe (III) S = 5/2 high-spin (HS) and Fe(III) S = 1/2 low-spin (LS) hemes. N-14 ENDOR spectroscopy on the S = 5/2 signal reveals resonances consistent with an axial histidine ligation. Reaction of PpoA with the substrate leads to the formation of an amino acid radical on the early millisecond time scale concomitant to a substantial reduction of the S = 5/2 heme signal. High-frequency EPR (95- and 180-GHz) unambiguously identifies the new radical as a tyrosyl, based on g-values and hyperfine couplings from spectral simulations. The radical displays enhanced T-1-spin-lattice relaxation due to the proximity of the heme centers. Further, EPR distance measurements revealed that the radical is distributed among the monomeric subunits of the tetrameric enzyme at a distance of approximately 5 nm. The identification of three active paramagnetic centers involved in the reaction of PpoA supports the previously proposed reaction mechanism based on radical chemistry."],["dc.description.sponsorship","DFG-IRTG [1422]; Max Planck Society"],["dc.identifier.doi","10.1021/ja202207t"],["dc.identifier.isi","000291667600049"],["dc.identifier.pmid","21548577"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22816"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0002-7863"],["dc.title","Multifrequency Electron Paramagnetic Resonance Characterization of PpoA, a CYP450 Fusion Protein that Catalyzes Fatty Acid Dioxygenation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","883"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","The Plant Journal"],["dc.bibliographiccitation.lastpage","896"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Stumpe, Michael"],["dc.contributor.author","Goebel, Cornelia"],["dc.contributor.author","Demchenko, Kirill N."],["dc.contributor.author","Hoffmann, Manuela"],["dc.contributor.author","Kloesgen, Ralf B."],["dc.contributor.author","Pawlowski, Katharina"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2018-11-07T09:23:37Z"],["dc.date.available","2018-11-07T09:23:37Z"],["dc.date.issued","2006"],["dc.description.abstract","Allene oxide synthase (AOS) enzymes are members of the cytochrome P450 enzyme family, sub-family CYP74. Here we describe the isolation of three cDNAs encoding AOS from potato (StAOS1-3). Based on sequence comparisons, they represent members of either the CYP74A (StAOS1 and 2) or the CYP74C (StAOS3) sub-families. StAOS3 is distinguished from the other two AOS isoforms in potato by its high substrate specificity for 9-hydroperoxides of linoleic and linolenic acid, compared with 13-hydroperoxides, which are only poor substrates. The highest activity was shown with (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid (9-HPODE) as a substrate. This hydroperoxide was metabolized in vitro to alpha- and gamma-ketols as well as to the cyclopentenone compound 10-oxo-11-phytoenoic acid. They represent hydrolysis products of the initial StAOS3 product 9,10-epoxyoctadecadienoic acid, an unstable allene oxide. By RNA gel hybridization blot analysis, StAOS3 was shown to be expressed in sprouting eyes, stolons, tubers and roots, but not in leaves. StAOS3 protein was found in all organs tested, but mainly in stems, stolons, sprouting eyes and tubers. As in vivo reaction products, the alpha-ketols derived from 9-hydroperoxides of linoleic and linolenic acid were only found in roots, tubers and sprouting eyes. Immunolocalization showed that StAOS3 was associated with amyloplasts and leucoplasts."],["dc.identifier.doi","10.1111/j.1365-313X.2006.02843.x"],["dc.identifier.isi","000240147100006"],["dc.identifier.pmid","16899083"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29625"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing"],["dc.relation.issn","0960-7412"],["dc.title","Identification of an allene oxide synthase (CYP74C) that leads to formation of alpha-ketols from 9-hydroperoxides of linoleic and linolenic acid in below-ground organs of potato"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Plant Science"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Yu, Dingyi"],["dc.contributor.author","Boughton, Berin A."],["dc.contributor.author","Hill, Camilla B."],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Roessner, Ute"],["dc.contributor.author","Rupasinghe, Thusitha W. T."],["dc.date.accessioned","2020-12-10T18:44:40Z"],["dc.date.available","2020-12-10T18:44:40Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.3389/fpls.2020.00001"],["dc.identifier.eissn","1664-462X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78551"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Insights Into Oxidized Lipid Modification in Barley Roots as an Adaptation Mechanism to Salinity Stress"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","437"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","European Journal of Plant Pathology"],["dc.bibliographiccitation.lastpage","442"],["dc.bibliographiccitation.volume","127"],["dc.contributor.author","Eschen-Lippold, Lennart"],["dc.contributor.author","Altmann, Simone"],["dc.contributor.author","Gebhardt, Christiane"],["dc.contributor.author","Goebel, Cornelia"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Rosahl, Sabine"],["dc.date.accessioned","2018-11-07T08:40:45Z"],["dc.date.available","2018-11-07T08:40:45Z"],["dc.date.issued","2010"],["dc.description.abstract","The role of 9- and 13-lipoxygenase-derived oxylipins for race-cultivar-specific resistance in potato was analyzed by expressing RNA interference constructs against oxylipin biosynthetic genes in transgenic potato plants carrying the resistance gene R1 against Phytophthora infestans. Down-regulation of 9-lipoxygenase expression resulted in highly reduced levels of 9-hydroxyoctadecatrienoic acid after treatment with the pathogen-associated molecular pattern Pep-13. However, neither 9-lipoxygenase nor 9-divinyl ether synthase RNAi plants exhibited alterations in their resistance to P. infestans. Similarly, successful down-regulation of transcript accumulation of the 13-lipoxygenase pathway genes encoding allene oxide cyclase, 12-oxophytodienoic acid reductase 3 and the jasmonic acid receptor coronatine-insensitive 1 resulted in highly reduced levels of jasmonic acid after Pep-13 treatment. Race-cultivar-specific resistance, however, was not lost in these plants. Our results suggest that neither 9-lipoxygenase-derived oxylipins nor jasmonic acid are required for R-gene-mediated resistance in potato. Importantly, in tobacco, the silencing of 9-lipoxygenase expression was previously demonstrated to suppress race-cultivar-specific resistance. Thus, we conclude a differential requirement of oxylipins for R-gene-mediated resistance in different solanaceous plants."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB 648, TP A4]"],["dc.identifier.doi","10.1007/s10658-010-9621-1"],["dc.identifier.isi","000279302100001"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19306"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0929-1873"],["dc.title","Oxylipins are not required for R gene-mediated resistance in potato"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","517"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Eukaryotic Cell"],["dc.bibliographiccitation.lastpage","526"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Du, Xiaoli"],["dc.contributor.author","Herrfurth, Cornelia"],["dc.contributor.author","Gottlieb, Thomas"],["dc.contributor.author","Kawelke, Steffen"],["dc.contributor.author","Feussner, Kristin"],["dc.contributor.author","Ruehling, Harald"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Maniak, Markus"],["dc.date.accessioned","2018-11-07T09:41:57Z"],["dc.date.available","2018-11-07T09:41:57Z"],["dc.date.issued","2014"],["dc.description.abstract","Triacylglycerol (TAG), the common energy storage molecule, is formed from diacylglycerol and a coenzyme A-activated fatty acid by the action of an acyl coenzyme A: diacylglycerol acyltransferase (DGAT). In order to conduct this step, most organisms rely on more than one enzyme. The two main candidates in Dictyostelium discoideum are Dgat1 and Dgat2. We show, by creating single and double knockout mutants, that the endoplasmic reticulum (ER)-localized Dgat1 enzyme provides the predominant activity, whereas the lipid droplet constituent Dgat2 contributes less activity. This situation may be opposite from what is seen in mammalian cells. Dictyostelium Dgat2 is specialized for the synthesis of TAG, as is the mammalian enzyme. In contrast, mammalian DGAT1 is more promiscuous regarding its substrates, producing diacylglycerol, retinyl esters, and waxes in addition to TAG. The Dictyostelium Dgat1, however, produces TAG, wax esters, and, most interestingly, also neutral ether lipids, which represent a significant constituent of lipid droplets. Ether lipids had also been found in mammalian lipid droplets, but the role of DGAT1 in their synthesis was unknown. The ability to form TAG through either Dgat1 or Dgat2 activity is essential for Dictyostelium to grow on bacteria, its natural food substrate."],["dc.identifier.doi","10.1128/EC.00327-13"],["dc.identifier.isi","000333903000008"],["dc.identifier.pmid","24562909"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33845"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","1535-9786"],["dc.relation.issn","1535-9778"],["dc.title","Dictyostelium discoideum Dgat2 Can Substitute for the Essential Function of Dgat1 in Triglyceride Production but Not in Ether Lipid Synthesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","553"],["dc.bibliographiccitation.journal","Biochemical Journal"],["dc.bibliographiccitation.lastpage","565"],["dc.bibliographiccitation.volume","425"],["dc.contributor.author","Brodhun, Florian"],["dc.contributor.author","Schneider, Stefan"],["dc.contributor.author","Goebel, Cornelia"],["dc.contributor.author","Hornung, Ellen"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2018-11-07T08:46:02Z"],["dc.date.available","2018-11-07T08:46:02Z"],["dc.date.issued","2010"],["dc.description.abstract","In Asperyillus nidulans Ppos [psi (precocious sexual inducer)-producing oxygenases] are required for the production of so-called psi factors, compounds that control the balance between the sexual and asexual life cycle of the fungus. The genome of A. nidulans harbours three different ppo genes: ppoA, ppoB and ppoC. For all three enzymes two different haem-containing domains are predicted: a fatty acid haem peroxidase/dioxygenase domain in the N-terminal region and a P450 haem-thiolate domain in the C-terminal region. Whereas PpoA was shown to use both haem domains for its bifunctional catalytic activity (linoleic acid 8-dioxygenation and 8-hydroperoxide isomerization), We found that PpoC apparently only harbours a functional haem peroxidase/dioxygenase domain. Consequently, we observed that PpoC catalyses mainly the dioxygenation of linoleic acid (18:2(Delta 9Z,12Z)), yielding 10-HPODE (10-hydroperoxyoctadecadienoic acid). No isomerase activity was detected. Additionally, 10-HPODE was converted at lower rates into 10-KODE (10-keto-octadecadienoic acid) and 10-HODE (10-hydroxyoctadecadienoic acid). In parallel, decomposition of 10-HPODE into 10-ODA (10-octadecynoic acid) and volatile C-8 alcohols that are, among other things, responsible for the characteristic mushroom flavour. Besides these principle differences we also found that PpoA and PpoC can convert 8-HPODE and 10-HPODE into the respective epoxy alcohols: 12,13-epoxy-8-HOME (where HOME is hydroxyoctadecenoic acid) and 12,13-epoxy-10-HOME. By using site-directed mutagenesis we demonstrated that both enzymes share a similar mechanism for the oxidation of 18:2(Delta 9Z,12Z); they both use a conserved tyrosine residue for catalysis and the directed oxygenation at the C-8 and C-10 is most likely controlled by conserved valine/leucine residues in the dioxygenase domain."],["dc.description.sponsorship","German Research Foundation [1422]"],["dc.identifier.doi","10.1042/BJ20091096"],["dc.identifier.isi","000275099500009"],["dc.identifier.pmid","19878096"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20594"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Portland Press Ltd"],["dc.relation.issn","0264-6021"],["dc.title","PpoC from Aspergillus nidulans is a fusion protein with only one active haem"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","335"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Lipids"],["dc.bibliographiccitation.lastpage","347"],["dc.bibliographiccitation.volume","51"],["dc.contributor.author","Newie, Julia"],["dc.contributor.author","Kasanmascheff, Muege"],["dc.contributor.author","Bennati, Marina"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2018-11-07T10:17:04Z"],["dc.date.available","2018-11-07T10:17:04Z"],["dc.date.issued","2016"],["dc.description.abstract","Lipoxygenases (LOX) catalyze the regio- and stereospecific insertion of dioxygen into polyunsaturated fatty acids. While the catalytic metal of LOX is typically a non-heme iron, some fungal LOX contain manganese as catalytic metal (MnLOX). In general, LOX insert dioxygen at C9 or C13 of linoleic acid leading to the formation of conjugated hydroperoxides. MnLOX (EC 1.13.11.45), however, catalyze the oxygen insertion also at C11, resulting in bis-allylic hydroperoxides. Interestingly, the iron-containing CspLOX2 (EC 1.13.11.B6) from Cyanothece PCC8801 also produces bis-allylic hydroperoxides. What role the catalytic metal plays and how this unusual reaction is catalyzed by either MnLOX or CspLOX2 is not understood. Our findings suggest that only iron is the catalytically active metal in CspLOX2. The enzyme loses its catalytic activity almost completely when iron is substituted with manganese, suggesting that the catalytic metal is not interchangeable. Using kinetic and spectroscopic approaches, we further found that first a mixture of bis-allylic and conjugated hydroperoxy products is formed. This is followed by the isomerization of the bis-allylic product to conjugated products at a slower rate. These results suggest that MnLOX and CspLOX2 share a very similar reaction mechanism and that LOX with a Fe or Mn cofactor have the potential to form bis-allylic products. Therefore, steric factors are probably responsible for this unusual specificity. As CspLOX2 is the LOX with the highest proportion of the bis-allylic product known so far, it will be an ideal candidate for further structural analysis to understand the molecular basis of the formation of bisallylic hydroperoxides."],["dc.identifier.doi","10.1007/s11745-016-4127-z"],["dc.identifier.isi","000375329700007"],["dc.identifier.pmid","26832735"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41159"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Heidelberg"],["dc.relation.issn","1558-9307"],["dc.relation.issn","0024-4201"],["dc.title","Kinetics of Bis-Allylic Hydroperoxide Synthesis in the Iron-Containing Lipoxygenase 2 from Cyanothece and the Effects of Manganese Substitution"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1800271"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Molecular Nutrition & Food Research"],["dc.bibliographiccitation.volume","62"],["dc.contributor.author","Pignitter, Marc"],["dc.contributor.author","Lindenmeier, Michael"],["dc.contributor.author","Andersen, Gaby"],["dc.contributor.author","Herrfurth, Cornelia"],["dc.contributor.author","Beermann, Christopher"],["dc.contributor.author","Schmitt, Joachim J."],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Fulda, Martin"],["dc.contributor.author","Somoza, Veronika"],["dc.date.accessioned","2021-06-01T10:47:04Z"],["dc.date.available","2021-06-01T10:47:04Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1002/mnfr.201800271"],["dc.identifier.eissn","1613-4133"],["dc.identifier.issn","1613-4125"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85466"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1613-4133"],["dc.relation.issn","1613-4125"],["dc.title","Effect of 1‐ and 2‐Month High‐Dose Alpha‐Linolenic Acid Treatment on 13 C‐Labeled Alpha‐Linolenic Acid Incorporation and Conversion in Healthy Subjects"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]