Brodhun, Florian

[["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","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","1449"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids"],["dc.bibliographiccitation.lastpage","1457"],["dc.bibliographiccitation.volume","1831"],["dc.contributor.author","Koch, Christian"],["dc.contributor.author","Tria, Giancarlo"],["dc.contributor.author","Fielding, Alistair J."],["dc.contributor.author","Brodhun, Florian"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Svergun, Dmitri I."],["dc.contributor.author","Bennati, Marina"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2018-11-07T09:20:44Z"],["dc.date.available","2018-11-07T09:20:44Z"],["dc.date.issued","2013"],["dc.description.abstract","In plants and mammals, oxylipins may be synthesized via multi step processes that consist of dioxygenation and isomerization of the intermediately formed hydroperoxy fatty acid. These processes are typically catalyzed by two distinct enzyme classes: dioxygenases and cytochrome P450 enzymes. In ascomycetes biosynthesis of oxylipins may proceed by a similar two-step pathway. An important difference, however, is that both enzymatic activities may be combined in a single bifunctional enzyme. These types of enzymes are named Psi-factor producing oxygenases (Ppo). Here, the spatial organization of the two domains of PpoA from Aspergillus nidulans was analyzed by small-angle X-ray scattering and the obtained data show that the enzyme exhibits a relatively flat trimeric shape. Atomic structures of the single domains were obtained by template-based structure prediction and docked into the enzyme envelope of the low resolution structure obtained by SAXS. EPR-based distance measurements between the tyrosyl radicals formed in the activated dioxygenase domain of the enzyme supported the trimeric structure obtained from SAXS and the previous assignment of Tyr374 as radical-site in PpoA. Furthermore, two phenylalanine residues in the cytochrome P450 domain were shown to modulate the specificity of hydroperoxy fatty acid rearrangement. (C) 2013 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbalip.2013.06.003"],["dc.identifier.isi","000323588100003"],["dc.identifier.pmid","23797010"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28946"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","1388-1981"],["dc.title","A structural model of PpoA derived from SAXS-analysis-Implications for substrate conversion"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e0167627"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Eng, Felipe"],["dc.contributor.author","Haroth, Sven"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Meldau, Dorothea"],["dc.contributor.author","Rekhter, Dmitrij"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Brodhun, Florian"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2018-11-07T10:05:11Z"],["dc.date.available","2018-11-07T10:05:11Z"],["dc.date.issued","2016"],["dc.description.abstract","Jasmonic acid is a plant hormone that can be produced by the fungus Lasiodiplodia theobromae via submerged fermentation. From a biotechnological perspective jasmonic acid is a valuable feedstock as its derivatives serve as important ingredients in different cosmetic products and in the future it may be used for pharmaceutical applications. The objective of this work was to improve the production of jasmonic acid by L. theobromae strain 2334. We observed that jasmonic acid formation is dependent on the culture volume. Moreover, cultures grown in medium containing potassium nitrate as nitrogen source produced higher amounts of jasmonic acid than analogous cultures supplemented with ammonium nitrate. When cultivated under optimal conditions for jasmonic acid production, L. theobromae secreted several secondary metabolites known from plants into the medium. Among those we found 3-oxo-2-(pent-2-enyI)-cyclopentane-1-butanoic acid (OPC-4) and hydroxy-jasmonic acid derivatives, respectively, suggesting that fungal jasmonate metabolism may involve similar reaction steps as that of plants. To characterize fungal growth and jasmonic acid-formation, we established a mathematical model describing both processes. This model may form the basis of industrial upscaling attempts. Importantly, it showed that jasmonic acid-formation is not associated to fungal growth. Therefore, this finding suggests that jasmonic acid, despite its enormous amount being produced upon fungal development, serves merely as secondary metabolite."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.1371/journal.pone.0167627"],["dc.identifier.isi","000389482700213"],["dc.identifier.pmid","27907207"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14001"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38855"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Optimized Jasmonic Acid Production by Lasiodiplodia theobromae Reveals Formation of Valuable Plant Secondary Metabolites"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","26"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","ChemistryOpen"],["dc.bibliographiccitation.lastpage","32"],["dc.bibliographiccitation.volume","1"],["dc.contributor.author","Fehr, Friederike"],["dc.contributor.author","Nadler, Andre"],["dc.contributor.author","Brodhun, Florian"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2018-11-07T09:14:10Z"],["dc.date.available","2018-11-07T09:14:10Z"],["dc.date.issued","2012"],["dc.description.abstract","Total synthesis of proteins can be challenging despite assembling techniques, such as native chemical ligation (NCL) and expressed protein ligation (EPL). Especially, the combination of recombinant protein expression and chemically addressable solid-phase peptide synthesis (SPPS) is well suited for the redesign of native protein structures. Incorporation of analytical probes and artificial amino acids into full-length natural protein domains, such as the sequence-specific DNA binding zinc-finger motifs, are of interest combining selective DNA recognition and artificial function. The semi-synthesis of the natural 90 amino acid long sequence of the zinc-finger domain of Zif268 is described including various chemically modified constructs. Our approach offers the possibility to exchange any amino acid within the third zinc finger. The realized modifications of the natural sequence include point mutations, attachment of a fluorophore, and the exchange of amino acids at different positions in the zinc finger by artificial amino acids to create additional metal binding sites. The individual constructs were analyzed by circular dichroism (CD) spectroscopy with respect to the integrity of the zinc-finger fold and DNA binding."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft (DFG) [IRTG 1422]"],["dc.identifier.doi","10.1002/open.201100002"],["dc.identifier.isi","000328606600005"],["dc.identifier.pmid","24551489"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8371"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27345"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","2191-1363"],["dc.rights","CC BY-NC 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/3.0"],["dc.title","Semi-Synthesis and Analysis of Chemically Modified Zif268 Zinc-Finger Domains"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e0159875"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Bruckhoff, Viktoria"],["dc.contributor.author","Haroth, Sven"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Koenig, Stefanie"],["dc.contributor.author","Brodhun, Florian"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2018-11-07T10:11:29Z"],["dc.date.available","2018-11-07T10:11:29Z"],["dc.date.issued","2016"],["dc.description.abstract","Over the past decades much research focused on the biosynthesis of the plant hormone jasmonyl-isoleucine (JA-Ile). While many details about its biosynthetic pathway as well about its physiological function are established nowadays, knowledge about its catabolic fate is still scarce. Only recently, the hormonal inactivation mechanisms became a stronger research focus. Two major pathways have been proposed to inactivate JA-Ile: i) The cleavage of the jasmonyl-residue from the isoleucine moiety, a reaction that is catalyzed by specific amidohydrolases, or ii), the sequential oxidation of the omega-end of the pentenyl side-chain. This reaction is catalyzed by specific members of the cytochrome P450 (CYP) subfamily CYP94: CYP94B1, CYP94B3 and CYP94C1. In the present study, we further investigated the oxidative fate of JA-Ile by expanding the analysis on Arabidopsis thaliana mutants, lacking only one (cyp94b1, cyp94b2, cyp94b3, cyp94c1), two (cyp94b1xcyp94b2, cyp94b1xcyp94b3, cyp94b2xcyp94b3), three (cyp94b1xcyp94b2xcyp94b3) or even four (cyp94b1xcyp94b2x-cyp94b3xcyp94c1) CYP94 functionalities. The results obtained in the present study show that CYP94B1, CYP94B2, CYP94B3 and CYP94C1 are responsible for catalyzing the sequential omega-oxidation of JA-Ile in a semi-redundant manner. While CYP94B-enzymes preferentially hydroxylate JA-Ile to 12-hydroxy-JA-Ile, CYP94C1 catalyzes primarily the subsequent oxidation, yielding 12-carboxy-JA-Ile. In addition, data obtained from investigating the triple and quadruple mutants let us hypothesize that a direct oxidation of unconjugated JA to 12-hydroxy-JA is possible in planta. Using a non-targeted metabolite fingerprinting analysis, we identified unconjugated 12-carboxy-JA as novel jasmonate derivative in floral tissues. Using the same approach, we could show that deletion of CYP94-genes might not only affect JA-homeostasis but also other signaling pathways. Deletion of CYP94B1, for example, led to accumulation of metabolites that may be characteristic for plant stress responses like systemic acquired resistance. Evaluation of the in vivo function of the different CYP94-enzymes on the JA-sensitivity demonstrated that particularly CYP94B-enzymes might play an essential role for JA-response, whereas CYP94C1 might only be of minor importance."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.1371/journal.pone.0159875"],["dc.identifier.isi","000381515600059"],["dc.identifier.pmid","27459369"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13504"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40053"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Functional Characterization of CYP94-Genes and Identification of a Novel Jasmonate Catabolite in Flowers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1251"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PLANT PHYSIOLOGY"],["dc.bibliographiccitation.lastpage","1266"],["dc.bibliographiccitation.volume","160"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Brodhun, Florian"],["dc.contributor.author","Sauer, Kristin"],["dc.contributor.author","Herrfurth, Cornelia"],["dc.contributor.author","Hamberg, Mats"],["dc.contributor.author","Brinkmann, Jens"],["dc.contributor.author","Scholz, Julia"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:48:22Z"],["dc.date.available","2017-09-07T11:48:22Z"],["dc.date.issued","2012"],["dc.description.abstract","In plants, oxylipins regulate developmental processes and defense responses. The first specific step in the biosynthesis of the cyclopentanone class of oxylipins is catalyzed by allene oxide cyclase (AOC) that forms cis(+)-12-oxo-phytodienoic acid. The moss Physcomitrella patens has two AOCs (PpAOC1 and PpAOC2) with different substrate specificities for C-18- and C-20-derived substrates, respectively. To better understand AOC's catalytic mechanism and to elucidate the structural properties that explain the differences in substrate specificity, we solved and analyzed the crystal structures of 36 monomers of both apo and ligand complexes of PpAOC1 and PpAOC2. From these data, we propose the following intermediates in AOC catalysis: (1) a resting state of the apo enzyme with a closed conformation, (2) a first shallow binding mode, followed by (3) a tight binding of the substrate accompanied by conformational changes in the binding pocket, and (4) initiation of the catalytic cycle by opening of the epoxide ring. As expected, the substrate dihydro analog cis-12,13S-epoxy-9Z,15Z-octadecadienoic acid did not cyclize in the presence of PpAOC1; however, when bound to the enzyme, it underwent isomerization into the corresponding trans-epoxide. By comparing complex structures of the C-18 substrate analog with in silico modeling of the C-20 substrate analog bound to the enzyme allowed us to identify three major molecular determinants responsible for the different substrate specificities (i.e. larger active site diameter, an elongated cavity of PpAOC2, and two nonidentical residues at the entrance of the active site)."],["dc.identifier.doi","10.1104/pp.112.205138"],["dc.identifier.gro","3142446"],["dc.identifier.isi","000310584200009"],["dc.identifier.pmid","22987885"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8374"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0032-0889"],["dc.title","Crystal Structures of Physcomitrella patens AOC1 and AOC2: Insights into the Enzyme Mechanism and Differences in Substrate Specificity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1047"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","FEBS Journal"],["dc.bibliographiccitation.lastpage","1063"],["dc.bibliographiccitation.volume","278"],["dc.contributor.author","Brodhun, Florian"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2018-11-07T08:57:42Z"],["dc.date.available","2018-11-07T08:57:42Z"],["dc.date.issued","2011"],["dc.description.abstract","In nearly every living organism, metabolites derived from lipid peroxidation, the so-called oxylipins, are involved in regulating developmental processes as well as environmental responses. Among these bioactive lipids, the mammalian and plant oxylipins are the best characterized, and much information about their physiological role and biosynthetic pathways has accumulated during recent years. Although the occurrence of oxylipins and enzymes involved in their biosynthesis has been studied for nearly three decades, knowledge about fungal oxylipins is still scarce as compared with the situation in plants and mammals. However, the research performed so far has shown that the structural diversity of oxylipins produced by fungi is high and, furthermore, that the enzymes involved in oxylipin metabolism are diverse and often exhibit unusual catalytic activities. The aim of this review is to present a synopsis of the oxylipins identified so far in fungi and the enzymes involved in their biosynthesis."],["dc.description.sponsorship","German Research Foundation"],["dc.identifier.doi","10.1111/j.1742-4658.2011.08027.x"],["dc.identifier.isi","000288560600007"],["dc.identifier.pmid","21281447"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23456"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1742-464X"],["dc.title","Oxylipins in fungi"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1594"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","FEBS Journal"],["dc.bibliographiccitation.lastpage","1606"],["dc.bibliographiccitation.volume","279"],["dc.contributor.author","Koch, Christian"],["dc.contributor.author","Fielding, Alistair J."],["dc.contributor.author","Brodhun, Florian"],["dc.contributor.author","Bennati, Marina"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2018-11-07T09:10:52Z"],["dc.date.available","2018-11-07T09:10:52Z"],["dc.date.issued","2012"],["dc.description.abstract","Psi factor producing oxygenases (Ppos) are fusion proteins consisting of a peroxidase-like functionality in the N-terminus and a P450-fold in the C-terminal part of the polypeptide chain. It was shown that they are responsible for the production of oxidized fatty acids that play a pivotal role in the control of fungal colonization of plant and mammalian hosts. The similarity of the primary structure of the single domains to various host-derived oxylipin-forming enzymes and functional conservation of these enzymatic activities was the basis for prediction of the 3D conformations of the single domains of a prototype Ppo enzyme. We were able to predict a putative substrate binding pocket in the N-terminal domain of the enzyme and support this finding by site-directed mutagenesis. With the proposed substrate binding mode all known determinants of oxygen insertion are in a reasonable spatial arrangement for catalysis. Additionally, we could identify an arginine and show its involvement in substrate binding by kinetic analysis of the respective variant. While substrate position in the dioxygenase domain is well defined, our results indicate that the substrate binding to the P450 domain is rather unconstrained. Nevertheless an asparagine residue within the I-helix is shown to be involved in catalysis and promotes a shortcut of the typical P450 reaction cycle. Taken together, the results presented here exemplify that fatty acids are oxidized in all kingdoms of life by structural and functional highly conserved enzymes."],["dc.identifier.doi","10.1111/j.1742-4658.2011.08352.x"],["dc.identifier.isi","000302995500008"],["dc.identifier.pmid","21920024"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26594"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1742-464X"],["dc.title","Linoleic acid positioning in psi factor producing oxygenase A, a fusion protein with an atypical cytochrome P450 activity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","177"],["dc.bibliographiccitation.journal","BMC Plant Biology"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Meyer, Danilo"],["dc.contributor.author","Herrfurth, Cornelia"],["dc.contributor.author","Brodhun, Florian"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2018-11-07T09:17:38Z"],["dc.date.available","2018-11-07T09:17:38Z"],["dc.date.issued","2013"],["dc.description.abstract","Background: Oilseed germination is characterized by the degradation of storage lipids. It may proceed either via the direct action of a triacylglycerol lipase, or in certain plant species via a specific lipid body 13-lipoxygenase. For the involvement of a lipoxygenase previous results suggested that the hydroxy-or oxo-group that is being introduced into the fatty acid backbone by this lipoxygenase forms a barrier to continuous beta-oxidation. Results: This study shows however that a complete degradation of oxygenated fatty acids is possible by isolated cucumber and sunflower glyoxysomes. Interestingly, degradation is accompanied by the formation of saturated short chain acyl-CoAs with chain length between 4 and 12 carbon atoms lacking the hydroxy-or oxo-diene system of the oxygenated fatty acid substrate. The presence of these CoA esters suggests the involvement of a specific reduction of the diene system at a chain length of 12 carbon atoms including conversion of the hydroxy-group at C7. Conclusions: To our knowledge this metabolic pathway has not been described for the degradation of polyunsaturated fatty acids so far. It may represent a new principle to degrade oxygenated fatty acid derivatives formed by lipoxygenases or chemical oxidation initiated by reactive oxygen species."],["dc.description.sponsorship","Deutsche Forschungs Gemeinschaft [FE 446/4]"],["dc.identifier.doi","10.1186/1471-2229-13-177"],["dc.identifier.isi","000329069200001"],["dc.identifier.pmid","24207097"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10049"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28212"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biomed Central Ltd"],["dc.relation.issn","1471-2229"],["dc.rights","CC BY 2.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.0"],["dc.title","Degradation of lipoxygenase-derived oxylipins by glyoxysomes from sunflower and cucumber cotyledons"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]