Brodhun, Florian

[["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.artnumber","e64919"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","PloS one"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Brodhun, Florian"],["dc.contributor.author","Cristobal-Sarramian, Alvaro"],["dc.contributor.author","Zabel, Sebastian"],["dc.contributor.author","Newie, Julia"],["dc.contributor.author","Hamberg, Mats"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2019-07-09T11:40:02Z"],["dc.date.available","2019-07-09T11:40:02Z"],["dc.date.issued","2013"],["dc.description.abstract","Jasmonates constitute a family of lipid-derived signaling molecules that are abundant in higher plants. The biosynthetic pathway leading to plant jasmonates is initiated by 13-lipoxygenase-catalyzed oxygenation of α-linolenic acid into its 13-hydroperoxide derivative. A number of plant pathogenic fungi (e.g. Fusarium oxysporum) are also capable of producing jasmonates, however, by a yet unknown biosynthetic pathway. In a search for lipoxygenase in F. oxysporum, a reverse genetic approach was used and one of two from the genome predicted lipoxygenases (FoxLOX) was cloned. The enzyme was heterologously expressed in E. coli, purified via affinity chromatography, and its reaction mechanism characterized. FoxLOX was found to be a non-heme iron lipoxygenase, which oxidizes C18-polyunsaturated fatty acids to 13S-hydroperoxy derivatives by an antarafacial reaction mechanism where the bis-allylic hydrogen abstraction is the rate-limiting step. With α-linolenic acid as substrate FoxLOX was found to exhibit a multifunctional activity, because the hydroperoxy derivatives formed are further converted to dihydroxy-, keto-, and epoxy alcohol derivatives."],["dc.identifier.doi","10.1371/journal.pone.0064919"],["dc.identifier.fs","594675"],["dc.identifier.pmid","23741422"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10603"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58079"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.subject.mesh","Amino Acid Sequence"],["dc.subject.mesh","Fatty Acids"],["dc.subject.mesh","Fusarium"],["dc.subject.mesh","Hydrogen-Ion Concentration"],["dc.subject.mesh","Iron"],["dc.subject.mesh","Kinetics"],["dc.subject.mesh","Lipoxygenase"],["dc.subject.mesh","Mass Spectrometry"],["dc.subject.mesh","Molecular Sequence Data"],["dc.subject.mesh","Oxidation-Reduction"],["dc.subject.mesh","Phylogeny"],["dc.subject.mesh","Recombinant Fusion Proteins"],["dc.subject.mesh","Sequence Alignment"],["dc.title","An iron 13S-lipoxygenase with an α-linolenic acid specific hydroperoxidase activity from Fusarium oxysporum."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]