Bennati, Marina

[["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Biological Chemistry"],["dc.bibliographiccitation.volume","386"],["dc.contributor.author","Hedderich, Reiner"],["dc.contributor.author","Hamann, Nils"],["dc.contributor.author","Bennati, Marina"],["dc.date.accessioned","2021-03-05T08:59:12Z"],["dc.date.available","2021-03-05T08:59:12Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.1515/BC.2005.112"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80398"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.eissn","1437-4315"],["dc.relation.issn","1431-6730"],["dc.title","Heterodisulfide reductase from methanogenic archaea: a new catalytic role for an iron-sulfur cluster"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["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.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Strohäker, Timo"],["dc.contributor.author","Jung, Byung Chul"],["dc.contributor.author","Liou, Shu-Hao"],["dc.contributor.author","Fernandez, Claudio O."],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Halliday, Glenda M."],["dc.contributor.author","Bennati, Marina"],["dc.contributor.author","Kim, Woojin S."],["dc.contributor.author","Lee, Seung-Jae"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2020-12-10T18:09:52Z"],["dc.date.available","2020-12-10T18:09:52Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1038/s41467-019-13564-w"],["dc.identifier.eissn","2041-1723"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17027"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73784"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","11144"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","Physical Chemistry Chemical Physics"],["dc.bibliographiccitation.lastpage","11149"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Enkin, Nikolay"],["dc.contributor.author","Liu, Guoquan"],["dc.contributor.author","Gimenez-Lopez, Maria del Carmen"],["dc.contributor.author","Porfyrakis, Kyriakos"],["dc.contributor.author","Tkach, Igor"],["dc.contributor.author","Bennati, Marina"],["dc.date.accessioned","2018-11-07T10:03:21Z"],["dc.date.available","2018-11-07T10:03:21Z"],["dc.date.issued","2015"],["dc.description.abstract","Overhauser DNP enhancements of toluene were measured at a magnetic field of 0.35 Tesla in a series of chemically functionalized nitroxide radicals. We observe that the enhancements increase systematically with polarizer size and rotational correlation time. Examination of the saturation factor of N-14 nitroxides by pulsed ELDOR spectroscopy led to a quantitative interpretation of the enhancements, for which the saturation factor increases up to almost unity due to enhanced nuclear (N-14) relaxation in the nitroxide radical. The observation has a direct impact on the choice of optimum DNP polarizers in liquids."],["dc.identifier.doi","10.1039/c5cp00935a"],["dc.identifier.isi","000353338800002"],["dc.identifier.pmid","25855020"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38442"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Royal Soc Chemistry"],["dc.relation.issn","1463-9084"],["dc.relation.issn","1463-9076"],["dc.title","A high saturation factor in Overhauser DNP with nitroxide derivatives: the role of N-14 nuclear spin relaxation"],["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","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.firstpage","411"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Reports on Progress in Physics"],["dc.bibliographiccitation.lastpage","448"],["dc.bibliographiccitation.volume","68"],["dc.contributor.author","Bennati, Marina"],["dc.contributor.author","Prisner, Thomas F."],["dc.date.accessioned","2021-03-05T08:58:50Z"],["dc.date.available","2021-03-05T08:58:50Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.1088/0034-4885/68/2/R05"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80269"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.eissn","1361-6633"],["dc.relation.issn","0034-4885"],["dc.title","New developments in high field electron paramagnetic resonance with applications in structural biology"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2170"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Chem. Sci."],["dc.bibliographiccitation.lastpage","2178"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Kasanmascheff, Müge"],["dc.contributor.author","Lee, Wankyu"],["dc.contributor.author","Nick, Thomas U."],["dc.contributor.author","Stubbe, JoAnne"],["dc.contributor.author","Bennati, Marina"],["dc.date.accessioned","2017-01-16T10:08:55Z"],["dc.date.accessioned","2021-10-27T13:12:30Z"],["dc.date.available","2017-01-16T10:08:55Z"],["dc.date.available","2021-10-27T13:12:30Z"],["dc.date.issued","2016"],["dc.description.abstract","Ribonucleotide reductases (RNRs) catalyze the conversion of ribonucleotides to deoxyribonucleotides in all living organisms. The catalytic cycle of E. coli RNR involves a long-range proton-coupled electron transfer (PCET) from a tyrosyl radical (Y122c) in subunit b2 to a cysteine (C439) in the active site of subunit a2, which subsequently initiates nucleotide reduction. This oxidation occurs over 35 °A and involves a specific pathway of redox active amino acids (Y1224[W48?]4Y356 in b2 to Y7314Y7304C439 in a2). The mechanisms of the PCET steps at the interface of the a2b2 complex remain puzzling due to a lack of structural information for this region. Recently, DFT calculations on the 3-aminotyrosyl radical (NH2Y731c)-a2 trapped by incubation of NH2Y731-a2/b2/CDP(substrate)/ATP(allosteric effector) suggested that R411-a2, a residue close to the a2b2 interface, interacts with NH2Y731c and accounts in part for its perturbed EPR parameters. To examine its role, we further modified NH2Y731-a2 with a R411A substitution. NH2Y731c/ R411A generated upon incubation of NH2Y731/R411A-a2/b2/CDP/ATP was investigated using multifrequency (34, 94 and 263 GHz) EPR, 34 GHz pulsed electron–electron double resonance (PELDOR) and electron–nuclear double resonance (ENDOR) spectroscopies. The data indicate a large conformational change in NH2Y731c/R411A relative to the NH2Y731c single mutant. Particularly, the inter-spin distance from NH2Y731c/R411A in one ab pair to Y122c in a second ab pair decreases by 3 °A in the presence of the R411A mutation. This is the first experimental evidence for the flexibility of pathway residue Y731-a2 in an a2b2 complex and suggests a role for R411 in the stacked Y731/Y730 conformation involved in collinear PCET. Furthermore, NH2Y731c/R411A serves as a probe of the PCET process across the subunit interface."],["dc.identifier.doi","10.1039/C5SC03460D"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14149"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91697"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.issn","2041-6539"],["dc.relation.issn","2041-6520"],["dc.relation.orgunit","Fakultät für Chemie"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","E. coli ribonucleotide; RNRs"],["dc.title","Radical transfer in E. coli ribonucleotide reductase: a NH2Y731/R411A-α mutant unmasks a new conformation of the pathway residue 731"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4480"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Physical Chemistry Chemical Physics"],["dc.bibliographiccitation.lastpage","4485"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Levien, Marcel"],["dc.contributor.author","Reinhard, Maik"],["dc.contributor.author","Hiller, Markus"],["dc.contributor.author","Tkach, Igor"],["dc.contributor.author","Bennati, Marina"],["dc.contributor.author","Orlando, Tomas"],["dc.date.accessioned","2021-04-14T08:28:34Z"],["dc.date.available","2021-04-14T08:28:34Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1039/d0cp05796g"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82649"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1463-9084"],["dc.relation.issn","1463-9076"],["dc.title","Spin density localization and accessibility of organic radicals affect liquid-state DNP efficiency"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","17"],["dc.bibliographiccitation.journal","Journal of Magnetic Resonance"],["dc.bibliographiccitation.lastpage","27"],["dc.bibliographiccitation.volume","303"],["dc.contributor.author","Tkach, Igor"],["dc.contributor.author","Bejenke, Isabel"],["dc.contributor.author","Hecker, Fabian"],["dc.contributor.author","Kehl, Annemarie"],["dc.contributor.author","Kasanmascheff, Müge"],["dc.contributor.author","Gromov, Igor"],["dc.contributor.author","Prisecaru, Ion"],["dc.contributor.author","Höfer, Peter"],["dc.contributor.author","Hiller, Markus"],["dc.contributor.author","Bennati, Marina"],["dc.date.accessioned","2020-12-10T14:25:14Z"],["dc.date.available","2020-12-10T14:25:14Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1016/j.jmr.2019.04.001"],["dc.identifier.issn","1090-7807"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/72491"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","1H high field electron-nuclear double resonance spectroscopy at 263 GHz/9.4 T"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]