@article{SelleKnorrLischeid2019, author = {Selle, Benny and Knorr, Klaus-Holger and Lischeid, Gunnar}, title = {Mobilisation and transport of dissolved organic carbon and iron in peat catchments-Insights from the Lehstenbach stream in Germany using generalised additive models}, series = {Hydrological processes}, volume = {33}, journal = {Hydrological processes}, number = {25}, publisher = {Wiley}, address = {Hoboken}, issn = {0885-6087}, doi = {10.1002/hyp.13552}, pages = {3213 -- 3225}, year = {2019}, abstract = {During the last decades, increasing exports of both dissolved organic carbon (DOC) and iron were observed from peat catchments in North America and Europe with potential consequences for water quality of streamwater and carbon storages of soils. As mobilisation and transport processes of DOC and iron in peat catchments are only partly understood, the purpose of this study was to elucidate these processes in an intensively monitored and studied system. Specifically, it was hypothesised that dissimilatory iron reduction in riparian peatland soils mobilises DOC initially adsorbed to iron minerals. During stormflow conditions, both DOC and iron will be transported into the stream network. Ferrous iron may be reoxidised at redox interfaces on its way to the stream, and subsequently, ferric iron could be transported together with DOC as complexes. To test these hypotheses, generalised additive models (GAMs) were applied to 14 years of weekly time series of discharge and concentrations of selected solutes measured in a German headwater stream called Lehstenbach. This stream drains a 4.19-km(2) forested mountain catchment; one third of which is covered by riparian peatland soils. We interpreted results of different types of GAM in the way that (a) iron reduction drove the mobilisation of DOC from peatland soils and that (b) both iron and DOC were transported as complexes after their joint mobilisation to and within the steam. It was speculated that low nitrate availability in the uppermost wetland soil layer, particularly during the growing season, promoted iron reduction and thus the mobilisation of DOC. However, the influence of nitrate on the DOC mobilisation remains relatively uncertain. This influence could be further investigated using methods similar to the GAM analysis conducted here for other catchments with long-term data as well as detailed measurements of the relevant species in riparian wetland soils and the adjacent stream network.}, language = {en} } @misc{SchwarzLossowKoppetal.2019, author = {Schwarz, Maria and Lossow, Kristina and Kopp, Johannes F. and Schwerdtle, Tanja and Kipp, Anna Patricia}, title = {Crosstalk of Nrf2 with the Trace Elements Selenium, Iron, Zinc, and Copper}, series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe}, journal = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe}, number = {1081}, issn = {1866-8372}, doi = {10.25932/publishup-47287}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-472873}, pages = {20}, year = {2019}, abstract = {Trace elements, like Cu, Zn, Fe, or Se, are important for the proper functioning of antioxidant enzymes. However, in excessive amounts, they can also act as pro-oxidants. Accordingly, trace elements influence redox-modulated signaling pathways, such as the Nrf2 pathway. Vice versa, Nrf2 target genes belong to the group of transport and metal binding proteins. In order to investigate whether Nrf2 directly regulates the systemic trace element status, we used mice to study the effect of a constitutive, whole-body Nrf2 knockout on the systemic status of Cu, Zn, Fe, and Se. As the loss of selenoproteins under Se-deprived conditions has been described to further enhance Nrf2 activity, we additionally analyzed the combination of Nrf2 knockout with feeding diets that provide either suboptimal, adequate, or supplemented amounts of Se. Experiments revealed that the Nrf2 knockout partially affected the trace element concentrations of Cu, Zn, Fe, or Se in the intestine, liver, and/or plasma. However, aside from Fe, the other three trace elements were only marginally modulated in an Nrf2-dependent manner. Selenium deficiency mainly resulted in increased plasma Zn levels. One putative mediator could be the metal regulatory transcription factor 1, which was up-regulated with an increasing Se supply and downregulated in Se-supplemented Nrf2 knockout mice.}, language = {en} } @article{SchwarzLossowKoppetal.2019, author = {Schwarz, Maria and Lossow, Kristina and Kopp, Johannes Florian and Schwerdtle, Tanja and Kipp, Anna Patricia}, title = {Crosstalk of Nrf2 with the Trace Elements Selenium, Iron, Zinc, and Copper}, series = {Nutrients}, volume = {11}, journal = {Nutrients}, number = {9}, publisher = {MDPI}, address = {Basel}, issn = {2072-6643}, doi = {10.3390/nu11092112}, pages = {18}, year = {2019}, abstract = {Trace elements, like Cu, Zn, Fe, or Se, are important for the proper functioning of antioxidant enzymes. However, in excessive amounts, they can also act as pro-oxidants. Accordingly, trace elements influence redox-modulated signaling pathways, such as the Nrf2 pathway. Vice versa, Nrf2 target genes belong to the group of transport and metal binding proteins. In order to investigate whether Nrf2 directly regulates the systemic trace element status, we used mice to study the effect of a constitutive, whole-body Nrf2 knockout on the systemic status of Cu, Zn, Fe, and Se. As the loss of selenoproteins under Se-deprived conditions has been described to further enhance Nrf2 activity, we additionally analyzed the combination of Nrf2 knockout with feeding diets that provide either suboptimal, adequate, or supplemented amounts of Se. Experiments revealed that the Nrf2 knockout partially affected the trace element concentrations of Cu, Zn, Fe, or Se in the intestine, liver, and/or plasma. However, aside from Fe, the other three trace elements were only marginally modulated in an Nrf2-dependent manner. Selenium deficiency mainly resulted in increased plasma Zn levels. One putative mediator could be the metal regulatory transcription factor 1, which was up-regulated with an increasing Se supply and downregulated in Se-supplemented Nrf2 knockout mice.}, language = {en} } @article{JayEckertVazdaCruzetal.2019, author = {Jay, Raphael Martin and Eckert, Sebastian and Vaz da Cruz, Vinicius and Fondell, Mattis and Mitzner, Rolf and F{\"o}hlisch, Alexander}, title = {Covalency-driven preservation of local charge densities in a metal-to-ligand charge-transfer excited iron photosensitizer}, series = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition}, volume = {58}, journal = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition}, number = {31}, publisher = {Wiley-VCH}, address = {Weinheim}, issn = {1433-7851}, doi = {10.1002/anie.201904761}, pages = {10742 -- 10746}, year = {2019}, abstract = {Charge-density rearrangements after metal-to-ligand charge-transfer excitation in an iron photosensitizer are investigated by R. M Jay, A. Fohlisch et al. in their Communication (DOI: 10.1002/anie.201904761). By using time-resolved X-ray absorption spectroscopy, surprising covalency-effects are revealed that inhibit charge-separation at the intra-molecular level. Furthermore, the underlying mechanism is proposed to be generally in effect for all commonly used photosensitizers in light-harvesting applications, which challenges the common perception of electronic charge-transfer.}, language = {en} } @article{NaolouLendleinNeffe2019, author = {Naolou, Toufik and Lendlein, Andreas and Neffe, Axel T.}, title = {Amides as non-polymerizable catalytic adjuncts enable the ring-opening polymerization of lactide with ferrous acetate under mild conditions}, series = {Frontiers in Chemistry}, volume = {7}, journal = {Frontiers in Chemistry}, publisher = {Frontiers Research Foundation}, address = {Lausanne}, issn = {2296-2646}, doi = {10.3389/fchem.2019.00346}, pages = {12}, year = {2019}, abstract = {Sn-based catalysts are effective in the ring-opening polymerization (ROP) but are toxic. Fe(OAc)(2) used as an alternative catalyst is suitable for the ROP of lactide only at higher temperatures (>170 degrees C), associated with racemization. In the ROP of ester and amide group containing morpholinediones with Fe(OAc)(2) to polydepsipeptides at 135 degrees C, ester bonds were selectively opened. Here, it was hypothesized that ROP of lactones is possible with Fe(OAc)(2) when amides are present in the reactions mixture as Fe-ligands could increase the solubility and activity of the metal catalytic center. The ROP of lactide in the melt with Fe(OAc)(2) is possible at temperatures as low as 105 degrees C, in the presence of N-ethylacetamide or N-rnethylbenzamide as non-polymerizable catalytic adjuncts (NPCA), with high conversion (up to 99 mol\%) and yield (up to 88 mol\%). Polydispersities of polylactide decreased with decreasing reaction temperature to <= 1.1. NMR as well as polarimetric studies showed that no racemization occurred at reaction temperatures <= 145 degrees C. A kinetic study demonstrated a living chain-growth mechanism. MALDI analysis revealed that no side reactions (e.g., cyclization) occurred, though transesterification took place.}, language = {en} } @phdthesis{Vranic2019, author = {Vranic, Marija}, title = {3D Structure of the biomarker hepcidin-25 in its native state}, doi = {10.25932/publishup-45929}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-459295}, school = {Universit{\"a}t Potsdam}, pages = {xii, 135}, year = {2019}, abstract = {Hepcidin-25 (Hep-25) plays a crucial role in the control of iron homeostasis. Since the dysfunction of the hepcidin pathway leads to multiple diseases as a result of iron imbalance, hepcidin represents a potential target for the diagnosis and treatment of disorders of iron metabolism. Despite intense research in the last decade targeted at developing a selective immunoassay for iron disorder diagnosis and treatment and better understanding the ferroportin-hepcidin interaction, questions remain. The key to resolving these underlying questions is acquiring exact knowledge of the 3D structure of native Hep-25. Since it was determined that the N-terminus, which is responsible for the bioactivity of Hep-25, contains a small Cu(II)-binding site known as the ATCUN motif, it was assumed that the Hep-25-Cu(II) complex is the native, bioactive form of the hepcidin. This structure has thus far not been elucidated in detail. Owing to the lack of structural information on metal-bound Hep-25, little is known about its possible biological role in iron metabolism. Therefore, this work is focused on structurally characterizing the metal-bound Hep-25 by NMR spectroscopy and molecular dynamics simulations. For the present work, a protocol was developed to prepare and purify properly folded Hep-25 in high quantities. In order to overcome the low solubility of Hep-25 at neutral pH, we introduced the C-terminal DEDEDE solubility tag. The metal binding was investigated through a series of NMR spectroscopic experiments to identify the most affected amino acids that mediate metal coordination. Based on the obtained NMR data, a structural calculation was performed in order to generate a model structure of the Hep-25-Ni(II) complex. The DEDEDE tag was excluded from the structural calculation due to a lack of NMR restraints. The dynamic nature and fast exchange of some of the amide protons with solvent reduced the overall number of NMR restraints needed for a high-quality structure. The NMR data revealed that the 20 Cterminal Hep-25 amino acids experienced no significant conformational changes, compared to published results, as a result of a pH change from pH 3 to pH 7 and metal binding. A 3D model of the Hep-25-Ni(II) complex was constructed from NMR data recorded for the hexapeptideNi(II) complex and Hep-25-DEDEDE-Ni(II) complex in combination with the fixed conformation of 19 C-terminal amino acids. The NMR data of the Hep-25-DEDEDE-Ni(II) complex indicates that the ATCUN motif moves independently from the rest of the structure. The 3D model structure of the metal-bound Hep-25 allows for future works to elucidate hepcidin's interaction with its receptor ferroportin and should serve as a starting point for the development of antibodies with improved selectivity.}, language = {en} }