@misc{BenndorfHohmannSchmidtetal., author = {Benndorf, Christopher and Hohmann, Andrea and Schmidt, Peer and Eckert, Hellmut and Johrendt, Dirk and Sch{\"a}fer, Konrad and P{\"o}ttgen, Rainer}, title = {2D 31P Solid state NMR spectroscopy, electronic structure and thermochemistry of PbP7}, series = {Journal of Solid State Chemistry}, volume = {235}, journal = {Journal of Solid State Chemistry}, doi = {10.1016/j.jssc.2015.12.028}, pages = {139 -- 144}, abstract = {Phase pure polycrystalline PbP7 was prepared from the elements via a lead flux. Crystalline pieces with edge-lengths up to 1 mm were obtained. The assignment of the previously published 31P solid state NMR spectrum to the seven distinct crystallographic sites was accomplished by radio-frequency driven dipolar recoupling (RFDR) experiments. As commonly found in other solid polyphosphides there is no obvious correlation between the 31P chemical shift and structural parameters. PbP7 decomposes incongruently under release of phosphorus forming liquid lead as remainder. The thermal decomposition starts at T>550 K with a vapor pressure almost similar to that of red phosphorus. Electronic structure calculations reveal PbP7 as a semiconductor according to the Zintl description and clearly shows the stereo-active Pb-6s2 lone pairs in the electron localization function ELF.}, language = {en} } @misc{KuhnBenndorfRappetal., author = {Kuhn, Ramona and Benndorf, Dirk and Rapp, Erdmann and Reichl, Udo and Palese, Luigi Leonardo and Pollice, Alfieri}, title = {Metaproteome analysis of sewage sludge from membrane bioreactors}, series = {Proteomics}, volume = {11}, journal = {Proteomics}, number = {13}, issn = {1615-9861}, doi = {10.1002/pmic.201000590}, pages = {2738 -- 2744}, abstract = {Microbial dynamics and enzymatic activities of activated sludge processes are not completely understood yet. A better understanding about the biology is indispensable for further process optimization. Since proteins play a key role as catalysts in sludge processes, a protocol for protein extraction and analysis by 2-D PAGE was established. It is based on phenol extraction of alkaline extracts and on a subsequent precipitation with ammonium sulphate. 2-D protein patterns obtained from different sludges collected from membrane bioreactors showed - besides common spots - significant differences. Selected proteins were identified with nano- HPLC-ESI-MS/MS. All membrane biological reactor (MBR) sludge samples investigated in this study contained elastase 3A, which implies that this human serine protease is a significant constituent of municipal wastewater. Although the identification of proteins from ammonia-oxidizing bacterium Nitrosomonas europaea was expected, the detection of a protein with homology to the marine bacterium Saprospira grandis in MBR1 was surprising.}, language = {en} } @misc{RiedelCommichauBenndorfetal., author = {Riedel, Ramona and Commichau, Fabian M. and Benndorf, Dirk and Hertel, Robert and Holzer, Katharina and Mardoukhi, Mohammad Saba Yousef and Noack, Laura and Martienssen, Marion}, title = {Biodegradation of selected aminophosphonates by the bacterial isolate Ochrobactrum sp. BTU1}, series = {Microbial Research}, volume = {280}, journal = {Microbial Research}, issn = {0944-5013}, doi = {10.1016/j.micres.2024.127600}, pages = {1 -- 12}, abstract = {Aminophosphonates, like glyphosate (GS) or metal chelators such as ethylenediaminetetra(methylenephosphonic acid) (EDTMP), are released on a large scale worldwide. Here, we have characterized a bacterial strain capable of degrading synthetic aminophosphonates. The strain was isolated from LC/MS standard solution. Genome sequencing indicated that the strain belongs to the genus Ochrobactrum. Whole-genome classification using pyANI software to compute a pairwise ANI and other metrics between Brucella assemblies and Ochrobactrum contigs revealed that the bacterial strain is designated as Ochrobactrum sp. BTU1. Degradation batch tests with Ochrobactrum sp. BTU1 and the selected aminophosphonates GS, EDTMP, aminomethylphosphonic acid (AMPA), iminodi(methylene-phosphonic) (IDMP) and ethylaminobis(methylenephosphonic) acid (EABMP) showed that the strain can use all phosphonates as sole phosphorus source during phosphorus starvation. The highest growth rate was achieved with AMPA, while EDTMP and GS were least supportive for growth. Proteome analysis revealed that GS degradation is promoted by C-P lyase via the sarcosine pathway, i.e., initial cleavage at the C-P bond. We also identified C-P lyase to be responsible for degradation of EDTMP, EABMP, IDMP and AMPA. However, the identification of the metabolite ethylenediaminetri(methylenephosphonic acid) via LC/MS analysis in the test medium during EDTMP degradation indicates a different initial cleavage step as compared to GS. For EDTMP, it is evident that the initial cleavage occurs at the C-N bond. The detection of different key enzymes at regulated levels, form the bacterial proteoms during EDTMP exposure, further supports this finding.}, language = {en} }